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stringlengths 6
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stringlengths 11
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stringlengths 108
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Q5FVE4 | MTGTPKTQEGAKDLEVDMNKTEVTPRLWTTCRDGEVLLRLSKHGPGHETPMTIPEFFRESVNRFGTYPALASKNGKKWEILNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILLVENDQQLQKILSIPQSSLEPLKAIIQYRLPMKKNNNLYSWDDFMELGRSIPDTQLEQVIESQKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKHETVVSYLPLSHIAAQMMDIWVPIKIGALTYFAQADALKGTLVSTLKEVKPTVFIGVPQIWEKIHEMVKKNSAKSMGLKKKAFVWARNIGFKVNSKKMLGKYNTPVSYRMAKTLVFSKVKTSLGLDHCHSFISGTAPLNQETAEFFLSLDIPIGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKNMLFQQNKDGIGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITAGGENVPPIPVETLVKKKIPIISNAMLVGDKLKFLSMLLTLKCEMNQMSGEPLDKLNFEAINFCRGLGSQASTVTEIVKQQDPLVYKAIQQGINAVNQEAMNNAQRIEKWVILEKDFSIYGGELGPMMKLKRHFVAQKYKKQIDHMYH | Function: Catalyzes the conversion of fatty acids such as long chain and very long-chain fatty acids to their active form acyl-CoAs for both synthesis of cellular lipids, and degradation via beta-oxidation. Can activate diverse saturated, monosaturated and polyunsaturated fatty acids . Has increased ability to activate oleic and linoleic acid . May play a role in spermatogenesis .
Catalytic Activity: a long-chain fatty acid + ATP + CoA = a long-chain fatty acyl-CoA + AMP + diphosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 74354
Sequence Length: 666
Subcellular Location: Cytoplasm
EC: 6.2.1.3
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O34847 | MAPRLEFEKPVIELQTKIAELKKFTQDSDMDLSAEIERLEDRLAKLQDDIYKNLKPWDRVQIARLADRPTTLDYIEHLFTDFFECHGDRAYGDDEAIVGGIAKFHGLPVTVIGHQRGKDTKENLVRNFGMPHPEGYRKALRLMKQADKFNRPIICFIDTKGAYPGRAAEERGQSEAIAKNLFEMAGLRVPVICIVIGEGGSGGALGLGVGNHLHMLENSTYSVISPEGAAALLWKDSSLAKKAAETMKITAPDLKELGIIDHMIKEVKGGAHHDVKLQASYMDETLKQSLKTLLKLSEEELVQQRYEKYKAIGKVSVEDQYIGVN | Function: Component of the acetyl coenzyme A carboxylase (ACC) complex. First, biotin carboxylase catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the carboxyltransferase to acetyl-CoA to form malonyl-CoA.
Catalytic Activity: acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein]
Sequence Mass (Da): 36334
Sequence Length: 325
Pathway: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.1.3.15
|
A1UQX6 | MYNYLDFEKPVADLDVQILELKKIAQEKGSLDMSDEIARLEMRSQTALRDLYKKLSPWQKTQVARHPDRPHFMDYSAQLLRDVTPLAGDRKFAEDEAIQAGFARFKGEAIAYIGQEKGHDTQTRLRYNFGSARPEGYRKAVRIMELADRFGLPLLTFVDTAGAYPGVSAEERGQAEAIAQSTAATLRLRVPVVSVIIGEGGSGGAIAIAAANKVYMLEHSIYSVISPEGAASILWRDPARAKDAATNMQITAQDLYRLKIIDGIIPEPLGGAHRQKEAAIEAAGDGIAAALKSMIGKDGETIKQERWDKYLQIGRSLA | Function: Component of the acetyl coenzyme A carboxylase (ACC) complex. First, biotin carboxylase catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the carboxyltransferase to acetyl-CoA to form malonyl-CoA.
Catalytic Activity: acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein]
Sequence Mass (Da): 34963
Sequence Length: 318
Pathway: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.1.3.15
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A9WBQ9 | MKEFFRLSRKGFTGREDQDSAQIPDDLWVKCSSCRELIYKKQLNDNLKVCPKCGHHMRLSAHEWLGLLDVGSFREMDANLLPTDPLGFVTDEESYAAKLAKTQQRTGMADAVIAGIGAISNMQICVAVADFSFMGASMGSVYGEKMARSAERAAELGVPLLTINTSGGARQQEGVIGLMQMAKVTMALTRLADAGQPHIALLVDPCYGGVTASYPSVADIIIAEPGANIGFAGKRLIEQIMRQKLPAGFQTAEFMLEHGMIDMVVPRSEMRDTLARILRLYRQRSTSPAKAELAGRRATLPQPIM | Cofactor: Binds 1 zinc ion per subunit.
Function: Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA.
Catalytic Activity: acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein]
Sequence Mass (Da): 33312
Sequence Length: 305
Pathway: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.1.3.15
|
Q3ATW0 | MSWFNRVKPSISSTAKRDVPEGLWWKCEECGAALHKKQMEASDHTCPQCGYHFRISPYKYFSLLFDNQKYVEFDDHLRAADPLHFVDTKKYPDRVSDTIEKSGKTEACRNAHGLCGGETLVISAMDFSFIGGSMGSVVGEKISRAVDKAIELQSPLLVISQSGGARMMEGAFSLMQMAKTAAKLSLLSEHRLPYISLMTDPTMGGITASFAMLGDINISEPKALIGFAGPRVIRDTIKRDLPEGFQRAEFLLEHGFIDRIIPRRELKSDLTTLLSLMKL | Cofactor: Binds 1 zinc ion per subunit.
Function: Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA.
Catalytic Activity: acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein]
Sequence Mass (Da): 31086
Sequence Length: 279
Pathway: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.1.3.15
|
Q3B5Y0 | MVWFKRVKPFIRTTDRRDVPEGLWSKCEDCGAMLHRRQLEENLNTCNECGHHFRISPYRYFSILFDNEEFTEFDDCLRAADPLTFVDTKKYPDRVHDTIEKSGKTEACRNAFGKSAGADLVISAMDFGFIGGSMGSVVGEKISRAADKAIELNAPLIVISQSGGARMMEGAFSLMQMAKTAARLTRLGENRLPFISLMTDPTMGGISASFAMLGDLNISEPKALIGFAGPRVIRDTIKRDLPEGFQRAEFLQEHGFVDMIVHRKELKQRLAKTLAMMRVEG | Cofactor: Binds 1 zinc ion per subunit.
Function: Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA.
Catalytic Activity: acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein]
Sequence Mass (Da): 31496
Sequence Length: 281
Pathway: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.1.3.15
|
B3QL38 | MVWFKRGIPSIKTTDKRDTPEGLWSKCDECGAALHKKQLEDHLYTCPECGHHFRISPDLYFSFLFDDGAWDEFDGQLRAADPLTFVDTKKYPDRVRDTMQKSGKSEACRNATGSMGGSAAVISAMDFGFIGGSMGSVVGEKISRAADKSVELNAPLILISQSGGARMMEGAFSLMQMAKTSARLTRLGERNIPFISLMTDPTMGGISASYAMLGDLNISEPKALIGFAGPRVIRDTIKRDLPEGFQRAEFLKEHGFVDMIVHRKDLRLQLIKLFKHLRG | Cofactor: Binds 1 zinc ion per subunit.
Function: Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA.
Catalytic Activity: acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein]
Sequence Mass (Da): 30903
Sequence Length: 279
Pathway: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.1.3.15
|
Q6MEK6 | MGLFSRDKPKIKIQTTKKDGFSGWLKCTHCNELIHANELEQNSNCCPKCDYHYRLSTEDRIKSLSNPNTFKPLFQNLQPVDTLNFVDTEPYPKRLANAQEKSTSNEAVVVGTCMINKHKIALGVLDFSFMGGSMGSVVGERLTRLIEHALKEKLPLIIVSTSGGARMQESILSLMQMAKTSGALAKLHEARIPYISVLTNPTTGGVTASFASLGDIIVAEPNALICFAGPRVIEQTIGQRLPPGAQKSEFLLEHGMIDCIVKRPELKQKLAELIDFLKGNFSEENEPSPPPKNLIKKTSPLKDKN | Cofactor: Binds 1 zinc ion per subunit.
Function: Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA.
Catalytic Activity: acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein]
Sequence Mass (Da): 33647
Sequence Length: 305
Pathway: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.1.3.15
|
P18823 | MINEDPSSLTDMDNNIDSWKNNSENSSYSHADSLADVSNIDNLLSDKIFSIRDSNSNIYDIYYAYDTNDTNITKYKWTNNINRCIESYLRSQICEDIDFNSDICDKVQRTIIILIRSTNDTNDISDTNDISDTNDTNDTNAIYDPFDISDTNDTNEIYDPFFILDINDTNDTNDIYGIYDPDDIYETNIKDICERYSEIYPRNREKSTFVPIDYSDPNCMEKLARLWVQCETCYGLNFKQFFRPKMNICEHCGEHLKMSSSDRIDLLIDRDTWNPMDEDMVSVDPIKFDSIKELGSEEESSKDRLDEDMLSPDPIELDSEEESSKDRVDSEEEKDQSYIDRLDSYQEKTGLPETVQTGTDQREEIHPLFEDIMNQLDLYLQTAKNRVDSEEEKDQSYIDRLDSYQEKTGLPEAVQTGTGQLNGIPLALAVMDSEFIAGSMGCVVGEKITRLIEYATNLLLPLIIVCASGGARMQEGSLSLMQMAKISSALYNYQINQKLFYVAILTSPTTGGVTASFGMLGDIIIAEPNATIAFAGKRVIEQLLNKEVPEGSQSADLLFDRGLLDAVVPRHLLKEFLTELFQFHGFVPLT | Cofactor: Binds 1 zinc ion per subunit.
Function: Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA.
Catalytic Activity: acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein]
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 67143
Sequence Length: 590
Pathway: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1.
Subcellular Location: Plastid
EC: 2.1.3.15
|
C6XT67 | MAWFKREKKGISTSTEEKKEAPDGLWNKCPNCKKALHSADLLENKYVCQYCNYHLRVGSKEYFQVLFDNNQFTELFPNLTSGDPLNFTDSKPYTERLIESMAKTGLKDAIRAAHGKIEGEDLVVACMDFNFIGGSMGSVVGEKIARSIDYSIKHKIPFLMISKSGGARMMEAAFSLMQMAKTSAKLALLSQAKIPYISLLTDPTTGGVTASYAMLGDINIAEPGSLIGFAGPRVIKETIKKDLPKGFQTAEFVLEHGFLDFIVDRRAMKAKLAAFLKMMKN | Cofactor: Binds 1 zinc ion per subunit.
