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Synthyra 5

P08495

MGLIVQKFGGTSVGSVEKIQNAANRAIAEKQKGHQVVVVVSAMGKSTDELVSLAKAISDQPSKREMDMLLATGEQVTISLLSMALQEKGYDAVSYTGWQAGIRTEAIHGNARITDIDTSVLADQLEKGKIVIVAGFQGMTEDCEITTLGRGGSDTTAVALAAALKADKCDIYTDVPGVFTTDPRYVKSARKLEGISYDEMLELANLGAGVLHPRAVEFAKNYQVPLEVRSSTETEAGTLIEEESSMEQNLIVRGIAFEDQITRVTIYGLTSGLTTLSTIFTTLAKRNINVDIIIQTQAEDKTGISFSVKTEDADQTVAVLEEYKDALEFEKIETESKLAKVSIVGSGMVSNPGVAAEMFAVLAQKNILIKMVSTSEIKVSTVVSENDMVKAVESLHDAFELSKHPSAV

Function: Catalyzes the phosphorylation of the beta-carboxyl group of aspartic acid with ATP to yield 4-phospho-L-aspartate, which is involved in the branched biosynthetic pathway leading to the biosynthesis of amino acids threonine, isoleucine and methionine. Catalytic Activity: ATP + L-aspartate = 4-phospho-L-aspartate + ADP Sequence Mass (Da): 43808 Sequence Length: 408 Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 1/4. EC: 2.7.2.4

P94417

MKVVKFGGSSLASGAQLDKVFHIVTSDPARKAVVVSAPGKHYAEDTKVTDLLIACAEQYLATGSAPELAEAVVERYALIANELQLGQSIIEKIRDDLFTLLEGDKSNPEQYLDAVKASGEDNNAKLIAAYFRYKGVKAEYVNPKDAGLFVTNEPGNAQVLPESYQNLYRLRERDGLIIFPGFFGFSKDGDVITFSRSGSDITGSILANGLQADLYENFTDVDAVYSVNPSFVENPKEISELTYREMRELSYAGFSVFHDEALIPAFRAGIPVQIKNTNNPSAEGTRVVSKRDNTNGPVVGIASDTGFCSIYISKYLMNREIGFGRRALQILEEHGLTYEHVPSGIDDMTIILRQGQMDAATERSVIKRIEEDLHADEVIVEHHLALIMVVGEAMRHNVGTTARAAKALSEAQVNIEMINQGSSEVSMMFGVKEAEERKAVQALYQEFFAGVLIS

Function: Catalyzes the phosphorylation of the beta-carboxyl group of aspartic acid with ATP to yield 4-phospho-L-aspartate, which is involved in the branched biosynthetic pathway leading to the biosynthesis of amino acids threonine, isoleucine and methionine. Catalytic Activity: ATP + L-aspartate = 4-phospho-L-aspartate + ADP Sequence Mass (Da): 49825 Sequence Length: 454 Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 1/4. EC: 2.7.2.4

P08660

MSEIVVSKFGGTSVADFDAMNRSADIVLSDANVRLVVLSASAGITNLLVALAEGLEPGERFEKLDAIRNIQFAILERLRYPNVIREEIERLLENITVLAEAAALATSPALTDELVSHGELMSTLLFVEILRERDVQAQWFDVRKVMRTNDRFGRAEPDIAALAELAALQLLPRLNEGLVITQGFIGSENKGRTTTLGRGGSDYTAALLAEALHASRVDIWTDVPGIYTTDPRVVSAAKRIDEIAFAEAAEMATFGAKVLHPATLLPAVRSDIPVFVGSSKDPRAGGTLVCNKTENPPLFRALALRRNQTLLTLHSLNMLHSRGFLAEVFGILARHNISVDLITTSEVSVALTLDTTGSTSTGDTLLTQSLLMELSALCRVEVEEGLALVALIGNDLSKACGVGKEVFGVLEPFNIRMICYGASSHNLCFLVPGEDAEQVVQKLHSNLFE

Catalytic Activity: ATP + L-aspartate = 4-phospho-L-aspartate + ADP Sequence Mass (Da): 48532 Sequence Length: 449 Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 1/4. EC: 2.7.2.4

O88845

MRGAGPSPRHSPRALRPDPGPAMSFFRRKVKGKEQEKTLDVKSTKASVAVHSPQKSTKNHALLEAAGPSHVAINAISANMDSFSSSRTATLKKQPSHMEAAHFGDLGRSCLDYQTQETKSSLSKTLEQVLRDTVVLPYFLQFMELRRMEHLVKFWLEAESFHSTTWSRIRAHSLNTVKQSSLAEPVSPSKRHETPASSVTEALDRRLGDSSSAPLLVTQSEGTDLSSRTQNPQNHLLLSQEGHSARSLHREVARTGSHQIPTDSQDSSSRLAVGSRNSCSSPLRELSEKLMKSIEQDAVNTFTKYISPDAAKPIPITEAMRNDIIAKICGEDGQVDPNCFVLAQAVVFSAMEQEHFSEFLRSHHFCKYQIEVLTSGTVYLADILFCESALFYFSEYMEKEDAVNILQFWLAADNFQSQLAAKKGQYDGQEAQNDAMILYDKYFSLQATHPLGFDDVVRLEIESNICREGGPLPNCFTTPLRQAWTTMEKVFLPGFLSSNLYYKYLNDLIHSVRGDEFLGGNVSLAAHGSVCLPEESHSGGSDGSTAQSSVKKASIKILKNFDEAIIVDAASLDPESLYQRTYAGKMSFGRVSDLGQFIRESEPEPDVKKSKGFMFSQAMKKWVQGNTDEAQEELAWKIAKMIVSDVMQQAHHDQPLEKSTKL

Function: Differentially targeted protein that binds to type I and II regulatory subunits of protein kinase A and anchors them to the mitochondria or the plasma membrane. Although the physiological relevance between PKA and AKAPS with mitochondria is not fully understood, one idea is that BAD, a proapoptotic member, is phosphorylated and inactivated by mitochondria-anchored PKA. It cannot be excluded too that it may facilitate PKA as well as G protein signal transduction, by acting as an adapter for assembling multiprotein complexes. With its RGS domain, it could lead to the interaction to G-alpha proteins, providing a link between the signaling machinery and the downstream kinase. Sequence Mass (Da): 73632 Sequence Length: 662 Domain: RII-alpha binding site, predicted to form an amphipathic helix, could participate in protein-protein interactions with a complementary surface on the R-subunit dimer. Subcellular Location: Mitochondrion

O43687

MGQLCCFPFSRDEGKISELESSSSAVLQRYSKDIPSWSSGEKNGGEPDDAELVRLSKRLVENAVLKAVQQYLEETQNKNKPGEGSSVKTEAADQNGNDNENNRK

Function: Targets the cAMP-dependent protein kinase (PKA) to the plasma membrane, and permits functional coupling to the L-type calcium channel. The membrane-associated form reduces epithelial sodium channel (ENaC) activity, whereas the free cytoplasmic form may negatively regulate ENaC channel feedback inhibition by intracellular sodium. Location Topology: Lipid-anchor Sequence Mass (Da): 11465 Sequence Length: 104 Subcellular Location: Lateral cell membrane

O55074

MGQLCCFPFARDEGKICEKDRREPEDAELVRLSKRLVENAVLKAVQQYLEETQNKKQPGEGNSTKAEEGDRNGDGSDNNRK

Function: Targets the cAMP-dependent protein kinase (PKA) to the plasma membrane, and permits functional coupling to the L-type calcium channel. The membrane-associated form reduces epithelial sodium channel (ENaC) activity, whereas the free cytoplasmic form may negatively regulate ENaC channel feedback inhibition by intracellular sodium (By similarity). Location Topology: Lipid-anchor Sequence Mass (Da): 9169 Sequence Length: 81 Subcellular Location: Lateral cell membrane

Q5ZJJ5

MNPFWSMSAASGRKRPEADEKTLSGELRTSPPRASAKKQLPSVPKNAVPVTKPASPAMSSQSTNGTHASYGPFYLEYSLLAEFTLVVKQKLPGVYVQPSYRSALMWFGVIFIRHGLYQDGVFKFTVYIPDNYPDGDCPRLVFDLPVFHPLVDPLSGELDVKRAFAKWRRNHNHIWQVLMYARRVFYKIDTTSPLNPEAAVLYEKDIQLFKSKVVDSVKLCSSHLFDQPKIEDPYAIVFSPWNPAIHDEAREKMLTQKKKPEDQHCKSMHVSGLSWVKPGSVQPFSKEEKTMPT

Function: May function to promote vesicle trafficking and/or fusion. May also regulate apoptosis (By similarity). Location Topology: Peripheral membrane protein Sequence Mass (Da): 33304 Sequence Length: 293 Subcellular Location: Cytoplasm

Q9H8T0

MNPFWSMSTSSVRKRSEGEEKTLTGDVKTSPPRTAPKKQLPSIPKNALPITKPTSPAPAAQSTNGTHASYGPFYLEYSLLAEFTLVVKQKLPGVYVQPSYRSALMWFGVIFIRHGLYQDGVFKFTVYIPDNYPDGDCPRLVFDIPVFHPLVDPTSGELDVKRAFAKWRRNHNHIWQVLMYARRVFYKIDTASPLNPEAAVLYEKDIQLFKSKVVDSVKVCTARLFDQPKIEDPYAISFSPWNPSVHDEAREKMLTQKKPEEQHNKSVHVAGLSWVKPGSVQPFSKEEKTVAT

Function: Component of the FTS/Hook/FHIP complex (FHF complex) . The FHF complex may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting complex (the HOPS complex). Regulates apoptosis by enhancing phosphorylation and activation of AKT1. Increases release of TNFSF6 via the AKT1/GSK3B/NFATC1 signaling cascade. FHF complex promotes the distribution of AP-4 complex to the perinuclear area of the cell . Location Topology: Peripheral membrane protein Sequence Mass (Da): 33128 Sequence Length: 292 Subcellular Location: Cytoplasm

Q70DU8

MAAKKVFGSAEASNLVTELRRSFDDGVTRGYEWRVTQLKKLMIICDNHEPEIVAALRDDLGKPELESSVYEVSLLRNSIKLALKQLKNWMAPEKAKTSLTTFPASAEIVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLTKLLEQYLDPSAVRVVEGAVTETSALLEQKWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIVGKWGCNNGQACVSPDYILTTKEYAPKLIDAMKLELEKFYGKNPIESKDMSRIVNSNHFDRLSKLLDEKEVSDKIVYGGEKDRENLKIAPTILLDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLALHTLPFGGVGESGMGAYHGKFSFDAFSHKKAVLYRSLFGDSAVRYPPYSRGKLRLLKALVDSNIFDLFKVLLGLA

Function: Involved in oxidative stress tolerance by detoxifying reactive aldehydes derived from lipid peroxidation. Medium- to long-chain saturated aldehydes are preferred substrates, while the short-chain aldehyde propanal is a weak substrate. Is strictely NAD(+) specific. Catalytic Activity: an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH Sequence Mass (Da): 53159 Sequence Length: 484 EC: 1.2.1.3

Q8W033

MTKLLEINHIQTLCFAKGFSPARLNVATSPFRISRRGGGGYCSNACIPYRLKFTCYATLSAVVKEQASDFSGKEAALLVDELRSNFNSGRTKSYEWRISQLQNIARMIDEKEKCITEALYQDLSKPELEAFLAEISNTKSSCMLAIKELKNWMAPETVKTSVTTFPSSAQIVSEPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLFSEYLDNTTIRVIEGGVPETTALLDQKWDKIFFTGGARVARIIMAAAARNLTPVVLELGGKCPALVDSDVNLQVAARRIIAGKWACNSGQACIGVDYVITTKDFASKLIDALKTELETFFGQNALESKDLSRIVNSFHFKRLESMLKENGVANKIVHGGRITEDKLKISPTILLDVPEASSMMQEEIFGPLLPIITVQKIEDGFQVIRSKPKPLAAYLFTNNKELEKQFVQDVSAGGITINDTVLHVTVKDLPFGGVGESGIGAYHGKFSYETFSHKKGVLYRSFSGDADLRYPPYTPKKKMVLKALLSSNIFAAILAFFGFSKDS

Function: Involved in oxidative stress tolerance by detoxifying reactive aldehydes derived from lipid peroxidation. Medium- to long-chain saturated aldehydes are preferred substrates, while the short-chain aldehyde propanal is a weak substrate. Can use both NAD(+) and NADP(+), but the coenzyme preference is substrate dependent. Catalytic Activity: an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH Sequence Mass (Da): 60173 Sequence Length: 550 Subcellular Location: Plastid EC: 1.2.1.3

Q7SY23

MLRARSAVSQSWKGFKTFSCVAVEVKNEPVLEFKEGSKERAELEEALRNLKGKTEEIPCVIGNEEVWTKDIRFQLSPFNHSHQVAKFCYADKDLLNKAIEASVAARREWDLKPVSDRAQIFFKAADIISGPKRAEVLAKTMIGQGKTVVQAEIDAAPELIDFFRFNAKHAIELEDQQPLDSDGSTNTMLYRGLEGFVAAVAPFNFTAIGGNLAGTPALMGNVVLWKPSDTAMSASYAVYKILRESGLPPNIIQFVPADGPVFGDTVTSSEHLAGINFTGSVPTFKRLWKQVAQNLDIYKNFPRVAGECGGKNFHFVHKSADVRSVVTGTIRSAFEYGGQKCSACSRMYVPDSLWPQIRQGLLDVYKQIKVGDPVEDFSTFFSAVIDDKSFSRIKGWLEHARSSPHLKIIAGGNCDDKKGYFVEPTIIETTDPQEKIMNEEIFGPVLTVYVYPENDYKKVLHLIDNTSPYALTGAIFPQDKSVIEEAGKALRNAAGNYYINDKSTGSIVAQQPFGGARASGTNDKPGGPHYVLRWTSPQVVKQTHVPLTEWKYPYMS

Function: Irreversible conversion of delta-1-pyrroline-5-carboxylate (P5C), derived either from proline or ornithine, to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles (By similarity). Catalytic Activity: H2O + L-glutamate 5-semialdehyde + NAD(+) = 2 H(+) + L-glutamate + NADH Sequence Mass (Da): 61587 Sequence Length: 556 Pathway: Amino-acid degradation; L-proline degradation into L-glutamate; L-glutamate from L-proline: step 2/2. Subcellular Location: Mitochondrion matrix EC: 1.2.1.88

P30038

MLLPAPALRRALLSRPWTGAGLRWKHTSSLKVANEPVLAFTQGSPERDALQKALKDLKGRMEAIPCVVGDEEVWTSDVQYQVSPFNHGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSGPRRAEILAKTMVGQGKTVIQAEIDAAAELIDFFRFNAKYAVELEGQQPISVPPSTNSTVYRGLEGFVAAISPFNFTAIGGNLAGAPALMGNVVLWKPSDTAMLASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRFHTFPRLAGECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDFGTFFSAVIDAKSFARIKKWLEHARSSPSLTILAGGKCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDKYKETLQLVDSTTSYGLTGAVFSQDKDVVQEATKVLRNAAGNFYINDKSTGSIVGQQPFGGARASGTNDKPGGPHYILRWTSPQVIKETHKPLGDWSYAYMQ

Function: Irreversible conversion of delta-1-pyrroline-5-carboxylate (P5C), derived either from proline or ornithine, to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, glutaric and adipic semialdehydes. Catalytic Activity: H2O + L-glutamate 5-semialdehyde + NAD(+) = 2 H(+) + L-glutamate + NADH Sequence Mass (Da): 61719 Sequence Length: 563 Pathway: Amino-acid degradation; L-proline degradation into L-glutamate; L-glutamate from L-proline: step 2/2. Subcellular Location: Mitochondrion matrix EC: 1.2.1.88