Function: Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA.
Catalytic Activity: acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein]
Sequence Mass (Da): 31164
Sequence Length: 281
Pathway: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.1.3.15
|
Q4FND1 | MNWIKKTLRFGEKIKTIIKARATKTEIANSDWTSCCKGPILKKDLEENLWVCPSCNKHHRISPRQRFDIIFGKNNYEVLKTPIPQDDPLNWNDAKPYKDRLKAARKKTGMDCGMMVVNTNILNLKITAIASDFDFVGGSIGAAEGEAFLYGIQHAIENEQPFVVFTSGGGMRMMESLISLSQMTRTTLAINELKKNNLPYIVVLTDPTAGGITASYAMLGDLHLAEPGALIAFAGARVIQGTVREELPEGFQRSEYVEKTGFVDLIVERKDLREKIGSLLSILLKKNSAINSSENETSEDSRALTKAAS | Cofactor: Binds 1 zinc ion per subunit.
Function: Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA.
Catalytic Activity: acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein]
Sequence Mass (Da): 34258
Sequence Length: 309
Pathway: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.1.3.15
|
P52769 | MSIKEWFEDKRKITALLKNSVERDSKDANETEKNKNKSIDYAKIKKLWAQCDNCENLLYLRFLRENQSVCKECGYYLQMNSSDRIELLIDRDTWRPMDEDMYTLDVLQFYSENEPSHSDNLNSEDESYKDHITFYQIETGLTDAIQTGIGQLNGLTIALGVMDFQFMGGSMGSVVGEKITRLIERATAESLPLIMVCASGGARMQEGSFSLMQMAKIASALYIHQKEKKLLYISILTSPTTGGVTASFGMLGDIIIAEPKAYIAFAGKRVIEQTLGQKVIEDFQVTEHLFGHGLFDLIVPRNLLKGVLSELFWFYVLRSSL | Cofactor: Binds 1 zinc ion per subunit.
Function: Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA.
Catalytic Activity: acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-CoA + N(6)-biotinyl-L-lysyl-[protein]
Sequence Mass (Da): 36403
Sequence Length: 321
Pathway: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1.
Subcellular Location: Plastid
EC: 2.1.3.15
|
Q41931 | MEKNMKFPVVDLSKLNGEERDQTMALINEACENWGFFEIVNHGLPHDLMDKIEKMTKDHYKTCQEQKFNDMLKSKGLDNLETEVEDVDWESTFYVRHLPQSNLNDISDVSDEYRTAMKDFGKRLENLAEDLLDLLCENLGLEKGYLKKVFHGTKGPTFGTKVSNYPPCPKPEMIKGLRAHTDAGGIILLFQDDKVSGLQLLKDGDWIDVPPLNHSIVINLGDQLEVITNGKYKSVLHRVVTQQEGNRMSVASFYNPGSDAEISPATSLVEKDSEYPSFVFDDYMKLYAGVKFQPKEPRFAAMKNASAVTELNPTAAVETF | Cofactor: Binds 1 Fe(2+) ion per subunit. Can also bind Cu(2+) ions.
Function: Enzyme involved in the ethylene biosynthesis. Required to mediate the 1-aminocyclopropane-1-carboxylic acid (ACC)-mediated reversion of the ABA-induced inhibition of seed germination via endosperm rupture. May promote stem elongation by maximizing the extensibility cells, possibly by activating ethylene biosynthesis, in response to very-long-chain fatty acids (VLCFAs C20:0 to C30:0).
Catalytic Activity: 1-aminocyclopropane-1-carboxylate + L-ascorbate + O2 = CO2 + ethene + 2 H2O + hydrogen cyanide + L-dehydroascorbate
Sequence Mass (Da): 36183
Sequence Length: 320
Pathway: Alkene biosynthesis; ethylene biosynthesis via S-adenosyl-L-methionine; ethylene from S-adenosyl-L-methionine: step 2/2.
EC: 1.14.17.4
|
Q06588 | MESFPIINLEKLNGEERAITMEKIKDACENWGFFECVNHGISLELLDKVEKMTKEHYKKCMEERFKESIKNRGLDSLRSEVNDVDWESTFYLKHLPVSNISDVPDLDDDYRTLMKDFAGKIEKLSEELLDLLCENLGLEKGYLKKVFYGSKRPTFGTKVSNYPPCPNPDLVKGLRAHTDAGGIILLFQDDKVSGLQLLKDGEWVDVPPVKHSIVVNLGDQLEVITNGKYKSVEHRVLSQTDGEGRMSIASFYNPGSDSVIFPAPELIGKEAEKEKKENYPRFVFEDYMKLYSAVKFQAKEPRFEAMKAMETTVANNVGPLATA | Function: Enzyme involved in the ethylene biosynthesis. May promote stem elongation by maximizing the extensibility cells, possibly by activating ethylene biosynthesis, in response to very-long-chain fatty acids (VLCFAs C20:0 to C30:0).
Catalytic Activity: 1-aminocyclopropane-1-carboxylate + L-ascorbate + O2 = CO2 + ethene + 2 H2O + hydrogen cyanide + L-dehydroascorbate
Sequence Mass (Da): 36677
Sequence Length: 323
Pathway: Alkene biosynthesis; ethylene biosynthesis via S-adenosyl-L-methionine; ethylene from S-adenosyl-L-methionine: step 2/2.
EC: 1.14.17.4
|
Q0WPW4 | MAIPVIDFSKLNGEEREKTLSEIARACEEWGFFQLVNHGIPLELLNKVKKLSSDCYKTEREEAFKTSNPVKLLNELVQKNSGEKLENVDWEDVFTLLDHNQNEWPSNIKETMGEYREEVRKLASKMMEVMDENLGLPKGYIKKAFNEGMEDGEETAFFGTKVSHYPPCPHPELVNGLRAHTDAGGVVLLFQDDEYDGLQVLKDGEWIDVQPLPNAIVINTGDQIEVLSNGRYKSAWHRVLAREEGNRRSIASFYNPSYKAAIGPAAVAEEEGSEKKYPKFVFGDYMDVYANQKFMPKEPRFLAVKSL | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Enzyme involved in the ethylene biosynthesis.
Catalytic Activity: 1-aminocyclopropane-1-carboxylate + L-ascorbate + O2 = CO2 + ethene + 2 H2O + hydrogen cyanide + L-dehydroascorbate
Sequence Mass (Da): 34947
Sequence Length: 307
Pathway: Alkene biosynthesis; ethylene biosynthesis via S-adenosyl-L-methionine; ethylene from S-adenosyl-L-methionine: step 2/2.
EC: 1.14.17.4
|
Q9FR99 | MAIPVIDFSKLDGKERAETMARIANGCEEWGFFQLVNHGIPVELLERVKKVSSECYKLREERFEGSKPVQLLDTLVKEGDGQRLDNVDWEDVFVLQDDNEWPSNPPDFEETMKEYREEIRKLAEKMMEVMDENLGFEKGCIKKAFSGDGQHPPFFGTKVSHYPPCPRLDLVKGLRAHTDAGGVILLFQDDQVGGLQMLKDGRWIDVQPLADAIVINTGDQIEVLSNGRYKSAWHRVLATSHGNRRSIASFYNPSLKATIAPAAGAATEEAAPPALYPKFLFGDYMDVYAKQKYEPKEPRFEAVRAI | Catalytic Activity: 1-aminocyclopropane-1-carboxylate + L-ascorbate + O2 = CO2 + ethene + 2 H2O + hydrogen cyanide + L-dehydroascorbate
Sequence Mass (Da): 34554
Sequence Length: 306
Pathway: Alkene biosynthesis; ethylene biosynthesis via S-adenosyl-L-methionine; ethylene from S-adenosyl-L-methionine: step 2/2.
EC: 1.14.17.4
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Q53WH9 | MSERVKVAILGSGNIGTDLMYKLLKNPGHMELVAVVGIDPKSEGLARARALGLEASHEGIAYILERPEIKIVFDATSAKAHVRHAKLLREAGKIAIDLTPAARGPYVVPPVNLKEHLDKDNVNLITCGGQATIPLVYAVHRVAPVLYAEMVSTVASRSAGPGTRQNIDEFTFTTARGLEAIGGAKKGKAIIILNPAEPPILMTNTVRCIPEDEGFDREAVVASVRAMEREVQAYVPGYRLKADPVFERLPTPWGERTVVSMLLEVEGAGDYLPKYAGNLDIMTASARRVGEVFAQHLLGKPVEEVVA | Function: Catalyzes the conversion of acetaldehyde or propanal to acetyl-CoA or propanoyl-CoA, respectively, using NAD(+) and coenzyme A. The aldehyde substrates can be directly channeled from the aldolase TTHB246 to the dehydrogenase TTHB247. Is the final enzyme in the meta-cleavage pathway for the degradation of aromatic compounds.
Catalytic Activity: acetaldehyde + CoA + NAD(+) = acetyl-CoA + H(+) + NADH
Sequence Mass (Da): 33115
Sequence Length: 307
EC: 1.2.1.10
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Q54RR5 | MIKKLILDPKNVSIIKNGIRNYSKSKSFIQPITTLSEEETLLKETVANFANEKVRPLVKVMDETSELNKGLLKDLFDMNLMGIDISDSYGGANMNFMGSIIAIEELAKVDPAISVIVDVQNTLVNNCINRYGSIQQREKYLSMLATNTVGSFCLSESGSGSDAFALATRAVRQSDGTFVLNGTKQWITNAKEAGVFIVMANVDPSQGYKGITAFIVESNNPGLRIGKKEDKLGIRASSTCEVILDNCVVKPTDILGELGRGYKIAIEGLNEGRIGIAAQMLGLAQGVFDSTIPYLMERKQFGKPIATFQGMQFTYADLAVDIEAGRLLTYNAARIKEAGLPFVFQASMAKLHCSRVAEKAASACISMLGGVGFTKEFPAEKFFRDSKVGQIYEGTSNIQLQTIAKEIVKNFNK | Function: Probable short and branched chain specific acyl-CoA dehydrogenase that catalyzes the removal of one hydrogen from C-2 and C-3 of the fatty acyl-CoA thioester, resulting in the formation of trans-2-enoyl-CoA.
Catalytic Activity: 2-methylbutanoyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = (2E)-2-methylbut-2-enoyl-CoA + reduced [electron-transfer flavoprotein]
Sequence Mass (Da): 45030
Sequence Length: 413
Pathway: Lipid metabolism; mitochondrial fatty acid beta-oxidation.
EC: 1.3.8.5
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P45954 | MEGLAVRLLRGSRLLRRNFLTCLSSWKIPPHVSKSSQSEALLNITNNGIHFAPLQTFTDEEMMIKSSVKKFAQEQIAPLVSTMDENSKMEKSVIQGLFQQGLMGIEVDPEYGGTGASFLSTVLVIEELAKVDASVAVFCEIQNTLINTLIRKHGTEEQKATYLPQLTTEKVGSFCLSEAGAGSDSFALKTRADKEGDYYVLNGSKMWISSAEHAGLFLVMANVDPTIGYKGITSFLVDRDTPGLHIGKPENKLGLRASSTCPLTFENVKVPEANILGQIGHGYKYAIGSLNEGRIGIAAQMLGLAQGCFDYTIPYIKERIQFGKRLFDFQGLQHQVAHVATQLEAARLLTYNAARLLEAGKPFIKEASMAKYYASEIAGQTTSKCIEWMGGVGYTKDYPVEKYFRDAKIGTIYEGASNIQLNTIAKHIDAEY | Function: Short and branched chain specific acyl-CoA dehydrogenase that catalyzes the removal of one hydrogen from C-2 and C-3 of the fatty acyl-CoA thioester, resulting in the formation of trans-2-enoyl-CoA . Among the different mitochondrial acyl-CoA dehydrogenases, acts specifically on short and branched chain acyl-CoA derivatives such as (S)-2-methylbutyryl-CoA as well as short straight chain acyl-CoAs such as butyryl-CoA . Plays an important role in the metabolism of L-isoleucine by catalyzing the dehydrogenation of 2-methylbutyryl-CoA, one of the steps of the L-isoleucine catabolic pathway . Can also act on valproyl-CoA, a metabolite of valproic acid, an antiepileptic drug .
Catalytic Activity: 2-methylbutanoyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = (2E)-2-methylbut-2-enoyl-CoA + reduced [electron-transfer flavoprotein]
Sequence Mass (Da): 47485
Sequence Length: 432
Pathway: Lipid metabolism; mitochondrial fatty acid beta-oxidation.
Subcellular Location: Mitochondrion matrix
EC: 1.3.8.5
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P70584 | MAVSAFQLWRAGGLLRRNFLTHSSSWKIPPRVLKSSQPEALLSVTNNALCFAPLQTFTDEDIMMQKAVKKFAQEQIAPLVSTMDENSKMEKSVIQGLFQQGMMGIEVEAKYGGTEASFLCSVLVIEELAKVDASVALLCDIQNTVINKLFRKHGTEEQKATYLPKLVTEKLGSFCLSEAGAGSDSFALKTRADKSGNYYVINGSKMWISNAEHAELFLVFANVDPPSGYRGITCFLVDRDTEGFQIGRRENKMGIRASSTCQLTFENVKVPETSVLGKIGHGYKYAIGSLNEGRIGIAAQMLGLAQGCFDYTIPYIKERMQFGKRIFDFQGLQHQVAHVATQLEAARLLTYNAARLVEAGRPFIKEASMAKYYASEVAGLTTSKCIEWMGGVGYTKDYPVEKFFRDAKIGTIYEGTSNIQLNTIAKHIDAEY | Function: Short and branched chain specific acyl-CoA dehydrogenase that catalyzes the removal of one hydrogen from C-2 and C-3 of the fatty acyl-CoA thioester, resulting in the formation of trans-2-enoyl-CoA . Among the different mitochondrial acyl-CoA dehydrogenases, acts specifically on short and branched chain acyl-CoA derivatives such as (S)-2-methylbutyryl-CoA as well as short straight chain acyl-CoAs such as butyryl-CoA . Plays an important role in the metabolism of L-isoleucine by catalyzing the dehydrogenation of 2-methylbutyryl-CoA, one of the steps of the L-isoleucine catabolic pathway (By similarity). Can also act on valproyl-CoA, a metabolite of the valproic acid drug .
Catalytic Activity: 2-methylbutanoyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = (2E)-2-methylbut-2-enoyl-CoA + reduced [electron-transfer flavoprotein]
Sequence Mass (Da): 47824
Sequence Length: 432
Pathway: Lipid metabolism; mitochondrial fatty acid beta-oxidation.
Subcellular Location: Mitochondrion matrix
EC: 1.3.8.5
|
P52042 | MDFNLTREQELVRQMVREFAENEVKPIAAEIDETERFPMENVKKMGQYGMMGIPFSKEYGGAGGDVLSYIIAVEELSKVCGTTGVILSAHTSLCASLINEHGTEEQKQKYLVPLAKGEKIGAYGLTEPNAGTDSGAQQTVAVLEGDHYVINGSKIFITNGGVADTFVIFAMTDRTKGTKGISAFIIEKGFKGFSIGKVEQKLGIRASSTTELVFEDMIVPVENMIGKEGKGFPIAMKTLDGGRIGIAAQALGIAEGAFNEARAYMKERKQFGRSLDKFQGLAWMMADMDVAIESARYLVYKAAYLKQAGLPYTVDAARAKLHAANVAMDVTTKAVQLFGGYGYTKDYPVERMMRDAKITEIYEGTSEVQKLVISGKIFR | Catalytic Activity: butanoyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = (2E)-butenoyl-CoA + reduced [electron-transfer flavoprotein]
Sequence Mass (Da): 41387
Sequence Length: 379
Pathway: Lipid metabolism; butanoate metabolism.
EC: 1.3.8.1
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Q06319 | MDFNLTDIQQDFLKLAHDFGEKKLAPTVTERDHKGIYDKELIDELLSLGITGAYFEEKYGGSGDDGGDVLSYILAVEELAKYDAGVAITLSATVSLCANPIWQFGTEAQKEKFLVPLVEGTKLGAFGLTEPNAGTDASGQQTIATKNDDGTYTLNGSKIFITNGGAADIYIVFAMTDKSKGNHGITAFILEDGTPGFTYGKKEDKMGIHTSQTMELVFQDVKVPAENMLGEEGKGFKIAMMTLDGGRIGVAAQALGIAEAALADAVEYSKQRVQFGKPLCKFQSISFKLADMKMQIEAARNLVYKAACKKQEGKPFTVDAAIAKRVASDVAMRVTTEAVQIFGGYGYSEEYPVARHMRDAKITQIYEGTNEVQLMVTGGALLR | Function: Has an optimum specificity for 4-carbon length fatty acyl-CoAs.
Catalytic Activity: butanoyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = (2E)-butenoyl-CoA + reduced [electron-transfer flavoprotein]
Sequence Mass (Da): 41408
Sequence Length: 383
EC: 1.3.8.1
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C3UVB0 | MDFNLSKELQMLQKEVRNFVNKKIVPFADQWDNENHFPYEEAVRPMGELGFFGTVIPEEYGGEGMDQGWLAAMIVTEEIARGSSALRVQLNMEVLGCAYTILTYGSEALKKKYVPKLSSAEFLGGFGITEPDAGSDVMAMSSTAEDKGDHWLLNGSKTWISNAAQADVLIYYAYTDKAAGSRGLSAFVIEPRNFPGIKTSNLEKLGSHASPTGELFLDNVKVPKENILGKPGDGARIVFGSLNHTRLSAAAGGVGLAQACLDAAIKYCNERRQFGKPIGDFQMNQDMIAQMAVEVEAARLLAYKAAAAKDEGRLNNGLDVAMAKYAAGEAVSKCANYAMRILGAYGYSTEYPVARFYRDAPTYYMVEGSANICKMIIALDQLGVRKANR | Function: Catalyzes the dehydrogenation of Glutaryl-CoA to glutaconyl-CoA.
Catalytic Activity: A + glutaryl-CoA = (2E)-glutaconyl-CoA + AH2
Sequence Mass (Da): 42382
Sequence Length: 389
Pathway: Aromatic compound metabolism; benzoyl-CoA degradation.
EC: 1.3.99.32
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Q58010 | MWGRDYELKYISYPKSVAIIGASKTEGKVGYAIMKNLKDFNGKIYPINPKYDEIFGIKCYKSVLDVEDDIDLAVIVVPNIVVPKVLEECGKKGVKGAVIITAGFSEVGNYELENKIKEIAKRYNIRIIGPNCLGIMNTHINLNATFAKVFPPKGGVSIISQSGAVLNAILDIAPLLNIGFSKVVSIGNKADIQESDLLEYFLDDEDTKIVVLYIEGLKDKRFLKVAKKLSKKKPIIALKSGRTEVGKKAAKSHTGSLAGEDVIYEAAFKEAGIIRAYTFEELVDLIHLFSTQPTISSNEIGIITNAGGFGVLAADSCVDYNMKLSNFEKSTIEKLKNILPPTANISNPLDIIGDATPERYKKVIEVLAEDSNVKGLLVILTPQEMTKPLEVAKSIIEVKNSHKEFKNKPLITSFVGGVSVKGAKSYLRKNGIPAYITPENGVKALSHLYKYSLMKVKEDYDEYLENIKEEFIKITEENKEIIKELLSNPNEYTAKKLLSIYGLPVPKGYLAKNEDEALEYCKKLGKCVMKIVSPQIIHKTEAGGVIINPKNPKEAFKKLIENAKEYAKRMGIDNLIIEGVLVEEFIEKDMMEIIIGAKRDDIFGSVVMVGLGGVFVEVLKDVSFGISPITRDFAHEMLRELKSYKVLEGVRGRPKRDINFIVDTLIKIGVFMDIHKEIKELDLNPVFVFNEKEGGCIGDARIIK | Function: Catalyzes the formation of acetate and ATP from acetyl-CoA by using ADP and phosphate. Can also use butyryl-CoA, but not phenylacetyl-CoA. Cannot catalyze the reverse reaction.
Catalytic Activity: acetate + ATP + CoA = acetyl-CoA + ADP + phosphate
Sequence Mass (Da): 78172
Sequence Length: 704
EC: 6.2.1.13
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Q10714 | MRLFLLALLATLAVTQALVKEEIQAKEYLENLNKELAKRTNVETEAAWAYGSNITDENEKKKNEISAELAKFMKEVASDTTKFQWRSYQSEDLKRQFKALTKLGYAALPEDDYAELLDTLSAMESNFAKVKVCDYKDSTKCDLALDPEIEEVISKSRDHEELAYYWREFYDKAGTAVRSQFERYVELNTKAAKLNNFTSGAEAWLDEYEDDTFEQQLEDIFADIRPLYQQIHGYVRFRLRKHYGDAVVSETGPIPMHLLGNMWAQQWSEIADIVSPFPEKPLVDVSAEMEKQGYTPLKMFQMGDDFFTSMNLTKLPQDFWDKSIIEKPTDGRDLVCHASAWDFYLTDDVRIKQCTRVTQDQLFTVHHELGHIQYFLQYQHQPFVYRTGANPGFHEAVGDVLSLSVSTPKHLEKIGLLKDYVRDDEARINQLFLTALDKIVFLPFAFTMDKYRWSLFRGEVDKANWNCAFWKLRDEYSGIEPPVVRSEKDFDAPAKYHISADVEYLRYLVSFIIQFQFYKSACIKAGQYDPDNVELPLDNCDIYGSAAAGAAFHNMLSMGASKPWPDALEAFNGERIMSGKAIAEYFEPLRVWLEAENIKNNVHIGWTTSNKCVSS | Cofactor: Binds 1 zinc ion per subunit.