Q8CHT0

MLPLPSLRRSLLSHAWRGAGLRWKHTSSLKVTNEPILAFSQGSPERDALQKALKDLKGQMEAIPCVVGDEEVWTSDIQYQLSPFNHAHKVAKFCYADKALLNRAIDAALAARKEWDLKPMADRAQVFLKAADMLSGPRRAEVLAKTMVGQGKTVIQAEIDAAAELIDFFRFNAKFAVELEGEQPISVPPSTNHTVYRGLEGFVAAISPFNFTAIGGNLAGAPALMGNVVLWKPSDTAMLASYAVYRILREAGLPPNIIQFVPADGPTFGDTVTSSEHLCGINFTGSVPTFKHLWRQVAQNLDRFRTFPRLAGECGGKNFHFVHSSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPKSLWPQIKGRLLEEHSRIKVGDPAEDFGTFFSAVIDAKAFARIKKWLEHARSSPSLSILAGGQCNESVGYYVEPCIIESKDPQEPIMKEEIFGPVLTVYVYPDDKYRETLQLVDSTTSYGLTGAVFAQDKAIVQEATRMLRNAAGNFYINDKSTGSVVGQQPFGGARASGTNDKPGGPHYILRWTSPQVIKETHKPLGDWRYSYMQ

Function: Irreversible conversion of delta-1-pyrroline-5-carboxylate (P5C), derived either from proline or ornithine, to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, glutaric and adipic semialdehydes (By similarity). PTM: Acetylation of Lys-98, Lys-113 and Lys-401 is observed in liver mitochondria from fasted mice but not from fed mice. Catalytic Activity: H2O + L-glutamate 5-semialdehyde + NAD(+) = 2 H(+) + L-glutamate + NADH Sequence Mass (Da): 61841 Sequence Length: 562 Pathway: Amino-acid degradation; L-proline degradation into L-glutamate; L-glutamate from L-proline: step 2/2. Subcellular Location: Mitochondrion matrix EC: 1.2.1.88

P0C2X9

MLPPALLRRSLLSYAWRGSGLRWKHASSLKVANEPILAFTQGSPERDALQKALNDLKDQTEAIPCVVGDEEVWTSDVRYQLSPFNHGHKVAKFCYADKALLNKAIEAAVLARKEWDLKPVADRAQIFLKAADMLSGPRRAEILAKTMVGQGKTVIQAEIDAAAELIDFFRFNAKFAVELEGEQPISVPPSTNHVVYRGLEGFVAAISPFNFTAIGGNLAGAPALMGNVVLWKPSDTAMLASYAVYRILREAGLPPNVIQFVPADGPTFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRFRTFPRLAGECGGKNFHFVHSSADVDSVVSGTLRSAFEYGGQKCSACSRLYVPQSLWPQIKGRLLEEHSRIKVGNPAEDFGTFFSAVIDAKAFARIKKWLEHARSSPSLSILAGGQCNESVGYFVEPCIIESKDPQEPIMKEEIFGPVLTVYVYPDEKYRETLQLVDSTTSYGLTGAVFAQDKTIVQEATRMLRNAAGNFYINDKSTGSVVGQQPFGGARASGERDIPGQPRLVQLWTEPPFTPLAVSPPLGDWRYSYMQ

Function: Irreversible conversion of delta-1-pyrroline-5-carboxylate (P5C), derived either from proline or ornithine, to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, glutaric and adipic semialdehydes (By similarity). Catalytic Activity: H2O + L-glutamate 5-semialdehyde + NAD(+) = 2 H(+) + L-glutamate + NADH Sequence Mass (Da): 61869 Sequence Length: 563 Pathway: Amino-acid degradation; L-proline degradation into L-glutamate; L-glutamate from L-proline: step 2/2. Subcellular Location: Mitochondrion matrix EC: 1.2.1.88

P20292

MDQETVGNVVLLAIVTLISVVQNGFFAHKVEHESRTQNGRSFQRTGTLAFERVYTANQNCVDAYPTFLAVLWSAGLLCSQVPAAFAGLMYLFVRQKYFVGYLGERTQSTPGYIFGKRIILFLFLMSVAGIFNYYLIFFFGSDFENYIKTISTTISPLLLIP

Function: Required for leukotriene biosynthesis by ALOX5 (5-lipoxygenase). Anchors ALOX5 to the membrane. Binds arachidonic acid, and could play an essential role in the transfer of arachidonic acid to ALOX5. Binds to MK-886, a compound that blocks the biosynthesis of leukotrienes. Location Topology: Multi-pass membrane protein Sequence Mass (Da): 18157 Sequence Length: 161 Domain: The C-terminal part after residue 140 is mostly unstructured. Subcellular Location: Nucleus membrane

P30357

MDQEAVGNVVLLAIVTLISVVQNGFFAHKVEHESRNQNGRSFQRTGTLAFERVYTANQNCVDAYPTFLAVLWTAGLLCSQVPAAFAGLMYLFVRQKYFVGYLGERTQSTPGYIFGKRIILFLFLMSLAGILNYCLILLFGSDFENYIKTISTT

Function: Required for leukotriene biosynthesis by ALOX5 (5-lipoxygenase). Anchors ALOX5 to the membrane. Binds arachidonic acid, and could play an essential role in the transfer of arachidonic acid to ALOX5. Binds to MK-886, a compound that blocks the biosynthesis of leukotrienes (By similarity). Location Topology: Multi-pass membrane protein Sequence Mass (Da): 17159 Sequence Length: 153 Domain: The C-terminal part after residue 140 is mostly disordered. Subcellular Location: Nucleus membrane

P30358

MDQETVGNIVLLAIVTLISVVQNGFFAHKVEHESKTHNGRSFQRTGPLAFERVYTANQNCVDAYPTFLVMLWSAGLLCSQVPAAFAGLMYLFVRQKYFVGYLGERTQSTPGYIFGKRIILFLFAMSLAGILNYFLIAFFGSDFENYIKTVTTT

Function: Required for leukotriene biosynthesis by ALOX5 (5-lipoxygenase). Anchors ALOX5 to the membrane. Binds arachidonic acid, and could play an essential role in the transfer of arachidonic acid to ALOX5. Binds to MK-886, a compound that blocks the biosynthesis of leukotrienes (By similarity). Location Topology: Multi-pass membrane protein Sequence Mass (Da): 17207 Sequence Length: 153 Domain: The C-terminal part after residue 140 is mostly disordered. Subcellular Location: Nucleus membrane

Q2KJC9

MWRVPGLLCVRVARKSKFSGSWNRPAAFMSTLLINQPQYAWLKELGLREENDGVYNGSWGGRGEVITTYCPANNEPIARVRQASMADYEETVEKAREAWSIWADVPAPKRGEVVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQEYVDVCDYAVGLSRMIGGPILPSERPGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNACLWKGAPTTSLISVAVTKIIAKVLEDNKLPGAICSLTCGGADIGTAMAKDERVDLLSFTGSTQVGKQVALMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFLHESIHDEVVNRLKKAYAQIRVGNPWDSNVLYGPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKVMDRPGNYVEPTIVTGLDHDASIVHTETFAPILYVFKFKNEDEVFAWNNEVKQGLSSSIFTKDMGRIFRWLGPKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDAWKQYMRRSTCTINYSKDLPLAQGIKFQ

Function: Multifunctional enzyme mediating important protective effects. Metabolizes betaine aldehyde to betaine, an important cellular osmolyte and methyl donor. Protects cells from oxidative stress by metabolizing a number of lipid peroxidation-derived aldehydes. Involved in lysine catabolism. Catalytic Activity: H2O + NAD(+) + nonanal = 2 H(+) + NADH + nonanoate Sequence Mass (Da): 58582 Sequence Length: 539 Pathway: Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine from betaine aldehyde: step 1/1. Subcellular Location: Cytoplasm EC: 1.2.1.31

P10593

MAETNPELSDLMAQTNKKIVPKFTEIFPVEDVNYPYSAFIASVRKDVIKHCTDHKGIFQPVLPPEKKVPELWFYTELKTRTSSITLAIRMDNLYLVGFRTPGGVWWELARPATPTSSATTPGGSASAAGTRTSSATRVWRPSPWAARDDQGRQRPGEEEEDGDTGGGGGADADADAGGAELAAAAAAADPQADTKSKLVKLVVMVCEGLRFNTLSRTVDAGFNSQHGVTLTVTQGKQVQKWDRISKAAFEWADHPTAVIPDMQKLGIKDKNEAARIVALVKNQTTAAAAAATAASADNDDDEA

Function: A possible regulatory factor for the synthesis of zeins, the major group of storage proteins. Catalytic Activity: Endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S rRNA. Sequence Mass (Da): 32428 Sequence Length: 303 Subcellular Location: Cytoplasm EC: 3.2.2.22

Q9FYL3

MSSTISLKPTHLILSSFSTGKVLQFRRSRFSHTPSSSSSRYRTLVAQLGFRPDSFDFIKDHAENLLYTIADAAVSSSETFESVAGTTTKTTQSNDWFSGIANYMETILKVLKDGLSTVHVPYSYGFAIILLTVLVKAATFPLTKKQVESAMAMKSLTPQIKAIQERYAGDQEKIQLETARLYKLAGINPLAGCLPTLATIPVWIGLYRALSNVADEGLLTEGFFWIPSLAGPTTVAARQNGSGISWLFPFIEGHPPLGWPDTLAYLVLPLLLVFSQYLSIQIMQSSQSNDPAMKSSQAVTKLLPLMIGYFALSVPSGLSLYWLTNNILSTAQQVWLQKYGGAKNPVEKFTNLVTKEDKTQQIEKSFSEPLVQKSVSELKIPREKGGEKVTPECPKPGERFRLLKEQEAKRRREKEERQKAEAALSNQNTDKAHEQDEKSDTAIVAEDDKKTELSAVDETSDGTVAVNGKPSIQKDETTNGTFGIGHDTEQQHSHETEKR

Function: Required for the insertion of some light harvesting chlorophyll-binding proteins (LHCP) into the chloroplast thylakoid membrane. Plays a role in the accumulation of some cytochrome b6f components in the thylakoid membrane . Required for the assembly and/or stability of the F(1)F(0) ATP synthase in chloroplast thylakoid membranes. Functions to stabilize or promote assembly of F(1) during its attachment to the membrane-embedded F(0) part . Participates with STIC2 in thylakoid protein targeting. May function with a specific subset of thylakoidal proteins . Location Topology: Multi-pass membrane protein Sequence Mass (Da): 55188 Sequence Length: 499 Subcellular Location: Plastid

Q9YAW1

MSIEPQKPNTILVGRKPTINYVMAALKLLNEEGAPEVVIKARGRNICNAVDTVEMLKNLFIKNLVIKKVNIYSESLDSEGKKKVSAIEIVVAKG

Function: Binds double-stranded DNA tightly but without sequence specificity. It is distributed uniformly and abundantly on the chromosome, suggesting a role in chromatin architecture. However, it does not significantly compact DNA. Binds rRNA and mRNA in vivo. May play a role in maintaining the structural and functional stability of RNA, and, perhaps, ribosomes (By similarity). PTM: Acetylated. Deacetylation by the SIR2-homolog deacetylase may regulate its activity (By similarity). Sequence Mass (Da): 10336 Sequence Length: 94 Subcellular Location: Cytoplasm

Q8TXF9

MAEEENVVYVGSKPVMNYVLACITQFNEGANEVRIKARGRAISRAVDVAEIVRNRFMPEVEVKDIKIGTEELETEEGDTVNVSTIEIVLEKPV

Function: Binds double-stranded DNA tightly but without sequence specificity. It is distributed uniformly and abundantly on the chromosome, suggesting a role in chromatin architecture. However, it does not significantly compact DNA. Binds rRNA and mRNA in vivo. May play a role in maintaining the structural and functional stability of RNA, and, perhaps, ribosomes (By similarity). PTM: Acetylated. Deacetylation by the SIR2-homolog deacetylase may regulate its activity (By similarity). Sequence Mass (Da): 10381 Sequence Length: 93 Subcellular Location: Cytoplasm

P60849

MSSGTPTPSNVVLIGKKPVMNYVLAALTLLNQGVSEIVIKARGRAISKAVDTVEIVRNRFLPDKIEIKEIRVGSQVVTSQDGRQSRVSTIEIAIRKK

Function: Binds double-stranded DNA tightly but without sequence specificity. It is distributed uniformly and abundantly on the chromosome, suggesting a role in chromatin architecture. May be involved in DNA compaction. May bind rRNA and mRNA, playing a role in maintaining the structural and functional stability of RNA, and, perhaps, ribosomes. PTM: Acetylated. Deacetylation by the SIR2-homolog deacetylase increases its DNA-binding affinity, thereby repressing transcription. Regulation of DNA-based activities is therefore achieved at the chromatin level. Sequence Mass (Da): 10585 Sequence Length: 97 Subcellular Location: Cytoplasm

Q9YAX2

MACEGAPEVRIGRKPVMNYVLAILTTLMEQGTNQVVVKARGRNINRAVDAVEIVRKRFAKNIEIKDIKIDSQEIEVQTPEGQTRTRRVSSIEICLEKAGESA

Function: Binds double-stranded DNA tightly but without sequence specificity. It is distributed uniformly and abundantly on the chromosome, suggesting a role in chromatin architecture. However, it does not significantly compact DNA. Binds rRNA and mRNA in vivo. May play a role in maintaining the structural and functional stability of RNA, and, perhaps, ribosomes (By similarity). PTM: Acetylated. Deacetylation by the SIR2-homolog deacetylase may regulate its activity (By similarity). Sequence Mass (Da): 11380 Sequence Length: 102 Subcellular Location: Cytoplasm

O28323

MAEHVVYVGNKPVMNYVLATLTQLNEGADEVVIKARGRAISRAVDVAEIVRNRFMPGVKVKEIKIDTEELESEQGRRSNVSTIEIVLAK

Function: Binds double-stranded DNA tightly but without sequence specificity. It is distributed uniformly and abundantly on the chromosome, suggesting a role in chromatin architecture. However, it does not significantly compact DNA. Binds rRNA and mRNA in vivo. May play a role in maintaining the structural and functional stability of RNA, and, perhaps, ribosomes (By similarity). PTM: Acetylated. Deacetylation by the SIR2-homolog deacetylase may regulate its activity (By similarity). Sequence Mass (Da): 9894 Sequence Length: 89 Subcellular Location: Cytoplasm

Q97ZF4

MTEKLNEIVVRKTKNVEDHVLDVIVLFNQGIDEVILKGTGREISKAVDVYNSLKDRLGDGVQLVNVQTGSEVRDRRRISYILLRLKRVY

Function: Binds double-stranded DNA tightly but without sequence specificity. It is distributed uniformly and abundantly on the chromosome, suggesting a role in chromatin architecture. However, it does not significantly compact DNA. Binds rRNA and mRNA in vivo. May play a role in maintaining the structural and functional stability of RNA, and, perhaps, ribosomes (By similarity). PTM: Acetylated. Deacetylation by the SIR2-homolog deacetylase may regulate its activity (By similarity). Sequence Mass (Da): 10239 Sequence Length: 89 Subcellular Location: Cytoplasm

P71011

MFIEQMFPFINESVRVHQLPEGGVLEIDYLRDNVSISDFEYLDLNKTAYELCMRMDGQKTAEQILAEQCAVYDESPEDHKDWYYDMLNMLQNKQVIQLGNRASRHTITTSGSNEFPMPLHATFELTHRCNLKCAHCYLESSPEALGTVSIEQFKKTADMLFDNGVLTCEITGGEIFVHPNANEILDYVCKKFKKVAVLTNGTLMRKESLELLKTYKQKIIVGISLDSVNSEVHDSFRGRKGSFAQTCKTIKLLSDHGIFVRVAMSVFEKNMWEIHDMAQKVRDLGAKAFSYNWVDDFGRGRDIVHPTKDAEQHRKFMEYEQHVIDEFKDLIPIIPYERKRAANCGAGWKSIVISPFGEVRPCALFPKEFSLGNIFHDSYESIFNSPLVHKLWQAQAPRFSEHCMKDKCPFSGYCGGCYLKGLNSNKYHRKNICSWAKNEQLEDVVQLI

Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine, the other is coordinated via 3 cysteines and maybe direct contact with the SboA precursor. Function: Catalyzes the formation of 3 thioether bonds during production of the sactipeptide subtilosin from SboA. In vitro the thioether bonds cannot be made in the absence of the SboA propeptide, suggesting this is the first reaction in subtilosin maturation . In vitro, in the absence of a second substrate, cleaves S-adenosyl-L-methionine into Met and 5'-dA . Sequence Mass (Da): 51514 Sequence Length: 448 Subcellular Location: Cytoplasm EC: 1.21.98.-

Q0W252

MPEDNVIFVGNKPVMNYVLAAVTQFNEGAKEVTIKARGRAISRAVDTAEVVRHRFLTDVEIDRIQISTEELASEKGEKINVSSIEIFLKRPRAATD

Function: Binds double-stranded DNA tightly but without sequence specificity. It is distributed uniformly and abundantly on the chromosome, suggesting a role in chromatin architecture. However, it does not significantly compact DNA. Binds rRNA and mRNA in vivo. May play a role in maintaining the structural and functional stability of RNA, and, perhaps, ribosomes. PTM: Acetylated. Deacetylation by the SIR2-homolog deacetylase may regulate its activity. Sequence Mass (Da): 10715 Sequence Length: 96 Subcellular Location: Cytoplasm

P00883

MPHSHPALTPEQKKELSDIAHRIVAPGKGILAADESTGSIAKRLQSIGTENTEENRRFYRQLLLTADDRVNPCIGGVILFHETLYQKADDGRPFPQVIKSKGGVVGIKVDKGVVPLAGTNGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGEHTPSALAIMENANVLARYASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHIYLEGTLLKPNMVTPGHACTQKYSHEEIAMATVTALRRTVPPAVTGVTFLSGGQSEEEASINLNAINKCPLLKPWALTFSYGRALQASALKAWGGKKENLKAAQEEYVKRALANSLACQGKYTPSGQAGAAASESLFISNHAY

Function: Plays a key role in glycolysis and gluconeogenesis. In addition, may also function as scaffolding protein. PTM: Asn-361 in form alpha is deaminated to Asp in form beta. Catalytic Activity: beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate Sequence Mass (Da): 39343 Sequence Length: 364 Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4. Subcellular Location: Cytoplasm EC: 4.1.2.13

B5DGM7

MPHAFPFLTPDQKKELSDIALKIVAKGKGILAADESTGSVAKRFQSINTENTEENRRLYRQLLFTADDRAGPCIGGVIFFHETLYQKTDAGKTFPEHVKSRGWVVGIKVDKGVVPLAGTNGETTTQGLDGLYERCAQYKKDGCDFAKWRCVLKITSTTPSRLAIMENCNVLARYASICQMHGIVPIVEPEILPDGDHDLKRTQYVTEKVLAAMYKALSDHHVYLEGTLLKPNMVTAGHSCSHKYTHQEIAMATVTALRRTVPPAVPGVTFLSGGQSEEEASINLNVMNQCPLHRPWALTFSYGRALQASALKAWGGKPGNGKAAQEEFIKRALANSLACQGKYVASGDSAAAGDSLFVANHAY

Function: Plays a key role in glycolysis and gluconeogenesis. Catalytic Activity: beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate Sequence Mass (Da): 39556 Sequence Length: 363 Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4. EC: 4.1.2.13

P05062

MAHRFPALTQEQKKELSEIAQSIVANGKGILAADESVGTMGNRLQRIKVENTEENRRQFREILFSVDSSINQSIGGVILFHETLYQKDSQGKLFRNILKEKGIVVGIKLDQGGAPLAGTNKETTIQGLDGLSERCAQYKKDGVDFGKWRAVLRIADQCPSSLAIQENANALARYASICQQNGLVPIVEPEVIPDGDHDLEHCQYVTEKVLAAVYKALNDHHVYLEGTLLKPNMVTAGHACTKKYTPEQVAMATVTALHRTVPAAVPGICFLSGGMSEEDATLNLNAINLCPLPKPWKLSFSYGRALQASALAAWGGKAANKEATQEAFMKRAMANCQAAKGQYVHTGSSGAASTQSLFTACYTY

Function: Catalyzes the aldol cleavage of fructose 1,6-biphosphate to form two triosephosphates dihydroxyacetone phosphate and D-glyceraldehyde 3-phosphate in glycolysis as well as the reverse stereospecific aldol addition reaction in gluconeogenesis. In fructolysis, metabolizes fructose 1-phosphate derived from the phosphorylation of dietary fructose by fructokinase into dihydroxyacetone phosphate and D-glyceraldehyde . Acts as an adapter independently of its enzymatic activity, exerts a tumor suppressor role by stabilizing the ternary complex with G6PD and TP53 to inhibit G6PD activity and keep oxidative pentose phosphate metabolism in check . Catalytic Activity: beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate Sequence Mass (Da): 39473 Sequence Length: 364 Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4. Subcellular Location: Cytoplasm EC: 4.1.2.13

P79226

MAHRFPALTPEQKKELSDIAQRIVANGKGILAADESVGTMGNRLQRIKVENTEENRRQFREILFTVDNSINQSIGGVILFHETLYQKDSQGKLFRNILKEKGIVVGIKLDQGGAPLAGTNKETTIQGLDGLSERCAQYKKDGVDFGKWRAVLRIADQCPSSLAIQENANTLARYASICQQNGLVPIVEPEVIPDGDHDLEHCQYVTEKVLAAVYKALNDHHVYLEGTLLKPNMVTAGHACTKKYTPEQVAMATVTALHRTVPAAVPGICFLSGGMSEEDATLNLNAINLCPLPKPWKLSFSYGRALQASALAAWGGKAENKKATQEAFMKRAVVNCQAAKGQYVHTGSSGAASTQSLFTASYTY

Function: Catalyzes the aldol cleavage of fructose 1,6-biphosphate to form two triosephosphates dihydroxyacetone phosphate and D-glyceraldehyde 3-phosphate in glycolysis as well as the reverse stereospecific aldol addition reaction in gluconeogenesis. In fructolysis, metabolizes fructose 1-phosphate derived from the phosphorylation of dietary fructose by fructokinase into dihydroxyacetone phosphate and D-glyceraldehyde (By similarity). Acts as an adapter independently of its enzymatic activity, exerts a tumor suppressor role by stabilizing the ternary complex with G6PD and TP53 to inhibit G6PD activity and keep oxidative pentose phosphate metabolism in check (By similarity). Catalytic Activity: beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate Sequence Mass (Da): 39605 Sequence Length: 364 Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4. Subcellular Location: Cytoplasm EC: 4.1.2.13

P53448

MTHQYPALTTEQKRELQDIAQRIVAPGKGILAADESTGSMAKRLNPIGVENTEENRRLYRQLLFTADERMDKCIGGVIFFHETLYQKADDGTPFAKMIKDRGIVVGIKVDKGVVPLAGTNGETTTQGLDGLSERCAQYKKDGADFAKWRSVLKISETSPSELAIMENANVLARYASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAACYKALSDHHVYLEGTLLKPNMVTAGHSCPTKFSNQEIAMATVTALRRTVPPAVTGVTFLSGGQSEEEASINLNAINNCPLTKPWALTFSYGRALQASALSAWRGVKENEKAATEEFLKRAEANGLAAQGKYVSSGMDGSAGQSLYVANHAY

Catalytic Activity: beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate Sequence Mass (Da): 39475 Sequence Length: 363 Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4. EC: 4.1.2.13

P53449

LLKPNMVTPGHSCPTKYSPEEIAMATVTALRRTVPPAVPGVTFLSGGQSEEEASINLNAINTCPLVRPWALTFSYGRALQASALSAWRGQRDNANAATEEFVKRAEVNGLAALGKYEGSGDDSGAAGQSLYVANHAY

Catalytic Activity: beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate Sequence Mass (Da): 14438 Sequence Length: 137 Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4. EC: 4.1.2.13

Q9GKW3

MPHSYPALSAEQKKELSDIALRIVAPGKGILAADESVGSMAKRLSQIGVENTEENRRLYRQVLFSADDRVKKCIGGVIFFHETLYQKDDNGVPFVRTIQDKGIVVGIKVDKGVVPLAGTDGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKISERTPSALAILENANVLARYASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHVYLEGTLLKPNMVTPGHACPIKYTPEEIAMATVTALRRTVPPAVPGVTFLSGGQSEEEASLNLNAINRCPLPRPWALTFSYGRALQASALNAWRGQRDNAGAATEEFIKRAEVNGLAAQGKYEGSGEDGGAAAQSLYIANHAY

Catalytic Activity: beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate Sequence Mass (Da): 39422 Sequence Length: 364 Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4. EC: 4.1.2.13

Q9USD4

MTSKESICWYLANILLVTCIGYYSYKTPFTKVEESFAMQAIHDIQTYRWDLSKYDHLEFPGAVKRSFIPSLFIAVLSYIPSWFVNPLLAARWTIGYLSWESMNSVSCSISKRFGTLSGALFILFSCAQFHLVYYMSRPLSNIFGLIATNHSLSLLLKNNYYGSISILVFAAAIVRSEIALLLMCLILPLLLQRRITLSKLLLVGISSSLAAVGASFLIDSYFWGAWCWPELEAFLFNVVEGKSSDWGTSPFYYYFVRLPWLFLNPTTLLFLLISFVYIKPARLLIYVPLFFIFVYSFLGHKEWRFIIYSIPWFNAASAIGASLCFNASKFGKKIFEILRLMFFSGIIFGFIGSSFLLYVFQYAYPGGLALTRLYEIENHPQVSVHMDVYPCMTGITRFSQLPSWYYDKTEDPKMLSNSLFISQFDYLITEDPESYNDTFDVIESVNSNTKIPILPKWLSNHIPREISIRNPAQPVYILANKKARATKPAAVDDYSSFIGHKVDEIKLWPPIYRVVSPDTLLTRDYREDRLNFFIDKDRILTHITQG

Function: Adds the eighth mannose residue in an alpha-1,6 linkage onto the dolichol-PP-oligosaccharide precursor (dolichol-PP-Man(7)GlcNAc(2)) required for protein glycosylation. Catalytic Activity: a dolichyl beta-D-mannosyl phosphate + alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol = a dolichyl phosphate + alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + H(+) Location Topology: Multi-pass membrane protein Sequence Mass (Da): 62880 Sequence Length: 546 Pathway: Protein modification; protein glycosylation. Subcellular Location: Endoplasmic reticulum membrane EC: 2.4.1.260

P53730

MRWSVLDTVLLTVISFHLIQAPFTKVEESFNIQAIHDILTYSVFDISQYDHLKFPGVVPRTFVGAVIIAMLSRPYLYLSSLIQTSRPTSIDVQLVVRGIVGLTNGLSFIYLKNCLQDMFDEITEKKKEENEDKDIYIYDSAGTWFLLFLIGSFHLMFYSTRTLPNFVMTLPLTNVALGWVLLGRYNAAIFLSALVAIVFRLEVSALSAGIALFSVIFKKISLFDAIKFGIFGLGLGSAISITVDSYFWQEWCLPEVDGFLFNVVAGYASKWGVEPVTAYFTHYLRMMFMPPTVLLLNYFGYKLAPAKLKIVSLASLFHIIVLSFQPHKEWRFIIYAVPSIMLLGATGAAHLWENMKVKKITNVLCLAILPLSIMTSFFISMAFLYISRMNYPGGEALTSFNDMIVEKNITNATVHISIPPCMTGVTLFGELNYGVYGINYDKTENTTLLQEMWPSFDFLITHEPTASQLPFENKTTNHWELVNTTKMFTGFDPTYIKNFVFQERVNVLSLLKQIIFDKTPTVFLKELTANSIVKSDVFFTYKRIKQDEKTD

Function: Adds the eighth mannose residue in an alpha-1,6 linkage onto the dolichol-PP-oligosaccharide precursor (dolichol-PP-Man(7)GlcNAc(2)) required for protein glycosylation. Catalytic Activity: a dolichyl beta-D-mannosyl phosphate + alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol = a dolichyl phosphate + alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + H(+) Location Topology: Multi-pass membrane protein Sequence Mass (Da): 62672 Sequence Length: 551 Pathway: Protein modification; protein glycosylation. Subcellular Location: Endoplasmic reticulum membrane EC: 2.4.1.260

Q750J3

MSTTTKSKMEGPKTVVVTCGATVPFPGLVNAVLDRRVLAELAQCGFSRVMVQYGRGFAAEFERQVGAAGAVRAACDAEGLEGCDAHAWRWQGLEIIGFAFHAQMESLIGTSAALVVSHAGTGSILDALRQQKPLIVCVNEALLDNHQEQIARRFEALGHLWAIRADVDELAGALARSTRETLAPLPPAYKQGFAELLQDVAHR

Function: Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway (By similarity). Catalytic Activity: N-acetyl-alpha-D-glucosaminyl-diphosphodolichol + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N,N'-diacetylchitobiosyl diphosphodolichol + UDP Sequence Mass (Da): 21794 Sequence Length: 203 Subcellular Location: Endoplasmic reticulum EC: 2.4.1.141

Q4WQN1

MLATKVCFVTVGATASFEELVRAALDPSFVTALEENGYSHLLVQYGKNAVIYENFLKQYPPERRPWRRINISGFSFHEHGLGGDFALAQADISKGRSGGLVISHAGSGTILEVLRMGIPLIVVPNPSLQDNHQEELARQLQKQGYVVASHYQNLCQALHQAEQLRARMLRWPPVRGPDQKNQPTLEQVMSDEMGFVD

Function: Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway (By similarity). Catalytic Activity: N-acetyl-alpha-D-glucosaminyl-diphosphodolichol + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N,N'-diacetylchitobiosyl diphosphodolichol + UDP Sequence Mass (Da): 21969 Sequence Length: 197 Subcellular Location: Endoplasmic reticulum EC: 2.4.1.141

Q5ABE5

MFDWRRLKPLRPHQIFFFYTTIQNYSDNGYQYSYKSNQIKSNQIKLNQQQQTSRQLIRINNQLPPSVVLHNIIMKSILITTGATITFKSLIQIILSPQFLNNLIRLKINKLIIQYGHEIKNSINLSESFFNETINKYDLINLFNLEIEETPIGDDDDDEGIRLFKNSDIEILAFSYSSNINKYIENVDLIISHAGTGSIIDCLHLNKPLIVIVNDKLMDNHQLEIAQQFTKLNYCIYYSIKELEQYVNNNDNNKDSRFWNQLNQLINGELQLNKLPQTDGSIIETIICEELEK

Function: Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway (By similarity). Catalytic Activity: N-acetyl-alpha-D-glucosaminyl-diphosphodolichol + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N,N'-diacetylchitobiosyl diphosphodolichol + UDP Sequence Mass (Da): 34283 Sequence Length: 293 Subcellular Location: Endoplasmic reticulum EC: 2.4.1.141

Q6FVR6

MSAFVTCGATVPFPALVEAVLAPEFVGCLSREGYRVLCVQFGRGYDFEAQFTSVTCTRMPLESAEVSELRQLVRDERVTVMGYKVQDVVVLGFAYSNNILQIIDRYGDVVISHAGTGSILDSLRLNKKLIVVVNHTLMDNHQKQIAEKFQNLGHILATNPTAIELCDAMKRLKHEDLIPLSSETNTEFMERLKSIAYS

Function: Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway (By similarity). Catalytic Activity: N-acetyl-alpha-D-glucosaminyl-diphosphodolichol + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N,N'-diacetylchitobiosyl diphosphodolichol + UDP Sequence Mass (Da): 22088 Sequence Length: 198 Subcellular Location: Endoplasmic reticulum EC: 2.4.1.141