Function: May be involved in the specific maturation or degradation of a number of bioactive peptides. May play a role in the contractions of the heart, gut and testes, and in spermatid differentiation.
PTM: Glycosylated.
Catalytic Activity: Release of a C-terminal dipeptide, oligopeptide-|-Xaa-Yaa, when Xaa is not Pro, and Yaa is neither Asp nor Glu. Thus, conversion of angiotensin I to angiotensin II, with increase in vasoconstrictor activity, but no action on angiotensin II.
Sequence Mass (Da): 70914
Sequence Length: 615
Subcellular Location: Secreted
EC: 3.4.15.1
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Q6Q4G4 | MNLINFSYLNLLFGAGLFSVLESATILNTESDAKKWLTTYNDEAGKYIYDATEAEWNYNTNLTDHNLGISIKKSNDLATFTEQKAIEANKKFVWKNFTDPLLKREFSKITDIGTASLSDEDFQKMSGLNSDLTKIYSTAKVCNKPNDPSGKCYPLDPDLSDIISKSNDLEELTWAWKGWRDASGKHMPDKYDEFVQLLNKAANINGYEDNGDYWRSWYESPTFRKDCEDLWQEIKPFYEQLHAYVRRKLQKKYPQIAFPKEGHIPAHLLGNMWAQSWENIEYLLRPAPDLPSMDITEELVKQNYTALKLFQLSDTFFKSLGLIQMPQPFWEKSMIEKPADRDVVCHASAWDFYNRKDFRIKQCTVVDMHWFMTTHHEMGHIEYYLHYKDQPISFRSGANPGFHEAIADIASLSVATPEYMQSVSLLPNFTDDPNGDLNFLMNQALTKVAFLPFGYLIDQWRWDVFSGDTPRPKYNSKWWHNRCKYQGVYPPVIRSEQDFDAGSKFHVPNNTPYIRYFVAHIIQFQFHEALCKAANNSRPLHRCNIANSKEAGKKLAELMKSGSSIPWPKVLENLTGSEKMSAKSLMAYYKPLIDWPEKRKPRAENWMGGKMSSWIV | Cofactor: Binds 1 zinc ion per subunit.
Catalytic Activity: Release of a C-terminal dipeptide, oligopeptide-|-Xaa-Yaa, when Xaa is not Pro, and Yaa is neither Asp nor Glu. Thus, conversion of angiotensin I to angiotensin II, with increase in vasoconstrictor activity, but no action on angiotensin II.
Sequence Mass (Da): 71481
Sequence Length: 616
Subcellular Location: Secreted
EC: 3.4.15.1
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P58382 | MEALLVINAGSSSLKFQIFGIATAGLERQVRAKLDGIATQPRLKATAADGTELINRRLDATAVPDLPEALSVARDWLATLRGFDLRAIGHRVVHGGPDYVRPVLIETTVLDRLASYQDLAPLHQPNNLAPIRLAMDIKPDVPQVACFDTAFHRGRTEHTDCYALPRTFYEQGVRRYGFHGISYEYIAGRLREVAPEVARGRVIVAHLGSGASMCALKDGRSVETTMGFTALDGLPMGTRPGQLDPGVVLHLLTDQGMSAQAVSDLLYHRSGLKGLSGISNDMRELLGSDDPRASFAIDHFVHRCALDAGMLAAALGGLDAFVFTAGIGENSAPIRARVSEGLAWLGAELDPAANDAGASVISKAGSRVALHVMPTDEELMIARHTLAIIRAR | Cofactor: Mg(2+). Can also accept Mn(2+).
Function: Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction.
Catalytic Activity: acetate + ATP = acetyl phosphate + ADP
Sequence Mass (Da): 42023
Sequence Length: 392
Pathway: Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis; acetyl-CoA from acetate: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.7.2.1
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Q9X449 | MDALLVVNAGSSSLKFQVFGIVGMDLTRQIRGKVDGIGTRPRLQATAADGTQLIDQTYDAKAVRDLPAAITEARRWLLTLEGFELQAVGHRVVHGGPDYTRPVLIDATVLDHLAGYQDLAPLHQPNNLAPIRLAMEINPDVPQVACFDTAFHRGHAKHTDCYALPRSFYDEGVRRYGFHGLSYEYIAERLREVASRAAKGRVVVAHLGSGASMCGLRDGRSIESTMLHRPSTGCRWDTPGQLDPGVVLYLILQKGMKAQAVSDLLYHDAGLKGLSGLSNDMRDLLASDDPHAALSVAHFVYRCVLNGGMLAAALGGIDAFVFTAGVGENSPPIRARIVEGLAWLGAELDPAANEAGAALISTATSRVAVHVLPTDEELMIARHTLALISAPNA | Cofactor: Mg(2+). Can also accept Mn(2+).
Function: Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction.
Catalytic Activity: acetate + ATP = acetyl phosphate + ADP
Sequence Mass (Da): 42135
Sequence Length: 393
Pathway: Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis; acetyl-CoA from acetate: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.7.2.1
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Q6N143 | MSDVLLVLNAGSSSIKFALYEAHTEPTADHLICEGGIGSLGHRPHFKVVNSDGSTRYDTYLPEGTSHDDAMAVLIGWIETTFPEHRLSAVGHRVVHGGALFDGPVDVTPEVIAQLRAFDRLAPLHQPHNVSAIEALAKLHPSLPQIACFDTAFHHRLPEVATAFALPRELTEQGVRRYGFHGLSYEYIAGRLPDVAGQAVADGRVVVAHLGAGASMCAMLRCRSIATTMGFTALDGLMMGSRCGELDPGVVLYLLEEKSMTAREIEDLLYRESGLLGVSGISDDMRTLLASDDPHACEAIELFVYRIARELGSLAAALGGLDALVFTGGIGEHASEIRRRVCEQAAWLGVTLDPDANASLSGAGRISAPDSKVSAWAIPTDEDLMIARHVWRLADGGR | Cofactor: Mg(2+). Can also accept Mn(2+).
Function: Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction.
Catalytic Activity: acetate + ATP = acetyl phosphate + ADP
Sequence Mass (Da): 42663
Sequence Length: 398
Pathway: Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis; acetyl-CoA from acetate: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.7.2.1
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Q54YA0 | MTNSNFNHGNHGSNLPARLFTKQSQALIYNYKEAAVQRMLDFDNVSQRDTPSVGGLIHPGSDGGMYKAFFGFKELVIPVYNSVSEACQQCPNADVFLNFASHRSAYQSSLLALREPSIQTVVIIAEGVPENEARSLISIAKKLGKVIIGPATVGGIQAGCFKIGNTAGTIVYIMACKLYRSGSVGFVSKSGGLSNEMYNVLSRCTDGIYEGIAIGGDAFPGSTLTDHALRYEKLPEVQMIVILGELGGWDEYGIVEALKKGEITKPICAWVSGTVAKIFPTEVQFGHAGAKSGGETESADAKNKALREAGAVVPTSFEDFSNVIAATYAKLQSKGLVKPVEEPTPPELPLDFKTAVKAGKVRKPTSIISTICDDRGDELSYAGVPISEVCKEQYNMGDVIGLLWFKRKLPPYASKFFEMCLKLVADHGPCVSGAHNTIVAARAGKDLVSSLVSGLLTIGPRFGGAIDDSARVFQDAVDNNLQPSQFVEGMKSKGKRIPGIGHLIKSADEIDKRVVLLKDYAFTHFSSTKYLEYALEVEKYTLQKANNLILNVDGCIGVLFLDLLHSSGLFTQHEIKEIIDVGYLNGFFIVGRSVGLIGHALDQRRNKQGLYRHQADDVHYAL | Function: ATP-citrate synthase is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA in many tissues.
Catalytic Activity: acetyl-CoA + ADP + oxaloacetate + phosphate = ATP + citrate + CoA
Sequence Mass (Da): 67320
Sequence Length: 622
Subcellular Location: Cytoplasm
EC: 2.3.3.8
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Q18007 | MPNYTVPPDPADTSWDSPYSIPVQIVVWIIIIVLSLETIIGNAMVVMAYRIERNISKQVSNRYIVSLAISDLIIGIEGFPFFTVYVLNGDRWPLGWVACQTWLFLDYTLCLVSILTVLLITADRYLSVCHTAKYLKWQSPTKTQLLIVMSWLLPAIIFGIMIYGWQAMTGQSTSMSGAECSAPFLSNPYVNMGMYVAYYWTTLVAMLILYKGIHQAAKNLEKKAKAKERRHIALILSQRLGTQVGVSLMLQSKAEKEKAEEAQKDSGYTSNQAGDANNLRRFGFSEPETSQFRVDPNSNNNLNVEGSLNTENDQNLGVIEEERSGFLSRRESNESYYPGPHPTAANSRRCSEMEKVSLLSESDGVPSTRPAKSYGRLSLRSRYSASESITTTHENDEKEVEKADSLQKLFADDELGSVLNFKEEKLKNTDSNNDSDTTSVILQRSRKYKKNKRPRSSRRSEHSTPRQIAKVKQAEGTAAQLIEESVPDDDQTETIEVKRTDRWVVSMKKRIARALIRRRSTTRPERGSSSNSDDSSSEVEGEEKPEVRNNGLKIPQLTVNNENRGETSSQPGRDRLAPPNKTDTFLSASGVSRKISTISTVITREKVISSIFAPIAVFNRGRKQTKAEKRAHKAFRTITFIVGFFAILWSPYYIMATVYGFCKGECIPSFLYTLSYYMCYLNSSGNPFAYALANRQFRSAFMRMFRGNFNKVA | Function: The muscarinic acetylcholine receptor mediates various cellular responses, including inhibition of adenylate cyclase, breakdown of phosphoinositides and modulation of potassium channels through the action of G proteins. Primary transducing effect is Pi turnover.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 80404
Sequence Length: 713
Subcellular Location: Cell membrane
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P16395 | MEPVMSLALAAHGPPSILEPLFKTVTTSTTTTTTTTTSTTTTTASPAGYSPGYPGTTLLTALFENLTSTAASGLYDPYSGMYGNQTNGTIGFETKGPRYSLASMVVMGFVAAILSTVTVAGNVMVMISFKIDKQLQTISNYFLFSLAIADFAIGAISMPLFAVTTILGYWPLGPIVCDTWLALDYLASNASVLNLLIISFDRYFSVTRPLTYRAKRTTNRAAVMIGAAWGISLLLWPPWIYSWPYIEGKRTVPKDECYIQFIETNQYITFGTALAAFYFPVTIMCFLYWRIWRETKKRQKDLPNLQAGKKDSSKRSNSSDENTVVNHASGGLLAFAQVGGNDHDTWRRPRSESSPDAESVYMTNMVIDSGYHGMHSRKSSIKSTNTIKKSYTCFGSIKEWCIAWWHSGREDSDDFAYEQEEPSDLGYATPVTIETPLQSSVSRCTSMNVMRDNYSMGGSVSGVRPPSILLSDVSPTPLPRPPLASISQLQEMSAVTASTTANVNTSGNGNGAINNNNNASHNGNGAVNGNGAGNGSGIGLGTTGNATHRDSRTLPVINRINSRSVSQDSVYTILIRLPSDGASSNAANGGGGGPGAGAAASASLSMQGDCAPSIKMIHEDGPTTTAAAAPLASAAATRRPLPSRDSEFSLPLGRRMSHAQHDARLLNAKVIPKQLGKAGGGAAGGGVGGAHALMNARNAAKKKKKSQEKRQESKAAKTLSAILLSFIITWTPYNILVLIKPLTTCSDCIPTELWDFFYALCYINSTINPMCYALCNATFRRTYVRILTCKWHTRNREGMVRGVYN | Function: The muscarinic acetylcholine receptor mediates various cellular responses, including inhibition of adenylate cyclase, breakdown of phosphoinositides and modulation of potassium channels through the action of G proteins. Primary transducing effect is Pi turnover. May have a role in the processing of olfactory and mechanosensory signals; regulation of neurosecretion.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 86623
Sequence Length: 805
Subcellular Location: Cell membrane
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P11229 | MNTSAPPAVSPNITVLAPGKGPWQVAFIGITTGLLSLATVTGNLLVLISFKVNTELKTVNNYFLLSLACADLIIGTFSMNLYTTYLLMGHWALGTLACDLWLALDYVASNASVMNLLLISFDRYFSVTRPLSYRAKRTPRRAALMIGLAWLVSFVLWAPAILFWQYLVGERTVLAGQCYIQFLSQPIITFGTAMAAFYLPVTVMCTLYWRIYRETENRARELAALQGSETPGKGGGSSSSSERSQPGAEGSPETPPGRCCRCCRAPRLLQAYSWKEEEEEDEGSMESLTSSEGEEPGSEVVIKMPMVDPEAQAPTKQPPRSSPNTVKRPTKKGRDRAGKGQKPRGKEQLAKRKTFSLVKEKKAARTLSAILLAFILTWTPYNIMVLVSTFCKDCVPETLWELGYWLCYVNSTINPMCYALCNKAFRDTFRLLLLCRWDKRRWRKIPKRPGSVHRTPSRQC | Function: The muscarinic acetylcholine receptor mediates various cellular responses, including inhibition of adenylate cyclase, breakdown of phosphoinositides and modulation of potassium channels through the action of G proteins. Primary transducing effect is Pi turnover.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 51421
Sequence Length: 460
Subcellular Location: Cell membrane
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Q09388 | MAVASVLLALFMLFLSIVTVIGNLAVLLSYYLDKNIRQPTNYFIFSLAISDLLIGLEGIPVYTAFYLNNNEWIWGDVLCDLWLSIDYIVCLASIYTVLGITVDRYYSVKKPATYRNWRTPGRVVLIIIFIWLVPSILFSVSIFGYGTFTGTGRILKETECYVQFMTNPYLNMGMYISYYWTTLFVMLYLYWGIYRAAKKLALKSDQKTKRLALLTEMRRPEVSVRTSDAGNSSSDSPNDTSNSSKCFRTAPPTTTVQTTQTNVGTPPPVFRNHMTLHNNNMDFTKDNEIVRPPTPPDDNTYSNPNFSMISEQLTNGFSRQEPSSVIERESTAPCVSPEPSHASLENEFNENHHAHFKPELSLPFIDADSVSSMVGHDDLRRAMSIRISRSVSMQGTARATPVIEIVENLEEALKICENLEELREDENKNEEEKQKNGLENGGMNHVIIANDEQQPSTSKESEQKEEMTPENHDPNEVKVPLIAVSRVESVKSTAGGKVRRLITQMRSHSIRSKRKANKNKSVLSALNFFQRKKEYKSRSENRARKALRTITFILGSFIILWTPFYVLATIYGFCETCKASPSFNTLYTISYYLCYMNSPLNPFCYAMANQQFKKTLTRIFKGDFRRV | Function: The muscarinic acetylcholine receptor mediates various cellular responses, including inhibition of adenylate cyclase, breakdown of phosphoinositides and modulation of potassium channels through the action of G proteins . Primary transducing effect is Pi turnover (By similarity). Regulates the activity of ventral cord motor neurons . Couples to the G(o)-alpha G-protein subunit goa-1 to negatively regulate cholinergic receptor activity in the presence of high levels of the neurotransmitter acetylcholine in ventral cord motor neurons . As acetylcholine depolarizes body wall muscles, modulation of acetylcholine levels most likely results in the control locomotory behavior and egg-laying .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 71483
Sequence Length: 627
Subcellular Location: Cell membrane
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Q83SG7 | MTDNLPEVREAQEWFRSETRRVAPITLDVMWDHFLSRHWSQLSPDFPLQEFVCYAREQVMTILPDSPPRFINLNNYLWSEQWLVRYRDMDFIQNVLNGMASRRPRLDALRDSWYDLDAHYDALETRFWQFYPRMMAQASHKAL | Function: Converts holo-ACP to apo-ACP by hydrolytic cleavage of the phosphopantetheine prosthetic group from ACP.
Catalytic Activity: H2O + holo-[ACP] = (R)-4'-phosphopantetheine + apo-[ACP] + H(+)
Sequence Mass (Da): 17418
Sequence Length: 143
EC: 3.1.4.14
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Q9PPY4 | MSINIKDLIMKIAKENKIALNMDNLNIELKSLGIDSLSAMNLIMKIEDQIGVQLPDEKLLKIKNLRDLINAFEDVLK | Function: Carrier of the growing fatty acid chain in fatty acid biosynthesis.
PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine of the apo-ACP-like protein.
Sequence Mass (Da): 8750
Sequence Length: 77
Pathway: Lipid metabolism; fatty acid biosynthesis.
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Q8ZC31 | MNFLAHLHLAALADSSLLGNLLADFVRGNPQGEYPPEIVAGIMMHRRVDVMTDTLPLVKEARTYFSADYRRVSPITLDVLWDHFLARHWDQLVPNCTLPDFLQHAQSQILPHLPHTPARFQSLNAYLWSERWLERYAELPFIADVLQGMANRRPKLAALAGSFYAIEQHYQPLEDLFLTFYPTMMRQAQHKQI | Function: Converts holo-ACP to apo-ACP by hydrolytic cleavage of the phosphopantetheine prosthetic group from ACP.
Catalytic Activity: H2O + holo-[ACP] = (R)-4'-phosphopantetheine + apo-[ACP] + H(+)
Sequence Mass (Da): 22351
Sequence Length: 193
EC: 3.1.4.14
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Q7PC63 | MDKQRIFEVLITNICEVLPELDGHRFEPEDQLVELGADSVDRAEIITMVLEDLSLKIPRIELSGVKNIGELAEVLYDKVQSA | Function: Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism.
PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine of apo-ACP by sfp.
Sequence Mass (Da): 9252
Sequence Length: 82
Pathway: Antibiotic biosynthesis; bacillaene biosynthesis.
Subcellular Location: Cytoplasm
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P53665 | MALRNAILRHLRVPVQTLGLNQSKIGFLGTIRSFSSHDDHLSREAVVDRVLDVVKSFPKVDPSKVTPEVHFQNDLGLDSLDTVEIVMAIEEEFKLEIPDKEADKIDSCSLAIEYVYNHPMSS | Function: Carrier of the growing fatty acid chain in fatty acid biosynthesis (By similarity). May be involved in the synthesis of short and medium chain fatty acids. Accessory and non-catalytic subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), which functions in the transfer of electrons from NADH to the respiratory chain (By similarity).
PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine of the apo-ACP-like protein.
Sequence Mass (Da): 13718
Sequence Length: 122
Pathway: Lipid metabolism; fatty acid biosynthesis.
Subcellular Location: Mitochondrion
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O80800 | MAARGAMLRYLRVNVNPTIQNPRECVLPFSILLRRFSEEVRGSFLDKSEVTDRVLSVVKNFQKVDPSKVTPKANFQNDLGLDSLDSVEVVMALEEEFGFEIPDNEADKIQSIDLAVDFIASHPQAK | Function: Carrier of the growing fatty acid chain in fatty acid biosynthesis (By similarity). May be involved in the synthesis of short and medium chain fatty acids. Accessory and non-catalytic subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), which functions in the transfer of electrons from NADH to the respiratory chain (By similarity).
PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine of the apo-ACP-like protein.
Sequence Mass (Da): 14167
Sequence Length: 126
Pathway: Lipid metabolism; fatty acid biosynthesis.
Subcellular Location: Mitochondrion
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Q9FGJ4 | MHCIRSSILQHLRLRVSVRPTSLLQNENGFKSIGIFNFTSEAAADGGQDQILSRVIELVKKYDKTNTSEVTERADFQKDLSLDSLDKTELVMAIEEEFSIEIPDEKADKLTCCGDVATYILSETPTKASES | Function: Carrier of the growing fatty acid chain in fatty acid biosynthesis (By similarity). May be involved in the synthesis of short and medium chain fatty acids. Accessory and non-catalytic subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), which functions in the transfer of electrons from NADH to the respiratory chain (By similarity).
PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine of the apo-ACP-like protein.
Sequence Mass (Da): 14615
Sequence Length: 131
Pathway: Lipid metabolism; fatty acid biosynthesis.