P0CN89

MAHPFTLLVTVGSTLFPSLTSHVLLPTFLSLLQSLGVQRLVVQYGRAELKLQDDVKQTLNIDSQGDGIGVWSDNDGDRVRDEKQNGMVVEVMRFTNDFEGLVGKSDAVISHAGSGSILTVLRRAPPIPLLVVPNRSLMDDHQSELADALYKDGYVMVASVEDLEEKVQPFLKIWPSQAKLFPETRKEVFREVVDDLMGYD

Function: Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway (By similarity). Catalytic Activity: N-acetyl-alpha-D-glucosaminyl-diphosphodolichol + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N,N'-diacetylchitobiosyl diphosphodolichol + UDP Sequence Mass (Da): 22241 Sequence Length: 200 Subcellular Location: Endoplasmic reticulum EC: 2.4.1.141

Q6BST1

MTSVLFTSGATVTFRELIEVITSYDFIVETIIGNGITRMIVQYGNEIETGTQKHVSEEFYRQCVEDKELKQSLQLEVVSGSQNDSNVVTYRSNKYRGFEMVVFPFSNDIGSFISESDVVISHAGTGSIIDTLRLEKPLIVVTNDKLMNKHQEEVADELVKLGCCRKMTIEDMKSSQLKDCISEILSGPETFNKLPECSTTEVEGIIYHELVK

Function: Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway (By similarity). Catalytic Activity: N-acetyl-alpha-D-glucosaminyl-diphosphodolichol + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N,N'-diacetylchitobiosyl diphosphodolichol + UDP Sequence Mass (Da): 23838 Sequence Length: 212 Subcellular Location: Endoplasmic reticulum EC: 2.4.1.141

Q6CXY0

MNNTVLVTCGATVSFPRLVETVLDRSVTEKLKVLGYGRIVIQYGRGFSDTFLQLVEKHLGLFTEKKSCGIKVLDKIENLKVISVDGIEICGFEFSHDIEKLIANNIDLVISHAGTGSILDSLRVGKKLIVVVNDTLMDNHQQLIADKFEQQKLLWSVHANTEELLRALDRSENEELLKIDNTYNKQFEKLLYNVAID

Function: Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway (By similarity). Catalytic Activity: N-acetyl-alpha-D-glucosaminyl-diphosphodolichol + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N,N'-diacetylchitobiosyl diphosphodolichol + UDP Sequence Mass (Da): 22234 Sequence Length: 197 Subcellular Location: Endoplasmic reticulum EC: 2.4.1.141

O14190

MNAFVTVGSTQFDDLIRAVLKPEFQHCLVKHGINQLIVQYGKGKQAFGDPKSVAGLTILGFDYAPEIESYIHDASIVISHAGAGSILQTLRSGKRLLVVPNESLMDNHQVELATKLASMNYLVTCSTSNLVEGLEELYPKILTPFPKSDCSTFQKVMQDVAR

Function: Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway (By similarity). Catalytic Activity: N-acetyl-alpha-D-glucosaminyl-diphosphodolichol + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N,N'-diacetylchitobiosyl diphosphodolichol + UDP Sequence Mass (Da): 17769 Sequence Length: 162 Subcellular Location: Endoplasmic reticulum EC: 2.4.1.141

Q6C3P1

MHESSALSKLYNWDCSVVFIILNIYTTMLVLVTTGGTVPFEALIELVLSHESITTLSQLGFSKMRVQYGRGNRHIFTKHHKEGVMSITGFEYTDDLAGEMSRAHLVISHAGTGSVLDALRIGKHPVVVVNSKLMDNHQIEIAEELFRKRHLLVSGDTDSVGFIKALKMHREYLFETLPDPEEGILQRIIEETVSFM

Function: Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway (By similarity). Catalytic Activity: N-acetyl-alpha-D-glucosaminyl-diphosphodolichol + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N,N'-diacetylchitobiosyl diphosphodolichol + UDP Sequence Mass (Da): 22071 Sequence Length: 196 Subcellular Location: Endoplasmic reticulum EC: 2.4.1.141

P53178

MGIIEEKALFVTCGATVPFPKLVSCVLSDEFCQELIQYGFVRLIIQFGRNYSSEFEHLVQERGGQRESQKIPIDQFGCGDTARQYVLMNGKLKVIGFDFSTKMQSIIRDYSDLVISHAGTGSILDSLRLNKPLIVCVNDSLMDNHQQQIADKFVELGYVWSCAPTETGLIAGLRASQTEKLKPFPVSHNPSFERLLVETIYS

Function: Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway. Catalytic Activity: N-acetyl-alpha-D-glucosaminyl-diphosphodolichol + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N,N'-diacetylchitobiosyl diphosphodolichol + UDP Sequence Mass (Da): 22661 Sequence Length: 202 Subcellular Location: Endoplasmic reticulum EC: 2.4.1.141

Q750Y9

MAWLAIVCLLAATTALCVRMAALAPGVYGPAVCGGRSGGGRGPPRHVMIFLGSGGHTGEMLRLLEVYGAALVAGATVRVGYTDEASAERGRQSAALRAARGVEYVPLLKAREVGAGAGAAVRSTVRAAAQAFSAVRRARRALHTGPHVVVLNGPGTSVVVLFWLRVLDLLSLRRTRVVYVESLARTESLSLSGRLAYPFADEFVVQWPDLAQRYRRARWFGALV

Function: Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway. Anchors the catalytic subunit ALG13 to the ER (By similarity). Location Topology: Single-pass membrane protein Sequence Mass (Da): 23809 Sequence Length: 224 Subcellular Location: Endoplasmic reticulum membrane

Q4WNB5

MFSMLRRMKLDPSTYTYRTYVVSSGDNFSAARAVEFETEWLKQSPKLSFPANGSNSTESYAVVTVPRARRVHQSYLTAPLSTLQCFYACFLVLCGRHPEQKSPLPTTNSPYPDVILTNGPATAVCMVLAAKSLRLFHYLKSLFYIKDHQDRDSSRSSQVKRSEDAPAPVHFQLRTIYVESWARVTTFSLSGKLLLPFADRFLVQWPDLAGKQAWRGMRETEYAGTLVD

Function: Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway. Anchors the catalytic subunit alg13 to the ER (By similarity). Location Topology: Single-pass membrane protein Sequence Mass (Da): 25865 Sequence Length: 228 Subcellular Location: Endoplasmic reticulum membrane

Q5A5N6

MDIETAACFSIAFIATPILIVLVRLLFILPSLRLPTSVKKKKKLIQECQLSILLGSGGHTGEMMRIISKLDMGKVSRTWIYTSGDNASLAKAQDYERKSGTSSQYIPIPRARTVGQSYISSIPTTIYSFLFSAIAMLKHRPAVILLNGPGTCVPVAYILFLYKLLGLCNTKIIYIESLARVNKLSLSGLLLLPISDRFIVQWESLYQQYSRVEYYGILI

Function: Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway. Anchors the catalytic subunit ALG13 to the ER (By similarity). Location Topology: Single-pass membrane protein Sequence Mass (Da): 24460 Sequence Length: 219 Subcellular Location: Endoplasmic reticulum membrane

Q6FV75

MPFLSTAHLCALLLILGCFYIGRLIKVIPILRFACAGEAEIKPLFIQPKSNDGIHLFVFLGSGGHTGEMLRLLQNHQEVLLNKRNTFYIGYSDDDSKARFLSMVEKYDFKAERIHFYPFAKAREVNAGPIASIVTISKTLLTGFTNVLSIKMNTLGQPHLTLLNGPGTCCIINFWLKLLEWLIYIPYLSNGSNVVYIESLARIESLSLTGKILYLLADVFVVQWEELKVRKAPRSEYYGILV

Function: Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway. Anchors the catalytic subunit ALG13 to the ER (By similarity). Location Topology: Single-pass membrane protein Sequence Mass (Da): 27335 Sequence Length: 242 Subcellular Location: Endoplasmic reticulum membrane

Q5PQ59

MQACHNFPDLDSFLVEKIPLAAYYVPEYISKSEEEYLLRQVYNAPKPKWTQLSGRKLQNWGGLPHSRGMVQEKLPSWLQKYTDQISSLGVFGDHSANHVLVNEYNAGEGIMPHEDGPMYYPTVTTISLGSHTLLDFYVPINKECQETQNQDKVASTEEQRHMLSLLLEPRSLLVVREELYTSYLHGICPRTSDTLSPMVANLGNSTAHAGDTLQRGTRVSLTIRFVPKVLKTSLLLGKGR

Cofactor: Binds 1 Fe(2+) ion per subunit. Function: Probable dioxygenase that requires molecular oxygen, alpha-ketoglutarate and iron. Sequence Mass (Da): 27077 Sequence Length: 240 Subcellular Location: Cytoplasm EC: 1.14.11.-

Q9BT30

MAGTGLLALRTLPGPSWVRGSGPSVLSRLQDAAVVRPGFLSTAEEETLSRELEPELRRRRYEYDHWDAAIHGFRETEKSRWSEASRAILQRVQAAAFGPGQTLLSSVHVLDLEARGYIKPHVDSIKFCGATIAGLSLLSPSVMRLVHTQEPGEWLELLLEPGSLYILRGSARYDFSHEILRDEESFFGERRIPRGRRISVICRSLPEGMGPGESGQPPPAC

Cofactor: Binds 1 Fe(2+) ion per subunit. Function: May function as protein hydroxylase; can catalyze auto-hydroxylation at Leu-110 (in vitro), but this activity may be due to the absence of the true substrate . Required to induce programmed necrosis in response to DNA damage caused by cytotoxic alkylating agents. Acts by triggering the collapse of mitochondrial membrane potential and loss of mitochondrial function that leads to energy depletion and cell death . ALKBH7-mediated necrosis is probably required to prevent the accumulation of cells with DNA damage . Does not display DNA demethylase activity . Involved in fatty acid metabolism (By similarity). Sequence Mass (Da): 24516 Sequence Length: 221 Subcellular Location: Mitochondrion matrix EC: 1.14.11.-

Q9D6Z0

MAGSRRLAMRLLSGCAWVRGSDSAVLGRLRDEAVVHPGFLSQEEEDTLTRELEPQLRRRRYEYDHWDAAIHGFRETEKSCWSDASQVILQRVRAAAFGPDQSLLSPVHVLDLEPRGYIKPHVDSVKFCGSTIAGLSLLSPSVMKLVHTQEPEQWLELLLEPGSLYILRGSARYDFSHEILRDEESFFGEHRVPRGRRISVICRSLPEGMGPGRPEEPPPAC

Cofactor: Binds 1 Fe(2+) ion per subunit. Function: May function as protein hydroxylase; can catalyze auto-hydroxylation at Leu-110 (in vitro), but this activity may be due to the absence of the true substrate. Required to induce programmed necrosis in response to DNA damage caused by cytotoxic alkylating agents. Acts by triggering the collapse of mitochondrial membrane potential and loss of mitochondrial function that leads to energy depletion and cell death. ALKBH7-mediated necrosis is probably required to prevent the accumulation of cells with DNA damage. Does not display DNA demethylase activity (By similarity). Involved in fatty acid metabolism. Sequence Mass (Da): 24970 Sequence Length: 221 Subcellular Location: Mitochondrion matrix EC: 1.14.11.-

Q8RWY1

MVQPRFVRPTQSSPSSISGEPNSSNLYVANCGPAVGLTHNAIAAVFAEFGEVNGVYAADDSGVRVIVSFADPFSAKAALEALSGRPCPDLKGRSLHIRYSVLQLPSETQVNDCVPVSLIDSELNIPGLFLLPDFVTVAEEQQLLAAVDARHWIGLAKRRVQHYGYEFCYGTRNVDTKKRLGELPSFVSPILERIYLFPNFDNGSASLNLDQLTVNEYPSGVGLSPHIDTHSAFEDCIFSLSLAGPCIMEFRRYSVSTWKASTTDAEKSGDSSCIKKALYLPPRSMLLLSGEARYAWNHYIPHHKIDKVKDKVIRRSSRRVSFTLRKVRNHPCSCKYPQYCDSQQQM

Cofactor: Binds 1 Fe(2+) ion per subunit. Function: Binds tRNA and catalyzes the iron and alpha-ketoglutarate dependent hydroxylation of 5-methylcarboxymethyl uridine at the wobble position of the anticodon loop in tRNA via its dioxygenase domain, giving rise to 5-(S)-methoxycarbonylhydroxymethyluridine. Sequence Mass (Da): 38424 Sequence Length: 346 EC: 1.14.11.-

Q96BT7

MDSNHQSNYKLSKTEKKFLRKQIKAKHTLLRHEGIETVSYATQSLVVANGGLGNGVSRNQLLPVLEKCGLVDALLMPPNKPYSFARYRTTEESKRAYVTLNGKEVVDDLGQKITLYLNFVEKVQWKELRPQALPPGLMVVEEIISSEEEKMLLESVDWTEDTDNQNSQKSLKHRRVKHFGYEFHYENNNVDKDKPLSGGLPDICESFLEKWLRKGYIKHKPDQMTINQYEPGQGIPAHIDTHSAFEDEIVSLSLGSEIVMDFKHPDGIAVPVMLPRRSLLVMTGESRYLWTHGITCRKFDTVQASESLKSGIITSDVGDLTLSKRGLRTSFTFRKVRQTPCNCSYPLVCDSQRKETPPSFPESDKEASRLEQEYVHQVYEEIAGHFSSTRHTPWPHIVEFLKALPSGSIVADIGCGNGKYLGINKELYMIGCDRSQNLVDICRERQFQAFVCDALAVPVRSGSCDACISIAVIHHFATAERRVAALQEIVRLLRPGGKALIYVWAMEQEYNKQKSKYLRGNRNSQGKKEEMNSDTSVQRSLVEQMRDMGSRDSASSVPRINDSQEGGCNSRQVSNSKLPVHVNRTSFYSQDVLVPWHLKGNPDKGKPVEPFGPIGSQDPSPVFHRYYHVFREGELEGACRTVSDVRILQSYYDQGNWCVILQKA

Cofactor: Binds 1 Fe(2+) ion per subunit. Function: Catalyzes the methylation of 5-carboxymethyl uridine to 5-methylcarboxymethyl uridine at the wobble position of the anticodon loop in tRNA via its methyltransferase domain . Catalyzes the last step in the formation of 5-methylcarboxymethyl uridine at the wobble position of the anticodon loop in target tRNA . Has a preference for tRNA(Arg) and tRNA(Glu), and does not bind tRNA(Lys). Binds tRNA and catalyzes the iron and alpha-ketoglutarate dependent hydroxylation of 5-methylcarboxymethyl uridine at the wobble position of the anticodon loop in tRNA via its dioxygenase domain, giving rise to 5-(S)-methoxycarbonylhydroxymethyluridine; has a preference for tRNA(Gly) . Required for normal survival after DNA damage . May inhibit apoptosis and promote cell survival and angiogenesis . Catalytic Activity: 5-(carboxymethyl)uridine(34) in tRNA + S-adenosyl-L-methionine = 5-(2-methoxy-2-oxoethyl)uridine(34) in tRNA + S-adenosyl-L-homocysteine Sequence Mass (Da): 75208 Sequence Length: 664 Subcellular Location: Cytoplasm

Q80Y20

MNINHKGVLKLTKMEKKFLRKQSKARHVLLKHEGIQAVSYPTQSLVIANGGLGNGVSRKQLLLTLEKCGPVEALLMPPNKPYAFVIFQTIEESKKAYFTLNGKEIIDDLGQKIFLYLNFVEKAQWKNMGLEALPPGLLVVEEIISSEEEKKLLESVNWTEDTGNQNFQRSLKHRRVKHFGYEFHYESNTVDKDKPLPGGLPEVCSSILEKLLKEGYIKHKPDQLTINQYEPGHGIPAHIDTHSAFEDEIISLSLGSAIVMDFKHPEGVTVQVMLPRRSLLVMTGESRYLWTHGITPRKFDTVQASEQFKGGIITSDIGDLTLSKRGMRTSFTFRKVRRMPCNCSYSSVCDRQRKATPPSLTESSKEALELEQKHVHQVYNEIASHFSSTRHSPWPRIVEFLKALPSGSIVADIGCGNGKYLGINKDLYMIGCDRSQNLVDICRERQFQALVCDALAVPVRSGSCDACISIAVIHHFATAERRVEALQELARLLRPGGQALIYVWAMEQEYKNQKSKYLRGKRISQGDKDELNSATSTEEFLVNQTPEGVNEDPALSVNSSSITKEEEYKSRKVPNSELPIHINRTCFHSQDVLVPWHLKRNPGKDKAIEPSGVAGCPDPSPVFHRYYHVFCDGELEASCQAVGDVSILQSYYDQGNWCVVLQKV

Cofactor: Binds 1 Fe(2+) ion per subunit. Function: Catalyzes the methylation of 5-carboxymethyl uridine to 5-methylcarboxymethyl uridine at the wobble position of the anticodon loop in tRNA via its methyltransferase domain . Catalyzes the last step in the formation of 5-methylcarboxymethyl uridine at the wobble position of the anticodon loop in target tRNA . Has a preference for tRNA(Arg) and tRNA(Glu), and does not bind tRNA(Lys) (By similarity). Binds tRNA and catalyzes the iron and alpha-ketoglutarate dependent hydroxylation of 5-methylcarboxymethyl uridine at the wobble position of the anticodon loop in tRNA via its dioxygenase domain, giving rise to 5-(S)-methoxycarbonylhydroxymethyluridine; has a preference for tRNA(Gly) . Required for normal survival after DNA damage (By similarity). May inhibit apoptosis and promote cell survival and angiogenesis (By similarity). Catalytic Activity: 5-(carboxymethyl)uridine(34) in tRNA + S-adenosyl-L-methionine = 5-(2-methoxy-2-oxoethyl)uridine(34) in tRNA + S-adenosyl-L-homocysteine Sequence Mass (Da): 74768 Sequence Length: 664 Domain: The Fe2OG dioxygenase domain does not have demethylase activity with methylated nucleotides. Subcellular Location: Cytoplasm

Q07G10

MGSIDGTRPKLSKDNKKLLKKQAKAKHILLKHEGIETVLHLSQSLVVANGGLGNGVSRQQLLAVLERCGKVETLLMPPNKPYAFVTYSSAEEAIKAYSSLSGQELCGEDAEQPITLYLSFVEKVVVKEVLSPSLPPGLIIVEDFVSPEQERTMLESIDWDSETSSQKSLKHRQVKHYGYEFRYDNNNVDKDKPLPGGLPDFCTEALRKCVQRGLIKHDPDQLTINQYEPGQGIPPHVDTHSAFEDEILSLSLGAEIVMDFKHPNGSVVPVMLPQRSLLIMSGESRYLWTHGITPRKFDVIQVSEGQTVGTISGNSGELTLSKRSTRTSFTFRKVRHSPCDCAFPSECDSQQTQKEKSPPTVGELGASTLEREYVHKVYDDIAGHFSSTRHTPWPKIGDFLASLPKGSLVADVGCGNGKYLGVNKDLCMIGCDRSKNLVDICRERTFEAFVCDALSVPFRAGAFDACISIAVIHHFATEERRIAALQELIRLLRKGGKALIYVWALEQEYKKNKSKYLKESKTSQGPSSDALGTNLAVKAPLPIHTNRTSFHSQDLLVPWHLKPTNKSKVTPENKEQNEKEHGPDSVYHRFYHVFCEGELEAMCNRLSNVAVQHSYHDQGNWCVILEKL

Cofactor: Binds 1 Fe(2+) ion per subunit. Function: Catalyzes the methylation of 5-carboxymethyl uridine to 5-methylcarboxymethyl uridine at the wobble position of the anticodon loop in tRNA via its methyltransferase domain. Catalyzes the last step in the formation of 5-methylcarboxymethyl uridine at the wobble position of the anticodon loop in target tRNA. Has a preference for tRNA(Arg) and tRNA(Glu), and does not bind tRNA(Lys). Binds tRNA and catalyzes the iron and alpha-ketoglutarate dependent hydroxylation of 5-methylcarboxymethyl uridine at the wobble position of the anticodon loop in tRNA via its dioxygenase domain, giving rise to 5-(S)-methoxycarbonylhydroxymethyluridine; has a preference for tRNA(Gly). Required for normal survival after DNA damage. May inhibit apoptosis and promote cell survival and angiogenesis (By similarity). Catalytic Activity: 5-(carboxymethyl)uridine(34) in tRNA + S-adenosyl-L-methionine = 5-(2-methoxy-2-oxoethyl)uridine(34) in tRNA + S-adenosyl-L-homocysteine Sequence Mass (Da): 70022 Sequence Length: 628 Subcellular Location: Cytoplasm

Q9SA98

MYESANVSDDADRTAFRRAEKKYKLYYEQDSKFSRKKKLPKPIDLSELLDFNLISQNFNNDGVLPDGIRVSKVDSSPVFCIDNRPGFYFIPDALSLKEQCKWIKESLTSFPQPPNRTNHNAIYGPIDDLFDSAKENKVLVQDDLTNNKWKFYEEVDIEKATRSSCKSVSASVLLRKLRWSTLGLQFDWSKRNYDVSLPHNNIPDALCQLAKTHAAIAMPDGEEFRPEGAIVNYFGIGDTLGGHLDDMEADWSKPIVSMSLGCKAIFLLGGKSKDDPPHAMYLRSGDVVLMAGEARECFHGIPRIFTGEENADIGALESELSHESGHFFAEYIKTSRININIRQVF

Cofactor: Binds 1 Fe(2+) ion per subunit. Function: Putative dioxygenase that may repair alkylated DNA or RNA by oxidative demethylation. Requires molecular oxygen, alpha-ketoglutarate and iron (By similarity). Sequence Mass (Da): 39020 Sequence Length: 345 EC: 1.14.11.-

O60066

MLAGNMEQANVFRLEEKRYKCRADTIPDMSEVLDPNDPQSFGFEALVEIKPRVFSFQKAPGLLILKNYVSSELQMQLLKSIMFTQIQDPENKTNLSPFYQLPLGNDSIWRRYYNGDGESIIDGLGETKPLTVDRLVHKKLRWVTLGEQYDWTTKEYPDPSKSPGFPKDLGDFVEKVVKESTDFLHWKAEAAIVNFYSPGDTLSAHIDESEEDLTLPLISLSMGLDCIYLIGTESRSEKPSALRLHSGDVVIMTGTSRKAFHAVPKIIPNSTPNYLLTGNKAWDGWISRKRVNFNVRQVRPSR

Cofactor: Binds 1 Fe(2+) ion per subunit. Function: Putative dioxygenase that may repair alkylated DNA or RNA by oxidative demethylation. Requires molecular oxygen, alpha-ketoglutarate and iron (By similarity). Sequence Mass (Da): 34348 Sequence Length: 302 EC: 1.14.11.-

O31250

MNAPVHVDQNFEEVINAARSMREIDRKRYLWMISPALPVIGIGILAGYQFSPRPIKKIFALGGPIVLHIIIPVIDTIIGKDASNPTSEEIKQLENDPYYARLVKSFIPLQYIANVYACYLVSRKKTSFIDKILLGISMGAINGIAVNTAHELSHKADRLDHILSHLALVPTGYNHFRIEHPYGHHKRAATPEDPASSQMGETFYEFWPRTVFGSLKSAIEIETHRLKRKGKKFWSKDNELLQGWGMSAAFHSSIIAIFGKGTIPYLVTQAFYGISLFEIINYIEHYGLKRQKRADGNYERTMPEHSWNNNNIVTNLFLYQLQRHSDHHAYPTRPFQALRHFDEAPELPSGYASMLLPAMIPPLWFKMMDKRVFEHYKEDLTKANIYPKRRAKILAKFGLTDPNIENGK

Cofactor: Binds 2 Fe(3+) ions per subunit. Function: Catalyzes the hydroxylation of n-alkanes in the presence of a NADH-rubredoxin reductase and rubredoxin. It preferably hydroxylases long-chain-length alkanes with at least 12 carbon atoms. Catalytic Activity: 2 H(+) + O2 + octane + 2 reduced [rubredoxin] = H2O + octan-1-ol + 2 oxidized [rubredoxin] Location Topology: Multi-pass membrane protein Sequence Mass (Da): 46759 Sequence Length: 408 Pathway: Hydrocarbon metabolism; alkane degradation. Subcellular Location: Cell inner membrane EC: 1.14.15.3

P0CAT7

MAVVRRAVAARGLQMIAKPLTVVPGFDVWPGLLDISAQRALVEAVLAGAEQAPFSNYRTAYGKPMSVAMTALGSLGWTSDARGYRYVDRHPETGRPWPDMPPALLDLWTVLGDPETPPDSCLVNLYRDGARMGLHQDRDEADPRFPVLSISLGDTAVFRIGGVNRKDPTRSLRLASGDVCRLLGPARLAFHGVDRILPGSSSLVPGGGRINLTLRRARTA

Cofactor: Binds 1 Fe(2+) ion per subunit. Function: Dioxygenase that repairs alkylated DNA and RNA containing 3-methylcytosine or 1-methyladenine by oxidative demethylation. Has highest activity towards 3-methylcytosine. Has lower activity towards alkylated DNA containing ethenoadenine, and no detectable activity towards 1-methylguanine or 3-methylthymine. Accepts double-stranded and single-stranded substrates. Requires molecular oxygen, alpha-ketoglutarate and iron. Provides extensive resistance to alkylating agents such as MMS and DMS (SN2 agents), but not to MMNG and MNU (SN1 agents) (By similarity). Catalytic Activity: 2-oxoglutarate + a methylated nucleobase within DNA + O2 = a nucleobase within DNA + CO2 + formaldehyde + succinate Sequence Mass (Da): 23764 Sequence Length: 220 EC: 1.14.11.33

Q54N08

MYETEEDPTTSNVATTNNEKTASTAATTTEPVKKVTEFMRVQRLFRQVTKSANGKNIPKEKREPIDYSPVLDFHNLENNTEENKKLIIDCTSNVTTHDFEFNRDTEFYLHPREWKVYGLQGYPGFYFIKSPFTASQQKKWIKHALEDYADPPNNNNITLFHGPIKNLWKNGEKELINEELKSQGKHDDDEIEQPTRPLDKNGEPLPTYRQLLDKLAWSTLGYQYQWTPRLYSEEFYEEFPDDLQELVQKIAIATKFDPYVAEAATVNFYSEDSIMGGHLDDAEQEMEKPIISISFGSTAVFLMGAETRDIAPVPLFIRSGDIVIMGGRSRYCYHGVAKIVENSFDLGLIDENDDQDLKYKIQWLKEKNRRVNINTRQVFKVPKLGGKLINKNE

Cofactor: Binds 1 Fe(2+) ion per subunit. Function: Putative dioxygenase that may repair alkylated DNA or RNA by oxidative demethylation. Requires molecular oxygen, alpha-ketoglutarate and iron (By similarity). Sequence Mass (Da): 45446 Sequence Length: 393 EC: 1.14.11.-

P05050

MLDLFADAEPWQEPLAAGAVILRRFAFNAAEQLIRDINDVASQSPFRQMVTPGGYTMSVAMTNCGHLGWTTHRQGYLYSPIDPQTNKPWPAMPQSFHNLCQRAATAAGYPDFQPDACLINRYAPGAKLSLHQDKDEPDLRAPIVSVSLGLPAIFQFGGLKRNDPLKRLLLEHGDVVVWGGESRLFYHGIQPLKAGFHPLTIDCRYNLTFRQAGKKE

Cofactor: Binds 1 Fe(2+) ion per subunit. Function: Dioxygenase that repairs alkylated DNA and RNA containing 3-methylcytosine or 1-methyladenine by oxidative demethylation. Has highest activity towards 3-methylcytosine. Has lower activity towards alkylated DNA containing ethenoadenine, and no detectable activity towards 1-methylguanine or 3-methylthymine. Accepts double-stranded and single-stranded substrates. Requires molecular oxygen, alpha-ketoglutarate and iron. Provides extensive resistance to alkylating agents such as MMS and DMS (SN2 agents), but not to MMNG and MNU (SN1 agents). Catalytic Activity: 2-oxoglutarate + a methylated nucleobase within DNA + O2 = a nucleobase within DNA + CO2 + formaldehyde + succinate Sequence Mass (Da): 24076 Sequence Length: 216 EC: 1.14.11.33

P12691

MLEKHRVLDSAPEYVDKKKYLWILSTLWPATPMIGIWLANETGWGIFYGLVLLVWYGALPLLDAMFGEDFNNPPEEVVPKLEKERYYRVLTYLTVPMHYAALIVSAWWVGTQPMSWLEIGALALSLGIVNGLALNTGHELGHKKETFDRWMAKIVLAVVGYGHFFIEHNKGHHRDVATPMDPATSRMGESIYKFSIREIPGAFIRAWGLEEQRLSRRGQSVWSFDNEILQPMIITVILYAVLLALFGPKMLVFLPIQMAFGWWQLTSANYIEHYGLLRQKMEDGRYEHQKPHHSWNSNHIVSNLVLFHLQRHSDHHAHPTRSYQSLRDFPGLPALPTGYPGAFLMAMIPQWFRSVMDPKVVDWAGGDLNKIQIDDSMRETYLKKFGTSSAGHSSSTSAVAS

Cofactor: Binds 2 Fe(3+) ions per subunit. Function: Catalyzes the hydroxylation of n-alkanes and fatty acids in the presence of a NADH-rubredoxin reductase and rubredoxin. Catalytic Activity: 2 H(+) + O2 + octane + 2 reduced [rubredoxin] = H2O + octan-1-ol + 2 oxidized [rubredoxin] Location Topology: Multi-pass membrane protein Sequence Mass (Da): 45806 Sequence Length: 401 Pathway: Hydrocarbon metabolism; alkane degradation. Subcellular Location: Cell inner membrane EC: 1.14.15.3

P37462

MLDLFADEAPWQEPLAPGAVVLRRFAFRAAQSLLDDIGFVASQSPFRQMVTPGGYTMSVAMTNCGALGWTTDRHGYCYAVRDPLTDKPWPALPLSFASVCRQAAIAAGYASFQPDACLINRYAPGAKLSLHQDKDEPDLRAPIVSVSLGVPAVFQFGGLRRSDPIQRILLEHGDIVVWGGESRLFYHGIQPLKAGFHPMTGEFRYNLTFRQAAEKE

Cofactor: Binds 1 Fe(2+) ion per subunit. Function: Dioxygenase that repairs alkylated DNA and RNA containing 3-methylcytosine or 1-methyladenine by oxidative demethylation. Has highest activity towards 3-methylcytosine. Has lower activity towards alkylated DNA containing ethenoadenine, and no detectable activity towards 1-methylguanine or 3-methylthymine. Accepts double-stranded and single-stranded substrates. Requires molecular oxygen, alpha-ketoglutarate and iron. Provides extensive resistance to alkylating agents such as MMS and DMS (SN2 agents), but not to MMNG and MNU (SN1 agents) (By similarity). Catalytic Activity: 2-oxoglutarate + a methylated nucleobase within DNA + O2 = a nucleobase within DNA + CO2 + formaldehyde + succinate Sequence Mass (Da): 23787 Sequence Length: 216 EC: 1.14.11.33

O32149

MEKQKLSVKNSITDYIEWLAQYGASADGGVTRLLYTKEWMDAQLAVKTEMSSFGLETRFDDVGNVFGRLSGTQSPDEVIVTGSHIDTVINGGKYDGAYGVLAAMLALKQLKETYGAPKKTLEAVSLCEEEGSRFPMTYWGSGNMTGVFSEQDAKEPRDESGVSLQTAMHESGFGKGVFQSAYRTDISAFVELHIEQGKTLEMSGRDLGIVTSIAGQRRYLVTLEGECNHAGTTSMKWRKDPLAASSRIIHELLLRSDELPDELRLTCGKITAEPNVANVIPGRVQFSIDIRHQHQHVLEQFHQDMVALINGICLQKGIRAVIDEYMRIEPVPMDERLKAAAFETALENGFSCEEMVSGAGHDAQMIGRRYPACMLFVPSRGGVSHSPKEYTSARQLEIGVRALTDLLYKLAY