Subcellular Location: Mitochondrion
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P52505 | MAVRVLCACVRRLPTAFAPLPRLPTLAAARPLSTTLFAAETRTRPGAPLPALVLAQVPGRVTQLCRQYSDAPPLTLEGIKDRVLYVLKLYDKIDPEKLSVNSHFMKDLGLDSLDQVEIIMAMEDEFGFEIPDIDAEKLMCPQEIVDYIADKKDVYE | Function: Carrier of the growing fatty acid chain in fatty acid biosynthesis . Accessory and non-catalytic subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), which functions in the transfer of electrons from NADH to the respiratory chain . Accessory protein, of the core iron-sulfur cluster (ISC) assembly complex, that regulates, in association with LYRM4, the stability and the cysteine desulfurase activity of NFS1 and participates in the [2Fe-2S] clusters assembly on the scaffolding protein ISCU (By similarity). The core iron-sulfur cluster (ISC) assembly complex is involved in the de novo synthesis of a [2Fe-2S] cluster, the first step of the mitochondrial iron-sulfur protein biogenesis. This process is initiated by the cysteine desulfurase complex (NFS1:LYRM4:NDUFAB1) that produces persulfide which is delivered on the scaffold protein ISCU in a FXN-dependent manner. Then this complex is stabilized by FDX2 which provides reducing equivalents to accomplish the [2Fe-2S] cluster assembly. Finally, the [2Fe-2S] cluster is transferred from ISCU to chaperone proteins, including HSCB, HSPA9 and GLRX5 (By similarity).
PTM: Phosphopantetheinylation at Ser-112 is essential for interactions with LYR motif-containing proteins.
Sequence Mass (Da): 17402
Sequence Length: 156
Subcellular Location: Mitochondrion
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Q54E22 | MIRNTFKLVSNIAVRPAFSSTFVRQPIVASSMMVRNYGSISEKEITDRVIGVVSQYDKVSGKTVTPTTTFKELGLDSLDSADILVAVEEEFGIEIPDEEADKITSCAETISYLRKTPTAK | Function: Carrier of the growing fatty acid chain in fatty acid biosynthesis. May be involved in the synthesis of very-long-chain fatty acids. Accessory and non-catalytic subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), which functions in the transfer of electrons from NADH to the respiratory chain (By similarity).
PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine of apo-ACP by acpS. This modification is essential for activity because fatty acids are bound in thioester linkage to the sulfhydryl of the prosthetic group (By similarity).
Sequence Mass (Da): 13196
Sequence Length: 120
Pathway: Lipid metabolism; fatty acid biosynthesis.
Subcellular Location: Mitochondrion
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Q8R857 | MEIFVGTDIMEVERIKKILEKRPHFLERIFTEKEREFLRKKKNPWPHLAGFFSAKESVSKVLGTGIRGFSWQDIEIIHNEYGKPEVVLKGKAKAIAAEKGIKEIKLSISHTSDYAMSVAIAVGGENS | Function: Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
Catalytic Activity: apo-[ACP] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-[ACP]
Sequence Mass (Da): 14386
Sequence Length: 127
Subcellular Location: Cytoplasm
EC: 2.7.8.7
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A4XIB7 | MIFNIGIDIVEVERFKNIKRFDSFLKRVFTQKELEYIRSKNFNMLTIAGYFAAKEAVAKALSTGIVFGFKDIEIQKDTNGCPKVKLYNRAKEICENLKITNIVLSISHQNSVAVACAIAEKEE | Function: Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
Catalytic Activity: apo-[ACP] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-[ACP]
Sequence Mass (Da): 13982
Sequence Length: 123
Subcellular Location: Cytoplasm
EC: 2.7.8.7
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A7I379 | MIGIDIVSISRISKIYTKFGDKFLDKILSGNEQNSVLNLNYNLKLERLAGIYAAKEAFAKALGVGISADFGFLDVEILKNDRGAPFLEIAPCIIKKFNIKNADVSITHDGGFAISAVILEMSKF | Function: Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
Catalytic Activity: apo-[ACP] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-[ACP]
Sequence Mass (Da): 13558
Sequence Length: 124
Subcellular Location: Cytoplasm
EC: 2.7.8.7
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Q9PMP8 | MRVGCDIIAISRIEKIHSRHGKNFLDKFLNPKEQILIKNPATLAGLWAAKEAASKALGVGICELCSFFDIEISKDEKNAPKLKYSQKITKDFNITQTSLSISHDNGFAIAIVAVV | Function: Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
Catalytic Activity: apo-[ACP] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-[ACP]
Sequence Mass (Da): 12658
Sequence Length: 115
Subcellular Location: Cytoplasm
EC: 2.7.8.7
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Q9A807 | MIIGIGSDLCDIRRIEKSLERFGDRFTHKVFTETERTRSERKPDRASSYAKRFAAKEACSKALGTGLKRGVHLAGMGVVNLPSGQPTMALTGGALERLKAMVPEGMEPVIHLSLTDDHPYAQAFVIIEALPKR | Function: Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
Catalytic Activity: apo-[ACP] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-[ACP]
Sequence Mass (Da): 14622
Sequence Length: 133
Subcellular Location: Cytoplasm
EC: 2.7.8.7
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Q2RGI1 | MLEAGIDIIEISRLERSIKRHPRLLARVFTPAEVAYCLARHRPGASLAARFAAKEAVMKALGIGLGRCSWQDIEITREQGGRPRVILHNRARQLARELGVGEITVSLSHCHAYAAAVALVESSFSEEG | Function: Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
Catalytic Activity: apo-[ACP] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-[ACP]
Sequence Mass (Da): 14027
Sequence Length: 128
Subcellular Location: Cytoplasm
EC: 2.7.8.7
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Q7NB74 | MIIGVGIDVVSIDRFQAKKSDEFIKKLLTEHEQNKYKTVIGESNQNIFLAIRWSLKEAIFKALKTWDEFTQLEIRKIHGAYECSLNEKIKLHLSISHEGQRLVAMAVAERI | Function: Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
Catalytic Activity: apo-[ACP] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-[ACP]
Sequence Mass (Da): 12842
Sequence Length: 111
Subcellular Location: Cytoplasm
EC: 2.7.8.7
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B2HPL7 | MGIVGVGIDLVSIPDFAEQVDQPGTAFAATFTPGERRDASDKSSSAARHLAARWAAKEAVIKAWSGSRFAQRPVLPEDIHRDIEVVTDMWGRPRVRLTGEIAKHLADVTIHVSLTHEGDTAAAVAILETS | Function: Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
Catalytic Activity: apo-[ACP] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-[ACP]
Sequence Mass (Da): 13968
Sequence Length: 130
Subcellular Location: Cytoplasm
EC: 2.7.8.7
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Q6MT35 | MINNVGIDIVENKRIKLKKEFIIKVLSTNEIQTFNTKTKKQKKEFLAGRWAVKEAIIKTLDQAISMNKIDIEYVNQKPVIQNKELQNILISISHEKKYAIGIALKQSDNK | Function: Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
Catalytic Activity: apo-[ACP] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-[ACP]
Sequence Mass (Da): 12710
Sequence Length: 110
Subcellular Location: Cytoplasm
EC: 2.7.8.7
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P75480 | MILGIGIDLVEIKRFEQLARQTDNCFAKRLLTSTEYAHYAKLRKDSEKSSFLAVHWSLKEAIYKAVNHIKPLFSQLEITKKNQRYNCQIDPKIELLLSVSYSSNNITAICLAQQTPWKN | Function: Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
Catalytic Activity: apo-[ACP] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-[ACP]
Sequence Mass (Da): 13774
Sequence Length: 119
Subcellular Location: Cytoplasm
EC: 2.7.8.7
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Q98R97 | MTLIMIGVDLVKIERLENKSDHFVRKILSLDEYELYQKTKAKAIFLATRWAIKEALFKADNQHFCFKKINITKKDNVYKFDGFAISVSSEKEYVIAFVQKIGVACHRD | Function: Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
Catalytic Activity: apo-[ACP] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-[ACP]
Sequence Mass (Da): 12606
Sequence Length: 108
Subcellular Location: Cytoplasm
EC: 2.7.8.7
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A0R1H6 | MAIVGVGIDLVSIPDFAEQVDRPGTVFAETFTPGERRDAADKSSSAARHLAARWAAKEAVIKAWSSSRFSKRPALPEGIHRDIEVVTDMWGRPKVRLSGEIAKHLEDVTIHVSLTHEDQTAAAVAIIEEP | Function: Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
Catalytic Activity: apo-[ACP] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-[ACP]
Sequence Mass (Da): 14165
Sequence Length: 130
Subcellular Location: Cytoplasm
EC: 2.7.8.7
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Q30SB4 | MIGIDIIKISRMGALLERFGSKAMGRFLSKDEIELVKNHKTASGFWAAKEACSKALGVGIGAECGFHDITIFKSSNGAPNIRLSQKIVKEFNVKSISLSITHDGEYAIAVVTIESTAANKI | Function: Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
Catalytic Activity: apo-[ACP] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-[ACP]
Sequence Mass (Da): 13013
Sequence Length: 121
Subcellular Location: Cytoplasm
EC: 2.7.8.7
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A6Q7U5 | MKVGTDIIQIDRIEKLIDRYGDTFKQRYLSKEEIAAAKKVETLAGYWAAKEAIAKAFGCGIGAQLAFHDIMIAKDSRGAPYFTLSDEALKTYTIHSASISISHDGGFAIAVAAIDFEAA | Function: Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
Catalytic Activity: apo-[ACP] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-[ACP]
Sequence Mass (Da): 12904
Sequence Length: 119
Subcellular Location: Cytoplasm
EC: 2.7.8.7
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Q67K77 | MILGTGVDIVAVERVARAVERHGDRFLRRVFTPGELAYCTSSEAHRAARLAARFAAKEAVLKALGIGLREVRWTDAEVCRDERGRPSVRLTGRLAEIAAARGATRIHLSLSHTQEYAVAQVVIEG | Function: Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
Catalytic Activity: apo-[ACP] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-[ACP]
Sequence Mass (Da): 13676
Sequence Length: 125
Subcellular Location: Cytoplasm
EC: 2.7.8.7
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Q2LTJ7 | MVHGTGIDLVDIDRLEKILMKWDMSFLKKVFSPAEIEYCAKRAFPAIHYAARFAAKESFLKSLGMGIGMGIPLKDIEVRNDPLGRPVLNLYGKALEILEKRGITTVHVSLSHSRSQAGAVVILEGLKD | Function: Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
Catalytic Activity: apo-[ACP] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-[ACP]
Sequence Mass (Da): 14165
Sequence Length: 128
Subcellular Location: Cytoplasm
EC: 2.7.8.7
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Q8R9W1 | MIFEKVRNIIAEQLGIDPEEITMESSFIDDLGADSLDIVELIMALEEEFDIEIPDEDAEKIKTVGDVVEYLSNIVE | Function: Carrier of the growing fatty acid chain in fatty acid biosynthesis.
PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine of apo-ACP by AcpS. This modification is essential for activity because fatty acids are bound in thioester linkage to the sulfhydryl of the prosthetic group.
Sequence Mass (Da): 8589
Sequence Length: 76
Pathway: Lipid metabolism; fatty acid biosynthesis.
Subcellular Location: Cytoplasm
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A7GWR1 | MAVFDDVRDVVVEQLSVDPEAVKMESKIIEDLGADSLDVVELVMALEEKFEVEIPDTEAEKLISIADVVNYIEKLGK | Function: Carrier of the growing fatty acid chain in fatty acid biosynthesis.
PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine of apo-ACP by AcpS. This modification is essential for activity because fatty acids are bound in thioester linkage to the sulfhydryl of the prosthetic group.
Sequence Mass (Da): 8566
Sequence Length: 77
Pathway: Lipid metabolism; fatty acid biosynthesis.
Subcellular Location: Cytoplasm
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A7HZZ5 | MEVFEEVRDVVVEQLSVAPDAVKIDSKIIEDLGADSLDVVELVMALEEKFGIEIPDSEAEKLISIKDVVTYIENLNKNK | Function: Carrier of the growing fatty acid chain in fatty acid biosynthesis.
PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine of apo-ACP by AcpS. This modification is essential for activity because fatty acids are bound in thioester linkage to the sulfhydryl of the prosthetic group.
Sequence Mass (Da): 8819
Sequence Length: 79
Pathway: Lipid metabolism; fatty acid biosynthesis.
Subcellular Location: Cytoplasm
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A7H4T8 | MATFDDVKAVVAEQLSIDADAVKMESKIIEDLGADSLDVVELIMALEEKFEVEIPDSDAEKLIKIEDVVNYIDNLKK | Function: Carrier of the growing fatty acid chain in fatty acid biosynthesis.
PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine of apo-ACP by AcpS. This modification is essential for activity because fatty acids are bound in thioester linkage to the sulfhydryl of the prosthetic group.
Sequence Mass (Da): 8570
Sequence Length: 77
Pathway: Lipid metabolism; fatty acid biosynthesis.
Subcellular Location: Cytoplasm
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Q3AC56 | MAGVFERVKKIIVDQLGVEEDEVTMEASFIDDLGADSLDIVELIMAFEEEFELEIPDEDAEKIRTVGDAVNYIQERV | Function: Carrier of the growing fatty acid chain in fatty acid biosynthesis.
PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine of apo-ACP by AcpS. This modification is essential for activity because fatty acids are bound in thioester linkage to the sulfhydryl of the prosthetic group.
Sequence Mass (Da): 8722
Sequence Length: 77
Pathway: Lipid metabolism; fatty acid biosynthesis.
Subcellular Location: Cytoplasm
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B3PEV2 | MSSIEERVKKIVAEQLGVKEEEVKNEASFVEDLGADSLDTVELVMALEEEFETEIPDEEAEKITTVQLAIDYINANLA | Function: Carrier of the growing fatty acid chain in fatty acid biosynthesis.
PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine of apo-ACP by AcpS. This modification is essential for activity because fatty acids are bound in thioester linkage to the sulfhydryl of the prosthetic group.
Sequence Mass (Da): 8701
Sequence Length: 78
Pathway: Lipid metabolism; fatty acid biosynthesis.
Subcellular Location: Cytoplasm
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Q5FPB9 | MSDIADKVKKIVVEHLGVDESKVTPDASFIDDLGADSLDTVELVMAFEEAFSVEIPEDAAEKIATVKDAIDYIEKQKAA | Function: Carrier of the growing fatty acid chain in fatty acid biosynthesis.
PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine of apo-ACP by AcpS. This modification is essential for activity because fatty acids are bound in thioester linkage to the sulfhydryl of the prosthetic group.
Sequence Mass (Da): 8570
Sequence Length: 79
Pathway: Lipid metabolism; fatty acid biosynthesis.
Subcellular Location: Cytoplasm
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Q0BPZ5 | MSEVADKVKKIVVEHLGVEESKVTPEASFIDDLGADSLDTVELVMAFEEAFGVEIPEDAAEKISTVKDAVEYIEKQKAA | Function: Carrier of the growing fatty acid chain in fatty acid biosynthesis.
PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine of apo-ACP by AcpS. This modification is essential for activity because fatty acids are bound in thioester linkage to the sulfhydryl of the prosthetic group.
Sequence Mass (Da): 8584
Sequence Length: 79
Pathway: Lipid metabolism; fatty acid biosynthesis.
Subcellular Location: Cytoplasm
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Q6B8U3 | MSSSIFDKVQNIVANQLGVEKDKVTEDAKFAALGADSLDTVELVMAIEDAFSIDIPDEDAEKIANLSQAIEFIQHAIDKKKD | Function: Carrier of the growing fatty acid chain in fatty acid biosynthesis.
PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine of apo-ACP by AcpS. This modification is essential for activity because fatty acids are bound in thioester linkage to the sulfhydryl of the prosthetic group.
Sequence Mass (Da): 8953
Sequence Length: 82
Pathway: Lipid metabolism; fatty acid biosynthesis.
Subcellular Location: Plastid
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P29189 | MNEQEIFEKVQTIISEQLGVDKSQVTKDANFANDLGADSLDTVELVMAIEEAFNIEIPDDAAEQISNLQQAVDFISQKVAA | Function: Carrier of the growing fatty acid chain in fatty acid biosynthesis.
PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine of apo-ACP by AcpS. This modification is essential for activity because fatty acids are bound in thioester linkage to the sulfhydryl of the prosthetic group.
Sequence Mass (Da): 8886
Sequence Length: 81
Pathway: Lipid metabolism; fatty acid biosynthesis.
Subcellular Location: Plastid
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B0TGW1 | MSSIFDKVKAIVVEQLGVDEEEVTMETSFEDLNADSLDIVELVMALEEEFDIEIPDEDAEKIKTIGSAVEYIKENQ | Function: Carrier of the growing fatty acid chain in fatty acid biosynthesis.
PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine of apo-ACP by AcpS. This modification is essential for activity because fatty acids are bound in thioester linkage to the sulfhydryl of the prosthetic group.
Sequence Mass (Da): 8569
Sequence Length: 76
Pathway: Lipid metabolism; fatty acid biosynthesis.
Subcellular Location: Cytoplasm
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P0A2W0 | MAVFEKVQEIIVEELGKDASEVTLESTFDDLDADSLDLFQVISEIEDAFDIQIEAENDLKTVGDLVAYVEEQAK | Function: Carrier of the growing fatty acid chain in fatty acid biosynthesis.
PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine of apo-ACP by AcpS. This modification is essential for activity because fatty acids are bound in thioester linkage to the sulfhydryl of the prosthetic group.
Sequence Mass (Da): 8268
Sequence Length: 74
Pathway: Lipid metabolism; fatty acid biosynthesis.
Subcellular Location: Cytoplasm
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Q2LQM3 | MTLEEKIIEIIVDQLEVTAEECVPEASFINDLGADSLDLAELLLEMEDTFDVEISTEDLKKIRKIQDVIDYLKVRNVTWD | Function: Carrier of the growing fatty acid chain in fatty acid biosynthesis.
PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine of apo-ACP by AcpS. This modification is essential for activity because fatty acids are bound in thioester linkage to the sulfhydryl of the prosthetic group.
Sequence Mass (Da): 9214
Sequence Length: 80
Pathway: Lipid metabolism; fatty acid biosynthesis.
Subcellular Location: Cytoplasm
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Q31QV1 | MSQEDIFSKVKDIVAEQLSVDVAEVKPESSFQNDLGADSLDTVELVMALEEAFDIEIPDEAAEGIATVQDAVDFIASKAA | Function: Carrier of the growing fatty acid chain in fatty acid biosynthesis.
PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine of apo-ACP by AcpS. This modification is essential for activity because fatty acids are bound in thioester linkage to the sulfhydryl of the prosthetic group.
Sequence Mass (Da): 8560
Sequence Length: 80
Pathway: Lipid metabolism; fatty acid biosynthesis.
Subcellular Location: Cytoplasm
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A0LNX9 | MDVAAMQVKIVDIIANQLGVDKEIITPEANVVDDLGADSLDVVELVMALEEAFDVEIPDEDAESIRTVKDIFDYLAKNKAA | Function: Carrier of the growing fatty acid chain in fatty acid biosynthesis.
PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine of apo-ACP by AcpS. This modification is essential for activity because fatty acids are bound in thioester linkage to the sulfhydryl of the prosthetic group.
Sequence Mass (Da): 8820
Sequence Length: 81
Pathway: Lipid metabolism; fatty acid biosynthesis.
Subcellular Location: Cytoplasm
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Q8YJ48 | MSEKLYPVLPEAKKNTLIDNETYLEWYEESVSDPDGFWAKHGRRIDWFKPFTKVKNTDFNGDVTIKWYEDGVTNVSYNCIDRHLKSRGDKVAIIWEGDNPYIDKKITYRELYENVCRMANVLKKHGVKKGDRVTIYLPMIPEAAYAMLACARIGAVHSVVFAGFSPEALAGRIVDCESTFVITADEGVRGGKPVALKENTDTAIDIAAKQYVMVNKVLVVRRTGGKVSWGRGRDLWYHQEVASVEPHCEPEPMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYASMTHQYVFDYHDGEIYWCTADVGWVTGHSYIVYGPLANGATTLMFEGVPNFPDQGRFWEVVDKHHVNIFYTAPTALRALMGAGDEFVTRSSRSTLRLLGSVGEPINPEAWEWYYNVVGDQKCPIVDTWWQTENGGILITPLPGATDLKPGSATRPFFGVKPVLVDNEGNVQEGVADGNLCISDSWPGQMRTVYGDHKRFIETYFSTYKGMYFSGDGCRRDEDGYYWITGRVDDVLNISGHRLGTAEIESALVSHHSVSEAAVVGYPHPIKGQGIYCYVTLMTGADAQDPDELRKELVQHVRKEIGPIATPDKIQFAPGLPKTRSGKIMRRILRKIAEDEFGALGDTSTLADRGVVDDLIENRQNKK | Function: Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA.
PTM: Acetylated. Deacetylation by the SIR2-homolog deacetylase activates the enzyme.