Cofactor: Binds 2 Zn(2+) ions per subunit. Function: Involved in the anaerobic nitrogen utilization via the assimilation of allantoin . Catalyzes specifically the hydrolysis of allantoate to yield CO2, NH3 and S-ureidoglycine, which is unstable and readily undergoes a second deamination by S-ureidoglycine aminohydrolase AllE to yield S-ureidoglycolate and NH3 (By similarity). Catalytic Activity: allantoate + 2 H(+) + H2O = (S)-2-ureidoglycine + CO2 + NH4(+) Sequence Mass (Da): 45520 Sequence Length: 412 Pathway: Nitrogen metabolism; (S)-allantoin degradation. Subcellular Location: Cytoplasm EC: 3.5.3.9

P82678

MASTSHNPFYAAMQPQAQHWGATSPTSTGAGYDRPSAGYPAYTGYAAAGTSHPAPSSSSPSTALALYNPSSLYGLYYNEAVHGPFATGLQSNPFTPGLAPLSTVSRPSYATEDPLRQRYPATSANPHDPLNWITEDLFAIRMERAAISQQRTPLRSASVAAR

Function: Catalyzes the degradation of allantoate to (-)-ureidoglycolate and (+)-ureidoglycolate to glyoxylate. Catalytic Activity: allantoate + H2O = (S)-ureidoglycolate + urea Sequence Mass (Da): 17207 Sequence Length: 162 Pathway: Nitrogen metabolism; (S)-allantoin degradation; (S)-ureidoglycolate from allantoate (aminidohydrolase route): step 1/1. EC: 3.5.3.4

Q6DGA6

MAKRQVQKETRSQPHFLQFNNLACETAGGKVIFATDEWFAPARNLLKRDPPEFIASAFTEFGKWMDGWETRRKRIPGHDWCIVQLGVPGIIHGFDVDTSFFTGNYAPFASIQATCLDQMPSIALEGDRTGMAASPSQFEAVAQLNSDSWKEVVPVTKLKAGYSDTCHNYLSVSYPHRVTHIRFNIYPDGGIARLKVYGIGKKDWSSVFGQDLVDLVALVNGGVCVGFSDAHYGHPRNMIGLGMAENMGDGWETARRLDRPRVLKEDENGILQVPGSEWAIFRLGHPGIISKIELDTNHFKGNFPDSCRIEACSLTEDEENSFIQSQWSSDRSPMWNILLPPQKMKAHHRHVFSGPSLVHCGPVSHVRMVIAPDGGISRLRIWGRPVSSHQMISKL

Function: Utilization of purines as secondary nitrogen sources, when primary sources are limiting. Catalytic Activity: allantoate + H2O = (S)-ureidoglycolate + urea Sequence Mass (Da): 44144 Sequence Length: 395 Pathway: Nitrogen metabolism; (S)-allantoin degradation; (S)-ureidoglycolate from allantoate (aminidohydrolase route): step 1/1. EC: 3.5.3.4

Q54VL5

MVYANNNIDPNAPCYVSECAELLSDKVGGVVLGCTDQWFAECVNLIKHSAPVWDAEKYVDTGKWMDGWETKRHNPDHDWCIIKLGIPGVIYGFEIDTAYFTGNYPPHASIEALCDDSDPNFNTLKESNNWEVILNKSDLGSSCKKYFECKVEKRFTHIKFRIYPDGGVARLRAYGRVVKDWTLVIPGELVDLAAIENGGLVTQVSDHFYGNKNNIIMPGRSVNMGDGWETKRRRGPGNDWLTVKLAKEGIVKRIEVDTNWFKGNFPTSCSIDAIHSSSAPDETHLQDYEWTNILPNSPLCGHRRHFFQNELVNNDKPFTHIRLNIFPDGGVSRLRINCSLPDSKNNNNNNNNNNNNNTSNSFKTSDRQQ

Function: Utilization of purines as secondary nitrogen sources, when primary sources are limiting. Catalytic Activity: allantoate + H2O = (S)-ureidoglycolate + urea Sequence Mass (Da): 41778 Sequence Length: 369 Pathway: Nitrogen metabolism; (S)-allantoin degradation; (S)-ureidoglycolate from allantoate (aminidohydrolase route): step 1/1. EC: 3.5.3.4

P77425

MITHFRQAIEETLPWLSSFGADPAGGMTRLLYSPEWLETQQQFKKRMAASGLETRFDEVGNLYGRLNGTEYPQEVVLSGSHIDTVVNGGNLDGQFGALAAWLAIDWLKTQYGAPLRTVEVVAMAEEEGSRFPYVFWGSKNIFGLANPDDVRNICDAKGNSFVDAMKACGFTLPNAPLTPRQDIKAFVELHIEQGCVLESNGQSIGVVNAIVGQRRYTVTLNGESNHAGTTPMGYRRDTVYAFSRICHQSVEKAKRMGDPLVLTFGKVEPRPNTVNVVPGKTTFTIDCRHTDAAVLRDFTQQLENDMRAICDEMDIGIDIDLWMDEEPVPMNKELVATLTELCEREKLNYRVMHSGAGHDAQIFAPRVPTCMIFIPSINGISHNPAERTNITDLAEGVKTLALMLYQLAWQK

Cofactor: Binds 2 Zn(2+) ions per subunit . Also able to bind Mn(2+) . Function: Involved in the anaerobic nitrogen utilization via the assimilation of allantoin . Catalyzes specifically the hydrolysis of allantoate to yield CO2, NH3 and S-ureidoglycine, which is unstable and readily undergoes a second deamination by S-ureidoglycine aminohydrolase AllE to yield S-ureidoglycolate and NH3 . In vivo, the spontaneous release of S-ureidoglycolate and ammonia from S-ureidoglycine appears to be too slow to sustain an efficient flux of nitrogen . Catalytic Activity: allantoate + 2 H(+) + H2O = (S)-2-ureidoglycine + CO2 + NH4(+) Sequence Mass (Da): 45694 Sequence Length: 411 Pathway: Nitrogen metabolism; (S)-allantoin degradation. Subcellular Location: Cytoplasm EC: 3.5.3.9

P18407

MTDIDYKLEAVPATRIAADDIDKTFRSSTIDLISGALGGKVLGFSDEWFAEAANLLTPTAPIRQPGKMVYTGAWYDGWETRRHNPAEFDWVVIRLGVASGTVEGVEIDTAFFNGNHAPAISVEGCFSQNDDEVLSWKGERGGWETILGVQECGPSQRFGWKLENPTKKQYTHVRLNMYPDGGIARFRLFGHAVPVFPDNTDAIFDLAAAQNGGVAISCSDQHFGTKDNLILPGRGKDMGDGWETARSRTKGHVDWTIIRLGAPGYIQNFMVDTAHFRGNYPQQVKLQAIEWKSEGEPGADSEGWTEVVEPIKCGPDQEHPVESLVKDKPFTHVKLIIVPDGGVKRLRVFAKRAV

Function: Utilization of purines as secondary nitrogen sources, when primary sources are limiting. Catalytic Activity: allantoate + H2O = (S)-ureidoglycolate + urea Sequence Mass (Da): 39073 Sequence Length: 354 Pathway: Nitrogen metabolism; (S)-allantoin degradation; (S)-ureidoglycolate from allantoate (aminidohydrolase route): step 1/1. EC: 3.5.3.4

Q5YP02

MNETAADRVAPRGFTELPDLAVRSLGGAVIWADDEFFAEKENLIVPEAPEFRPATYGHRGQVYDGWETRRHRGLPGDDAAVVRLGVPGVIHGVVVDTSWFTGNYPPAISLSALAIDGYPPAADIAARTDWVPLLDRVPVRGDARNPFPIPSRDRWTHVRLTMHPDGGIARLRVHGEGRPDPALLGLGPVDLAALENGALVLDCSDRFYGSPHQLLHPGNARRMGDGWETARRRDDGNDWVRIRLAGPGLIRLAELDTSYFLGNSPAAARLTGRTTDGTEVELLPRTPLQPDTRHRFPTAAVAASVEEVRLDIYPDGGLARVRLFGELGG

Catalytic Activity: allantoate + H2O = (S)-ureidoglycolate + urea Sequence Mass (Da): 35822 Sequence Length: 329 Pathway: Nitrogen metabolism; (S)-allantoin degradation; (S)-ureidoglycolate from allantoate (aminidohydrolase route): step 1/1. EC: 3.5.3.4

Q55320

MKIKLLCISLAVLFCSSANAQKKQAKVQPSVFPQTVARPKLVVGMVIDQMRWDYLYRFYARYGNGGFKRLINEGFSAENTLIPYTPTLTACGHSSIYTGSVPAINGIIGNNWFDPQLGRDVYCVEDKSVKTVGSSSNEGLMSPKNLLVTTVTDELRMATNFRSKVISVSIKDRGAILPGGHTANGAYWYDDMTGSFISSTHYMQQLPTWVNDFNAQRLPNKYFEQDWNTLYPIETYTESTADAKPYERTFKGAKTSSFPHLFKQYANKNYSMMASMPQGNSFTLEFAKAAIPAEKLGQTGNTDFLAVSLSSTDYVGHQFGPNSIELEDTYLRLDKDLEDFFNYLDKTIGKGNYLLFLTADHGATHVPGFLRNKMPGGRLLLKVQTDLDSLIFNEFKVRCNFTIINNQVIFDTDAIKEAKADYAKIKQSTIDYLVKQDGVLNAVDIKNMGAVTIPQEIKNKIINGYNARRSGDVYIILDAGWYPTLTPGTGHAAWNPYDSHIPALFMGWGVKPGKTNKEYYMSDIAPTVSALLHIQQPSGSIGKVITDLLK

Cofactor: Binds 2 Zn(2+) ions. Function: Alkaline phosphatase with broad substrate specificity. Catalytic Activity: a phosphate monoester + H2O = an alcohol + phosphate Location Topology: Lipid-anchor Sequence Mass (Da): 61325 Sequence Length: 550 Subcellular Location: Cell inner membrane EC: 3.1.3.1

Q5NNZ8

MNSLLHHSFLKTVFSSLAIAIVTSSLSSVTIAATHPLDNHPKGEIAASSETAHNPWSGTRLIVAISVDQFSSDLFSEYRGRFRSGMKQLQNGVVYPMAYHSHAATETCPGHSVLLTGDHPARTGIIANNWYDFSVKRADKKVYCSEDPSLSADPQNYQPSVHYLKVPTLGDRMKKANPHSRVISVAGKDRAAIMMGGHMTDQIWFWSDNAYKTLADHKGEMPVTVKTVNEQVTRFMQQDEAPVMPSVCADHASALKIGNNRIIGLAPASRKAGDFKTFRVTPDYDRTTTDIAIGLIDELKLGHGNAPDLLTVSLSATDAVGHAYGTEGAEMCSQMAGLDDNIARIIAALDSNGVPYVLVLTADHGGQDVPERAKLRGVETAQRVDPALSPDQLSLRLAERFQLSHNQPLFFANEPQGDWYINRNLPEQTKAQLIQAAKSELSNHPQVAAVFTASELTHIPYPTRSPELWNLAERAKASFDPLRSGDLIVLLKPRVTPIAKPVSYVATHGSAWDYDRRVPIIFYTPHASGFEQPMPVETVDIMPSLAALLQIPLRKGEVDGRCLDLDPTEATTCPVK

Cofactor: Binds 2 Zn(2+) ions. Function: Alkaline phosphatase with broad substrate specificity. Has phosphatase activity towards nucleotide and sugar phosphates with a preference to nucleotide phosphates. Has no phosphodiesterase activity. Catalytic Activity: a phosphate monoester + H2O = an alcohol + phosphate Sequence Mass (Da): 63011 Sequence Length: 576 EC: 3.1.3.1

Q9M2U3

MGPIKTIKKKKRAEKKVDRNVLLAATAAATSASAAAALNNNDDDDDSSSQSLDWWDGFSRRIYGGSTDPKTFESVFKISRKTFDYICSLVKADFTAKPANFSDSNGNPLSLNDRVAVALRRLGSGESLSVIGETFGMNQSTVSQITWRFVESMEERAIHHLSWPSKLDEIKSKFEKISGLPNCCGAIDITHIVMNLPAVEPSNKVWLDGEKNFSMTLQAVVDPDMRFLDVIAGWPGSLNDDVVLKNSGFYKLVEKGKRLNGEKLPLSERTELREYIVGDSGFPLLPWLLTPYQGKPTSLPQTEFNKRHSEATKAAQMALSKLKDRWRIINGVMWMPDRNRLPRIIFVCCLLHNIIIDMEDQTLDDQPLSQQHDMNYRQRSCKLADEASSVLRDELSDQLCGKNSSA

Function: Transposase-derived protein that may have nuclease activity. Sequence Mass (Da): 45467 Sequence Length: 406 Subcellular Location: Nucleus EC: 3.1.-.-

P83610

GSTSYIYDTSAGSGTYAYIVDTGIITSHNGFNWAANDIISKSYSNYGTVLDIFAPGTSVLSS

Function: Serine protease. May be involved in the invasion of grains and hydrolyzation of grain proteins. Sequence Mass (Da): 6493 Sequence Length: 62 Subcellular Location: Secreted EC: 3.4.21.-

P58736

MTDDFEDSFPDNETDAFEQAPLRLTVDLGALADNWRDMKKRSGRARTAAVVKADAYGLGIEDCGATLYHAGARDFFVATVAEGATLRSYAPEARIFVLSGIWQGQERQVFDNDLVPVLASEEQLSFWMATVAERGDHPCALHVDTGFNRLGLPLDDALFLADDVTRPASFDPVLVLSHLACADTPSSPMNRAQLESFRRVSAAFEGIESSLSASAGIFLGPDYHFDLTRPGIALYGGEAVNDVANPMRPVAKAEARIIQIREAGEGQTVSYGSSFLLKRASRLAIASVGYADGYQRSLSGSGIPLREMGHGGAYGVVNGHKVPVAGRVTMDLTIFDVTDVPANAIRAGDYIELFGPNVPVDETARAAGTIGYEMLTGLGLRYERQYLVADD

Function: Catalyzes the interconversion of L-alanine and D-alanine. Provides the D-alanine required for cell wall biosynthesis (By similarity). Catalytic Activity: L-alanine = D-alanine Sequence Mass (Da): 42091 Sequence Length: 391 Pathway: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1. EC: 5.1.1.1

P10725

MSTKPFYRDTWAEIDLSAIKENVSNMKKHIGEHVHLMAVVKANAYGHGDAETAKAALDAGASCLAVAILDEAISLRKKGLKAPILVLGAVPPEYVAIAAEYDVTLTGYSVEWLQEAARHTKKGSLHFHLKVDTGMNRLGVKTEEEVQNVMAILDRNPRLKCKGVFTHFATADEKERGYFLMQFERFKELIAPLPLKNLMVHCANSAAGLRLKKGFFNAVRFGIGMYGLRPSADMSDEIPFQLRPAFTLHSTLSHVKLIRKGESVSYGAEYTAEKDTWIGTVPVGYADGWLRKLKGTDILVKGKRLKIAGRICMDQFMVELDQEYPPGTKVTLIGRQGDEYISMDEIAGRLETINYEVACTISSRVPRMFLENGSIMEVRNPLLQVNISN

Function: Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids. Catalytic Activity: L-alanine = D-alanine Sequence Mass (Da): 43265 Sequence Length: 389 Pathway: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1. EC: 5.1.1.1

Q8EAI6

MKPFPRAEISSSALQNNLAVLRQQASSSQVMAVVKANGYGHGLLNVAKCLNNADGFGLARLEEALELRAGSVKARLLLLEGFFRSTDLPLLVEHDIDTVVHHESQIEMLEQATLSKPVTVWLKVDSGMHRLGVTPEQFSAVYARLTACKNVAKPIHLMTHFACADEPDNHYTQVQMQTFNQLTADLPGFRTLANSAGALYWPKSQGDWIRPGIAMYGVSPVTGDCGANHGLIPAMNLVSRLIAVREHKANQPVGYGCYWTAKQDTRLGVVAIGYGDGYPRNAPEGTPVWINGRRVPIVGRVSMDMLTVDLGHDATDQVGDDVLLWGQALPVEEVAEHIGTIAYELVTKLTPRVAVCLA

Function: Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids. Catalytic Activity: L-alanine = D-alanine Sequence Mass (Da): 38942 Sequence Length: 358 Pathway: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1. EC: 5.1.1.1

Q2NTA8

MPRPIVAKVDSAVLASNLSIVRRHAPQAQVWSVVKANGYGHGLNTVWQGLQQTDGFALLDLHEAVVLREKGWRGPILLLEGFFQPADLAVIDRYRLTTVVHSDWQIEALRRMTPRAPLDIYLKLNSGMNRLGFSERALPGAWQSLNALKHVATLTLMSHFAYADMPEGVEGQMAVVARAGEGLTGPRCLANSAATLWHPATHGQWVRPGIILYGASPSGNWQDIAASGLRPVMTLQSELIAVQSVPAGGRIGYGGRHRVSETHRVGVVACGYADGYPRHAPTGTPILVDGVRTSTLGAVSMDMLMVDLQLCPKARIGSAVELWGDHVKIDEVAASAGTLGYELMSALAPRVTVQIR

Function: Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids. Catalytic Activity: L-alanine = D-alanine Sequence Mass (Da): 38378 Sequence Length: 356 Pathway: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1. EC: 5.1.1.1

A9ESU7

MRPTRAEVNLAHLRHNLRVLERGLTGATKPQIWGVLKADAYGHGAPAVARTLERAGIPGLCVALLEEAIELRDAGIRLPILVMGGYYGPRRDGFEEIIARDLVPVVYDAGQIERLASVVRLEQRGRVGVHLKVDTGMGRLGAASSEIEAVLATLAKHPEVKLDGLMTHLACADADDLGVTIEQMRLFGEIEQRAKSFGLTPRVRHASNSAAMLRLPAALLDIVRPGVALFGISPCAGLAPDLKPVIRVRSEIVALRTIAKGDRIGYGHTWQASRESVVATVPMGYADGLSRQLSNRGAALVRGQRAPIAGAVSMDLTMLDVTDVPGARLGDEVVFLGTQDGPLGRGTISAEEIAGLTGTIAWEVLTSISRRVPRFYREP

Function: Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids. Catalytic Activity: L-alanine = D-alanine Sequence Mass (Da): 40620 Sequence Length: 379 Pathway: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1. EC: 5.1.1.1

P00688

MKFVLLLSLIGFCWAQYDPHTSDGRTAIVHLFEWRWVDIAKECERYLAPKGFGGVQVSPPNENVVVHNPSRPWWERYQPISYKICTRSGNEDEFRDMVTRCNNVGVRIYVDAVINHMCGAGNPAGTSSTCGSYLNPNNREFPAVPYSAWDFNDNKCNGEIDNYNDAYQVRNCRLTGLLDLALEKDYVRTKVADYMNHLIDIGVAGFRLDAAKHMWPGDIKAVLDKLHNLNTKWFSQGSRPFIFQEVIDLGGEAIKGSEYFGNGRVTEFKYGAKLGTVIRKWNGEKMSYLKNWGEGWGLVPSDRALVFVDNHDNQRGHGAGGSSILTFWDARMYKMAVGFMLAHPYGFTRVMSSYRWNRNFQNGKDQNDWIGPPNNNGVTKEVTINADTTCGNDWVCEHRWRQIRNMVAFRNVVNGQPFSNWWDNNSNQVAFSRGNRGFIVFNNDDWALSATLQTGLPAGTYCDVISGDKVDGNCTGLRVNVGSDGKAHFSISNSAEDPFIAIHADSKL

Cofactor: Binds 1 Ca(2+) ion per subunit. Catalytic Activity: Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units. Sequence Mass (Da): 57318 Sequence Length: 508 Subcellular Location: Secreted EC: 3.2.1.1

B6K9M7

MPTESRSILARAEETRCRHLSRLLRAGLVFLLCDVLTSCLATPELQNTVIRSSKAHHLQLLFSSRSTPAVKFPLDATLSAPNSFGEQEARSVEAVKQNPWATTTAFADFMKRFNIPQVHGSGIFVDLGRDTEGYREVGGKCPVFGKAIQMHQPAEYSNNFLDDAPTSNDASKKPLPGGFNNPQVYTSGQKFSPIDDSLLQERLGTAGPKTAIGRCALYAYSTIAVNPSTNYTSTYKYPFVYDAVSRKCYVLSVSAQLLKGEKYCSVNGTPSGLTWACFEPVKEKSSARALVYGSAFVAEGNPDAWQSACPNDAVKDALFGKWEDGQCVPFDTKTSVQSDQATNKEECWKRVFANPLVASDAPTTYPEAAQKNWNDFWPVHEQSSPKSGGFGANWANFYLEKESGETICAIFDQVPDCFAPITGAVAYTALGSSTEVNLPQCDSASFIPIEGPCNNCVQVVTECVGNQFDQTSKACCTEPEIIPPVKPPVEPPVEPPVEPPVEPPVEPPVEPPVEPPVEPPVEPPVVEPPTEPSVPEPEPPVVLPPTPGEGGGGGTSGDETVEKEGSGGNTALIAGSVLGMLIILALVGTCVGFYYRKRPLPPTERPTVEASGGREVEGPSDVAVPPDHSWWGEGEHETESLLGSRAVDAEF

Function: May play a role in host cell invasion. PTM: Proteolytically cleaved within its transmembrane domain, releasing a soluble form from the cell surface. Location Topology: Single-pass type I membrane protein Sequence Mass (Da): 69944 Sequence Length: 651 Subcellular Location: Cell membrane

P16445

MKEIYYIVILCSLYLINLGNCSEGTDKIISENGDVKFDLIPKENTERSHKLINPWEKFMEKYDIEKVHGSGIRVDLGEDARVENQDYRIPSGKCPVMGKGITIQNSKVSFLTRVATGNQKVREGGLAFPQTDVNISPITIDNLKLMYKDHKEILALNDMSLCAKHASFYVPGTNVNTAYRHPAVYDKSNKTCYILYVAAQENMGPRYCSNEEDNENQPFCFTPEKKDEYKNLSYLTKNLREDWETSCPNKSIQNAKFGVWVDGYCSEYQKKEVHDNKTLLECNQIVFNESASDQPKQYEKHLEDTAKIRRGIVDRNGKLIGEALLPIGSYRADQVKSKGKGYNWANYDKKTKKCYIFNKKPTCLINDKDFVATTALSSLEEGPQESFPCDIYKKKIAEEIKVMNVNRNNNGNDTIKFPRIFISDDKESLNCPCEPTQLTQSTCKFFVCNCVEKRQFISENNEVEIKDEFKSEYESPINQRMLIIIILIATGAILASLLIFYFFKSNKPGDDYDKMGQADTYGKAQSRKDEMLDPEVSFWGEDKRASHTTPVLMEKPYY

Function: Involved in parasite invasion of erythrocytes. Location Topology: Single-pass type I membrane protein Sequence Mass (Da): 63974 Sequence Length: 558 Subcellular Location: Membrane

P22621

MRKLYCVLLLSAFEFTYMINFGRGQNYWEHPYQKSDVYHPINEHREHPKEYQYPLHQEHTYQQEDSGEDENTLQHAYPIDHEGAEPAPQEQNLFSSIEIVERSNYMGNPWTEYMAKYDIEEVHGSGIRVDLGEDAEVAGTQYRLPSGKCPVFGKGIIIENSNTTFLTPVATGNQYLKDGGFAFPPTEPLMSPMTLDEMRHFYKDNKYVKNLDELTLCSRHAGNMIPDNDKNSNYKYPAVYDDKDKKCHILYIAAQENNGPRYCNKDESKRNSMFCFRPAKDISFQNYTYLSKNVVDNWEKVCPRKNLQNAKFGLWVDGNCEDIPHVNEFSAIDLFECNKLVFELSASDQPKQYEQHLTDYEKIKEGFKNKNASMIKSAFLPTGAFKADRYKSHGKGYNWGNYNTETQKCEIFNVKPTCLINNSSYIATTALSHPIEVEHNFPCSLYKNEIMKEIERESKRIKLNDNDDEGNKKIIAPRIFISDDKDSLKCPCDPEIVSNSTCNFFVCKCVERRAEVTSNNEVVVKEEYKDEYADIPEHKPTYDKMKIIIASSAAVAVLATILMVYLYKRKGNAEKYDKMDEPQHYGKSNSRNDEMLDPEASFWGEEKRASHTTPVLMEKPYY

Function: Involved in parasite invasion of erythrocytes. Location Topology: Single-pass type I membrane protein Sequence Mass (Da): 72010 Sequence Length: 622 Subcellular Location: Membrane

B6KAM0

MICSIMGGLRSLRAARPYSHQSNTETKHMGLVGVASLLVLVADCTIFASGLSSSTRSRESQTLSASTSGNPFQANVEMKTFMERFNLTHHHQSGIYVDLGQDKEVDGTLYREPAGLCPIWGKHIELQQPDRPPYRNNFLEDVPTEKEYKQSGNPLPGGFNLNFVTPSGQRISPFPMELLEKNSNIKASTDLGRCAEFAFKTVAMDKNNKATKYRYPFVYDSKKRLCHILYVSMQLMEGKKYCSVKGEPPDLTWYCFKPRKSVTENHHLIYGSAYVGENPDAFISKCPNQALRGYRFGVWKKGRCLDYTELTDTVIERVESKAQCWVKTFENDGVASDQPHTYPLTSQASWNDWWPLHQSDQPHSGGVGRNYGFYYVDTTGEGKCALSDQVPDCLVSDSAAVSYTAAGSLSEETPNFIIPSNPSVTPPTPETALQCTADKFPDSFGACDVQACKRQKTSCVGGQIQSTSVDCTADEQNECGSNTALIAGLAVGGVLLLALLGGGCYFAKRLDRNKGVQAAHHEHEFQSDRGARKKRPSDLMQEAEPSFWDEAEENIEQDGETHVMVEGDY

Function: Essential microneme protein that plays an important role in host cell invasion. Part of the moving junction (MJ) complex, a ringlike structure formed between the plasma membranes of the apical tip of the parasite and the target host cell. During invasion, the MJ migrates from the anterior to the posterior of the parasite, leading to internalization of the parasite into a parasitophorous vacuole (PV). PTM: Proteolytically cleaved during invasion within its transmembrane domain, releasing a soluble form from the tachyzoite surface. The cytosolic tail generated by ROM4 cleavage during invasion may trigger parasite replication within the parasitophorous vacuole. Location Topology: Single-pass type I membrane protein Sequence Mass (Da): 63021 Sequence Length: 569 Subcellular Location: Cell membrane

P37112

MTKEEIKRLVDEVKTDVIAWRRHLHAHPELSFQEEKTAQFVYETLQSFGHLELSRPTKTSVMARLIGQQPGRVVAIRADMDALPIQEENTFEFASKNPGVMHACGHDGHTAMLLGTAKIFSQLRDDIRGEIRFLFQHAEELFPGGAEEMVQAGVMDGVDVVIGTHLWSPLERGKIGIVYGPMMAAPDRFFIRIIGKGGHGAMPHQTIDAIAIGAQVVTNLQHIVSRYVDPLEPLVLSVTQFVAGTAHNVLPGEVEIQGTVRTFDETLRRTVPQWMERIVKGITEAHGASYEFRFDYGYRPVINYDEGDPRHGGNGVRAVRRRGSGPLETEHGRRRFLRLFAKSARQLFLRRRGQCRKRHRLPAPPPALYD

Function: Hydrolyzes most efficiently N-acetyl derivatives of aromatic amino acids but is also active on other amino acids. L-stereospecific. Catalytic Activity: an N-acyl-L-amino acid + H2O = a carboxylate + an L-alpha-amino acid Sequence Mass (Da): 41676 Sequence Length: 370 EC: 3.5.1.14

Q80ZD5

MAWLVLLGLLLCMLGAGSGTSDLEGVLPPDPHNCPNKCVCAADVLSCAGRGLQDLPAALPATAAELDLSHNALKRLHPGWLAPLSRLRALYLGYNKLDVLGRGVFTNASGLRILDLSSNLLRRLRTYDLDGLEELEKLLLFNNRLMHLDLDAFQGLSMLSHLYLSCNELSSFSFNHLHGLGLTRLRTLDLSSNWLGHVSVPELAALPTFLKNRLYLHNNPLPCDCSLYHLLRRWHQRGLSALHDFEREYTCLAFKVAESRVRFFEHSRVFKNCSVAAAPGLELPEEELHTHVGQSLRLFCNTTVPAARVAWVSPKNELLVAPGSQDGSIAVLADGSLAIGRVQEQHAGLFVCLASGPRLHHNQTLEYNVSVHKPRPEPEAFNTGFTTLLGCIVGLVLVLLYLFAPPCRGCCRCCRRACRNRCWPRASSPLQELSAQSSVLSTTPPDAPSRKASVHKHVAFLEPGKKGLNGRVQLAVAEDFDLCNPMGLQLKAGSESASSTGSEGLMMS

Function: May mediate heterophilic cell-cell interaction. May contribute to signal transduction through its intracellular domain. Location Topology: Single-pass type I membrane protein Sequence Mass (Da): 55565 Sequence Length: 508 Subcellular Location: Membrane

D3FSJ2

MKITSGDLPGVGKKISFITSEGSMVVLVIHHTGKREMYFFDDADDDEVSFSLTLSAEETKQMGAQLLGAILNPADTDKIDRIKLIRKQVVVEWIDITKHSPIISKSIAQIEKMKPKGISIVGVFKNDEMMVDPEPTLVLEKGDTLMAVGKRDAIQKFEELCACKENN

Function: Modulates the activity of the ammonium/proton antiporter AmhT. Location Topology: Peripheral membrane protein Sequence Mass (Da): 18525 Sequence Length: 167 Subcellular Location: Cell membrane

Q16671

MLGSLGLWALLPTAVEAPPNRRTCVFFEAPGVRGSTKTLGELLDTGTELPRAIRCLYSRCCFGIWNLTQDRAQVEMQGCRDSDEPGCESLHCDPSPRAHPSPGSTLFTCSCGTDFCNANYSHLPPPGSPGTPGSQGPQAAPGESIWMALVLLGLFLLLLLLLGSIILALLQRKNYRVRGEPVPEPRPDSGRDWSVELQELPELCFSQVIREGGHAVVWAGQLQGKLVAIKAFPPRSVAQFQAERALYELPGLQHDHIVRFITASRGGPGRLLSGPLLVLELHPKGSLCHYLTQYTSDWGSSLRMALSLAQGLAFLHEERWQNGQYKPGIAHRDLSSQNVLIREDGSCAIGDLGLALVLPGLTQPPAWTPTQPQGPAAIMEAGTQRYMAPELLDKTLDLQDWGMALRRADIYSLALLLWEILSRCPDLRPDSSPPPFQLAYEAELGNTPTSDELWALAVQERRRPYIPSTWRCFATDPDGLRELLEDCWDADPEARLTAECVQQRLAALAHPQESHPFPESCPRGCPPLCPEDCTSIPAPTILPCRPQRSACHFSVQQGPCSRNPQPACTLSPV

Function: On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Receptor for anti-Muellerian hormone. Catalytic Activity: ATP + L-threonyl-[receptor-protein] = ADP + H(+) + O-phospho-L-threonyl-[receptor-protein] Location Topology: Single-pass type I membrane protein Sequence Mass (Da): 62750 Sequence Length: 573 Subcellular Location: Membrane EC: 2.7.11.30

Q62893

MLGTLGLWTLLPAAAQVSPNRRTCVFFEAPGVRGSTKTLGEVVDAGPGPPKGIRCLYSHCCFGIWNLTHGRAQVEMQGCLDSDEPGCESLHCDPVPRAHPSPSSTLFTCSCGTDFCNANYSHLPPSGNRGAPGPQEPQATPGGPIWMAQLLLGVFLVLLLSIIILALLQRKACRVQGGSDPEPEPGSGGDCSEELPELAELRFSQVIQEGGHAVVWAGRLQGEMVAIKAFPPRAVAQFRAERAVYQLLGLQHNHIVRFITAGQGGPGPLPSGPLLVLELYPKGSLCHYLTQYTSDWGSSLRMALSLAEGLAFLHGERWQDGQYKPGIAHRDLSSQNVLIREDRSCAIGDLGLALVLPGLAQPPALAPTQPRGPAAILEAGTQRYMAPELLDKTLDLQDWGTALQRADVYSLALLLWEILSRCSDLRPDHRPPPFQLAYEAELGSNPSACELWALAVAERKRPNIPSSWSCSATDPRGLRELLEDCWDADPEARLTAECVQQRLAALAYPQVASSFPESCPQGCPENCPAAPASAAFPCRPQQSSCLLSVQQGSGSKS

Function: On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Receptor for anti-Muellerian hormone. Catalytic Activity: ATP + L-threonyl-[receptor-protein] = ADP + H(+) + O-phospho-L-threonyl-[receptor-protein] Location Topology: Single-pass type I membrane protein Sequence Mass (Da): 59749 Sequence Length: 557 Subcellular Location: Membrane EC: 2.7.11.30

D3FSJ3

MVIPELFSAGLILLLLFITGFVGMKMKIPDVVIFILLGIAVGGLLSGSHLLHFAGEVGIVLLFFMLGMEFPLKQLMSIAKKVLRAGILDVALSFGVTMAICMMMGLDVITSLIIGGVAYATSSSITAKMLESSKRMANPESEFMLGLLIFEDLVAPILVAVLVGLTAGMALTAGSMSLLVVKVVALVAGAVILGVFLFRKLGSFFDRHMKHDLFILFVIGLALMYGGLALYLDLSEVLGAFLAGIMLAEVKRTHELELMVVRFRDLLLPLFFLYFGTTISFSEGIPMIPLLILVLVWSVIAKVIVGVLGGRWYGLTKKVSLRAGLSLTQRGEFSIIIASLAAGSIKAFSSVFILASAMIGILLFQFAPSIANKFYGKKAKTSVKQHVGSA

Function: Ammonium/proton antiporter that mediates the efflux of ammonium ions. Can also transport potassium or rubidium, but not sodium or lithium. Location Topology: Multi-pass membrane protein Sequence Mass (Da): 41791 Sequence Length: 390 Subcellular Location: Cell membrane

Q9FR37

MATNNDFGAFIEKVTISPTSTSSSPPSLQGLTFAIKDIFDVEGRVTGFGNPDWLRTHSAATSTAPVVSSLLEAGATALGITIMDEMAYSINGENAHYGTPRNPIAFDRVPGGSSSGSAVAVAARLVDFSIGTDTGGSVRVPASYCGIFGFRPSHGAVSTVGLTPMAQSFDTVGWFARDTATLKRVGCVLLQQHHLNPIEPSQLIIADDCFKLCSVPHDLLVQPLVGSVEKSFGGNTVVKKVNLGEYIGQNVPSLKHFMTSDDVTTQQEFCIPSLMALSSSMRLLQRHEFKINHGAWISSVKPEFGPGISERIEEAIRTSDEKIDHCRSVKSELITALSTLLGEKGVLVIPTVPGPPPHLQANVAALESFRSRAFSLLSIAGVSGFCQVSIPLGLHENLPVSVSLVAKYGSDGFLLSLVDSLAAFI

Function: Amidase involved in auxin biosynthesis. Converts indole-3-acetamide to indole-3-acetate . Converts phenyl-2-acetamide (PAM) to phenyl-2-acetate. Substrate preference is PAM > IAM . Can also use L-asparagine and 1-naphtalene-acetamide as substrates, but not indole-3-acetonitrile or indole-3-acetyl-L-aspartic acid . Catalytic Activity: a monocarboxylic acid amide + H2O = a monocarboxylate + NH4(+) Sequence Mass (Da): 45056 Sequence Length: 425 Subcellular Location: Cytoplasm EC: 3.5.1.4

Q7XTK3

MAMAGGGRGDYGAFMERFVLPPPPSQQLPLHGLTFAIKDIFDIAGRVTGFGNPDWARTHAPAAATSPVVLAALAAGATSLGTTIMDEMAYSINGENTHYGTPTNPCAPGRVPGGSSSGSAVAVAANLVDFSLGTDTGGSVRVPAAYCGIFGLRPSHGLVSAENVIPMAQMFDTVGWFSRDLSTLSRVTKVLLPLPDDIVKQPTQVTIPMDCFQILGSLDDRTYQIINASVAKRFDSQILDNRNLGDFISDNVPSIGKFITDFSESELPSVPALSVISHVMRGLQRSQFKANHAEWVNTVKPNLGPGLRERILEAIASGDNESLEDFQAIRAEFKSALAALLKDHGILAIPTVPGPPPKVGMEAAPLENFRARAFSLLSIAGLSGFCQVSIPLGMRNGLPVSVSLVARHGADHFLLNVVEELYQTLIDEATKTWSS

Function: Amidase involved in auxin biosynthesis (Probable). Converts indole-3-acetamide (IAM) to indole-3-acetate, and phenyl-2-acetamide (PAM) to phenyl-2-acetate. Substrate preference is PAM > IAM . Catalytic Activity: a monocarboxylic acid amide + H2O = a monocarboxylate + NH4(+) Sequence Mass (Da): 46180 Sequence Length: 435 Subcellular Location: Cytoplasm EC: 3.5.1.4

Q1PS23

MKSILKAMALSLTTSIALATILLFVYKFATRSKSTKKSLPEPWRLPIIGHMHHLIGTTPHRGVRDLARKYGSLMHLQLGEVPTIVVSSPKWAKEILTTYDISFANRPETLTGEIVLYHNTDVVLAPYGEYWRQLRKICTLELLSVKKVKSFQSLREEECWNLVQEIKASGSGRPVNLSENVFKLIATILSRAAFGKGIKDQKELTEIVKEILRQTGGFDVADIFPSKKFLHHLSGKRARLTSLRKKIDNLIDNLVAEHTVNTSSKTNETLLDVLLRLKDSAEFPLTSDNIKAIILDMFGAGTDTSSSTIEWAISELIKCPKAMEKVQAELRKALNGKEKIHEEDIQELSYLNMVIKETLRLHPPLPLVLPRECRQPVNLAGYNIPNKTKLIVNVFAINRDPEYWKDAEAFIPERFENSSATVMGAEYEYLPFGAGRRMCPGAALGLANVQLPLANILYHFNWKLPNGVSYDQIDMTESSGATMQRKTELLLVPSF

Function: Involved in the biosynthesis of the antimalarial endoperoxide artemisinin . Catalyzes three consecutive oxidations of amorpha-4,11-diene to produce artemisinic acid, with artemisinic alcohol and artemisinic aldehyde as intermediates products, but is unable to oxidize germacrene A . No activity with limonene, alpha-pinene, beta-pinene, pinocarveol, (-)-alloisolongifolene, caryophyllene, (-)-alpha-gurjunene, (+)-gamma-gurjunene, (+)-ledene, (+)-beta-selinene and (+)-valencene as substrates . Catalytic Activity: (+)-amorpha-4,11-diene + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = (+)-artemisinate + 4 H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase] Location Topology: Single-pass type II membrane protein Sequence Mass (Da): 55711 Sequence Length: 495 Pathway: Sesquiterpene biosynthesis. Subcellular Location: Endoplasmic reticulum membrane EC: 1.14.14.114

P46883

MGSPSLYSARKTTLALAVALSFAWQAPVFAHGGEAHMVPMDKTLKEFGADVQWDDYAQLFTLIKDGAYVKVKPGAQTAIVNGQPLALQVPVVMKDNKAWVSDTFINDVFQSGLDQTFQVEKRPHPLNALTADEIKQAVEIVKASADFKPNTRFTEISLLPPDKEAVWAFALENKPVDQPRKADVIMLDGKHIIEAVVDLQNNKLLSWQPIKDAHGMVLLDDFASVQNIINNSEEFAAAVKKRGITDAKKVITTPLTVGYFDGKDGLKQDARLLKVISYLDVGDGNYWAHPIENLVAVVDLEQKKIVKIEEGPVVPVPMTARPFDGRDRVAPAVKPMQIIEPEGKNYTITGDMIHWRNWDFHLSMNSRVGPMISTVTYNDNGTKRKVMYEGSLGGMIVPYGDPDIGWYFKAYLDSGDYGMGTLTSPIARGKDAPSNAVLLNETIADYTGVPMEIPRAIAVFERYAGPEYKHQEMGQPNVSTERRELVVRWISTVGNYDYIFDWIFHENGTIGIDAGATGIEAVKGVKAKTMHDETAKDDTRYGTLIDHNIVGTTHQHIYNFRLDLDVDGENNSLVAMDPVVKPNTAGGPRTSTMQVNQYNIGNEQDAAQKFDPGTIRLLSNPNKENRMGNPVSYQIIPYAGGTHPVAKGAQFAPDEWIYHRLSFMDKQLWVTRYHPGERFPEGKYPNRSTHDTGLGQYSKDNESLDNTDAVVWMTTGTTHVARAEEWPIMPTEWVHTLLKPWNFFDETPTLGALKKDK

Cofactor: Binds 1 copper ion per subunit. Can also use zinc ion as cofactor (By similarity). Function: The enzyme prefers aromatic over aliphatic amines. PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue. Catalytic Activity: an aliphatic amine + H2O + O2 = an aldehyde + H2O2 + NH4(+) Sequence Mass (Da): 84379 Sequence Length: 757 Pathway: Amino-acid degradation; L-phenylalanine degradation; phenylacetate from L-phenylalanine: step 2/3. Subcellular Location: Periplasm EC: 1.4.3.21

Q43077

MASTTTMRLALFSVLTLLSFHAVVSVTPLHVQHPLDPLTKEEFLAVQTIVQNKYPISNNRLAFHYIGLDDPEKDHVLRYETHPTLVSIPRKIFVVAIINSQTHEILINLRIRSIVSDNIHNGYGFPILSVDEQSLAIKLPLKYPPFIDSVKKRGLNLSEIVCSSFTMGWFGEEKNVRTVRLDCFMKESTVNIYVRPITGITIVADLDLMKIVEYHDRDIEAVPTAENTEYQVSKQSPPFGPKQHSLTSHQPQGPGFQINGHSVSWANWKFHIGFDVRAGIVISLASIYDLEKHKSRRVLYKGYISELFVPYQDPTEEFYFKTFFDSGEFGFGLSTVSLIPNRDCPPHAQFIDTYVHSANGTPILLKNAICVFEQYGNIMWRHTENGIPNESIEESRTEVNLIVRTIVTVGNYDNVIDWEFKASGSIKPSIALSGILEIKGTNIKHKDEIKEDLHGKLVSANSIGIYHDHFYIYYLDFDIDGTHNSFEKTSLKTVRIKDGSSKRKSYWTTETQTAKTESDAKITIGLAPAELVVVNPNIKTAVGNEVGYRLIPAIPAHPLLTEDDYPQIRGAFTNYNVWVTAYNRTEKWAGGLYVDHSRGDDTLAVWTKQNREIVNKDIVMWHVVGIHHVPAQEDFPIMPLLSTSFELRPTNFFERNPVLKTLSPRDVAWPGCSN

Cofactor: Binds 1 copper ion per subunit. PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue. Catalytic Activity: an aliphatic amine + H2O + O2 = an aldehyde + H2O2 + NH4(+) Sequence Mass (Da): 76358 Sequence Length: 674 EC: 1.4.3.21

P12807

MERLRQIASQATAASAAPARPAHPLDPLSTAEIKAATNTVKSYFAGKKISFNTVTLREPARKAYIQWKEQGGPLPPRLAYYVILEAGKPGVKEGLVDLASLSVIETRALETVQPILTVEDLCSTEEVIRNDPAVIEQCVLSGIPANEMHKVYCDPWTIGYDERWGTGKRLQQALVYYRSDEDDSQYSHPLDFCPIVDTEEKKVIFIDIPNRRRKVSKHKHANFYPKHMIEKVGAMRPEAPPINVTQPEGVSFKMTGNVMEWSNFKFHIGFNYREGIVLSDVSYNDHGNVRPIFHRISLSEMIVPYGSPEFPHQRKHALDIGEYGAGYMTNPLSLGCDCKGVIHYLDAHFSDRAGDPITVKNAVCIHEEDDGLLFKHSDFRDNFATSLVTRATKLVVSQIFTAANYEYCLYWVFMQDGAIRLDIRLTGILNTYILGDDEEAGPWGTRVYPNVNAHNHQHLFSLRIDPRIDGDGNSAAACDAKSSPYPLGSPENMYGNAFYSEKTTFKTVKDSLTNYESATGRSWDIFNPNKVNPYSGKPPSYKLVSTQCPPLLAKEGSLVAKRAPWASHSVNVVPYKDNRLYPSGDHVPQWSGDGVRGMREWIGDGSENIDNTDILFFHTFGITHFPAPEDFPLMPAEPITLMLRPRHFFTENPGLDIQPSYAMTTSEAKRAVHKETKDKTSRLAFEGSCCGK

Cofactor: Binds 1 copper ion per subunit. Can also use zinc ion as cofactor . PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue. Catalytic Activity: an aliphatic amine + H2O + O2 = an aldehyde + H2O2 + NH4(+) Sequence Mass (Da): 77534 Sequence Length: 692 Subcellular Location: Peroxisome EC: 1.4.3.21

H2A0M3

MSLPKTANGMDKLKLCYLLLFYLGSSSLTEVSGAQTCEIDSVLCTSDLSEPDDPPIFHDLTTKEIKSVQTYLYHQRDLRLLRPGLAKINTSFIQGMELYLPNKKDVIHYLQSKVPTPKPPRAAVVTIFRGDCDPAVVEEYIVFPLPWPTQHRLHRKVPYYLRPFNDVEFATISDFLTKQVDGVLRQFLEESFGGRLINCGNRCLNFQFASPVGPSVSNEPGARKSWYWLHQLVEYSALHPVDFAVLMKIVGCVYTIEKVYFNNMYFNSLQEVALHYRNPSFPRLRIPYPVDSKQLFSKMERRGILFPEKPVSPPRQVEPEGKRYSVKYQEVKYMNWKFNFRLSPGLGPRLHNIRYHDRLIVYELALQDIVVFYSGAEPPHQYANFFDSSYMIGMNLQGMVPGVDCPTGATFIDSHILTESSLKPAKLINAFCVFEQNTGDFLRRHISKTSPDGPFYEGVPSIVLVLRAITTIANYDYTIDFIFHHNGVLQTKVVPTGYILPSLYTKQNENKYGFRLNNKLIGNLHHHLFNFKVDIDINGQHNRYETLDIVLDKTSHPVSKKPYDVWYQNKIKHNLRKTEMEALFKYDFDKPMHHIFYNNNLKSPEGNNMAYRLVNRGMSKSLLPECSGNEGTGAWMRHQIAVTKRKETELTSSSVYSAFGTKNPVVNFRNFYADNENIVDEDLVAWVTMGTYHIPHTEDLPVTHTPGLDLSFFLSPFNYFPEDPAMGSRDSVRIEAVDKNNLKRGIKIDKQTFPEKMTCKAPIGNYFEYILKRPNVIFDIQ

Cofactor: Binds 1 copper ion per subunit. PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue. Sequence Mass (Da): 89950 Sequence Length: 781 Subcellular Location: Secreted EC: 1.4.3.-