Catalytic Activity: acetate + ATP + CoA = acetyl-CoA + AMP + diphosphate
Sequence Mass (Da): 72790
Sequence Length: 651
EC: 6.2.1.1
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Q9PMD2 | MLNQNNQELFKPSKEFSRNARIKNLCEYYDLCDEAKEDFEGFWKRQAFEKIEWFSPFSRVLNEDKAPFYKWFEGGTLNVSYQCLDRHMKTRRNKAALIFEGEMGDYEVYTYRRLLHETCKAANLLKKFGVKKGDRVVIYMPMIPETAIVMLACARIGAIHSVVFGGFSPEALRDRIIDAGAKLVVTADGAFRRGKPYMLKPAVDKALSEGCESVEKVLIVIRNNEPIEYIKGRDYVYNELVKNESYKCEPEIMDSEDLLFLLYTSGSTGKPKGVMHASAGYILWAQMTMEWVFDIKDYDNYWCSADVGWITGHTYVVYGPLACGATTIMHEGTPTYPNSGRWWRMIEEYQISKFYTSPTAIRMLHADAPNEPRKYDLSTLEVLGTVGEPINPSAWKWFYDEIGGTKSPIVDTWWQTETGGHMITPLPGATPLKPGCATLPLPGIFAEVIDEEGNKKDEGEDGLLCITKPWPSMIRGIWGNDERYIESYFSQAKKDGKAVYFSGDGAFYDKNGYITITGRTDDVVNVAGHRIGTAEIESAIAKHPSVAESAVVSILDTIKGESLFAFVVLSPASSCDLGGAIETLKELNDILRVEIGPIAKIEKILYTPGLPKTRSGKIMRRILRTIARGEEIKQDISTLEDSKVVETIVKLAKAEFE | Function: Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA.
PTM: Acetylated. Deacetylation by the SIR2-homolog deacetylase activates the enzyme.
Catalytic Activity: acetate + ATP + CoA = acetyl-CoA + AMP + diphosphate
Sequence Mass (Da): 73958
Sequence Length: 657
EC: 6.2.1.1
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Q554Z5 | MFSNGLSKLIKSKIASTSIITTKNNYSISKLSFSSTSILLNKKYKLSEPFNYEQDCEYALKEPIQFWDEVASKYVHWNKRYEKVYSGDEYNPEWFKGGVLNACYNALDVHAKDPITKNRIAIIHETPSKNNTNKLTYGELWDEVCIFARGLHNLGVEKGDRVVIYMPMINQALIAMLACARLGATHSVVFGGFASPQLAQRIEHFKPKVVISANFGVEGHKINCYTPLLSKALELSSHKPNHTIVYNRLDVKLDAGEVLPPRVEGSLDWSELIKNIAPYRDYALVDSTHPLYILYTSGTTGMPKGVVRDTGGYSVALNYSIRNCYGMKSGDTFFAGSDVGWVVGHTLSVYGPLMVGLTSIIFEGKPTVPDASTYWKLIEKHRVNALFSAPTAIRAIHRDDADGKLASKCDLSSLRSIWLGGERLDSSTFNFLRNITNNKPILDNYWNTESGSPLITNPSCQVPIKANATGKPMPGYQFHVLSPTSERLGADKIGEVCIKLPVAPGFTNTLYLNPEGYKNAYLNEYPGYLRTADSGYYDENGYYHIISRVDDIINVSGHRLSTGSIEEILVKHPKIVECAVIGVHDELKGEIPFGLVVLKPQYKDCAEEVENELIKEVRENIGPVATFKKVLSVNRLPKTRSGKILRNILRKMYNKEEYTVPPTIEDMEVLKEIDIEFEKYKLSHPPKK | Function: Activates acetate so that it can be used for lipid synthesis or for energy generation.
Catalytic Activity: acetate + ATP + CoA = acetyl-CoA + AMP + diphosphate
Sequence Mass (Da): 77120
Sequence Length: 688
Subcellular Location: Mitochondrion
EC: 6.2.1.1
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Q46389 | MLIIGERINGMFGDIKRAIQERDPAPVQEWARRQEEGGARALDLNVGPAVQDKVSAMEWLVEVTQEVSNLTLCLDSTNIKAIEAGLKKCKNRAMINSTNAEREKVEKLFPLAVEHGAALIGLTMNKTGIPKDSDTRLAFAMELVAAADEFGLPMEDLYIDPLILPANVAQDHAPEVLKTLQQIKMLADPAPKTVLGLSNVSQNCQNRPLINRTFLAMAMACGLDAAIADACDEALIETAATAEILLNQTVYCDSFVKMFKTR | Function: Methyltransferase that mediates the transfer of a N5-methyl group of (6S)-methyltetrahydrofolate to the 5-methoxybenzimidazolylcobamide cofactor of a corrinoid/Fe-S protein (AcsC/AcsD) in the anaerobic acetyl-CoA pathway (Wood-Ljungdahl pathway) of carbon monoxide and carbon dioxide fixation.
Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + methyl-Co(III)-[corrinoid Fe-S protein] = (6S)-5-methyl-5,6,7,8-tetrahydrofolate + Co(I)-[corrinoid Fe-S protein] + H(+)
Sequence Mass (Da): 28609
Sequence Length: 262
EC: 2.1.1.258
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Q17QJ1 | MAVYVGMLRVARLCARSPRVLGARVGLSRVWQEARLWGVRPLSSGELDHTVPLPVGGFSYVQGHVGLHLSNKTVGRCLDATAQRVPDQEALVVHHENIRLTFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLMQLATAQAGIILVSVNPAYQAMELEYALKKVGCKALVFPKQFKTQQYYNILKQICPEVEKAQPGALKSQRLPDLTTVISVDAHLPGTLLLDEVVAAGSQEQNLTRLRHTQQFLSCHDPINIQFTSGTTGSPKGATLSHYNIVNNANMIGQRLRLHQKTPEESRVVLPSPLYHCLGSVGGTMVSLMHGVTLILCSPVFEGKKTLEAISRERGCFLYGTPTMFVDVLNQPDFSSYDISTMRGGVIAGSPAPPELIRAIINKLNMKELVVAYGTTENSPVTFMNFTEDTVEQKAESVGRVMPHTEAQIVNTETGTLTELNTPGELCIRGYCVMLGYWGEPQKTEEAIGQDKWYRTGDIAMMDEQGFCKIVGRSKDMIIRGGENIYPAELEDFFHTHPQVQEVQVVGVKDDRMGEEICACIRLKEGEKTTAEEIKAFCKGKISHFKIPRYIVFVTNYPLTVSGKIQKFKLREQMEQHLNL | Function: Acyl-CoA synthases catalyze the initial reaction in fatty acid metabolism, by forming a thioester with CoA. Has some preference toward medium-chain substrates. Plays a role in adipocyte differentiation.
Catalytic Activity: a medium chain fatty acid + ATP + CoA = a medium-chain fatty acyl-CoA + AMP + diphosphate
Sequence Mass (Da): 68201
Sequence Length: 615
Subcellular Location: Mitochondrion
EC: 6.2.1.2
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Q0P4F7 | MSSKILLTNLRTSASFCKTLKFPQRPRTPFIASQQSCAIHVDNPPSIPTLTTSYVHGLSSHPLQSSTVDQCLQATVERYPDREAMVFVQDGIRKTFAEFYQDVEKAAAGLLAAGLKRGDRLGMWGPNIYEWVLMQFATAKAGIILVAVNPAYQLQEVEFALRKVQCNAVVCPTKFKSQHYCDMLKQLCPEMETASPGGIKSSRLPDLHTVIVTDSQQPGSFLLKDLMQAGSSQHYQQLQDLQKKLVCDDPINIQFTSGTTGKPKGATLSHHNIVNNAYFTGMRIGYNWRKNVRICLPVPLYHCFGSVGGGVIMALYGTTVIFPSTGYDGRANLRAIEKEKCTFVYGTPTMYIDMLGQPDLAKFDLSSVRGGIAAGSPCPPEVMRKILNVMGIKEMVIGYGTTENSPVTFCGFPVDSAERKIVTVGCISPHTEAKVVDPTTGEIVPLGAQGELMIRGYCVMLEYWQDEEKTRECITKDRWYKTGDIASLDQFAYCKIEGRIKDLIIRGGENIYPAEIEQFLHTHPKILEAQVVGVKDERMGEEVCACIRLKEGQECTVEEIKAYCKGKIAHYKVPRYILFVQDYPLTITGKIQKHKLRERTEKQLGL | Function: Acyl-CoA synthases catalyze the initial reaction in fatty acid metabolism, by forming a thioester with CoA. Has some preference toward medium-chain substrates. Plays a role in adipocyte differentiation.
Catalytic Activity: a medium chain fatty acid + ATP + CoA = a medium-chain fatty acyl-CoA + AMP + diphosphate
Sequence Mass (Da): 67514
Sequence Length: 606
Subcellular Location: Mitochondrion
EC: 6.2.1.2
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Q96CM8 | MAVYVGMLRLGRLCAGSSGVLGARAALSRSWQEARLQGVRFLSSREVDRMVSTPIGGLSYVQGCTKKHLNSKTVGQCLETTAQRVPEREALVVLHEDVRLTFAQLKEEVDKAASGLLSIGLCKGDRLGMWGPNSYAWVLMQLATAQAGIILVSVNPAYQAMELEYVLKKVGCKALVFPKQFKTQQYYNVLKQICPEVENAQPGALKSQRLPDLTTVISVDAPLPGTLLLDEVVAAGSTRQHLDQLQYNQQFLSCHDPINIQFTSGTTGSPKGATLSHYNIVNNSNILGERLKLHEKTPEQLRMILPNPLYHCLGSVAGTMMCLMYGATLILASPIFNGKKALEAISRERGTFLYGTPTMFVDILNQPDFSSYDISTMCGGVIAGSPAPPELIRAIINKINMKDLVVAYGTTENSPVTFAHFPEDTVEQKAESVGRIMPHTEARIMNMEAGTLAKLNTPGELCIRGYCVMLGYWGEPQKTEEAVDQDKWYWTGDVATMNEQGFCKIVGRSKDMIIRGGENIYPAELEDFFHTHPKVQEVQVVGVKDDRMGEEICACIRLKDGEETTVEEIKAFCKGKISHFKIPKYIVFVTNYPLTISGKIQKFKLREQMERHLNL | Function: Acyl-CoA synthases catalyze the initial reaction in fatty acid metabolism, by forming a thioester with CoA . Has some preference toward medium-chain substrates . Plays a role in adipocyte differentiation .
Catalytic Activity: a medium chain fatty acid + ATP + CoA = a medium-chain fatty acyl-CoA + AMP + diphosphate
Sequence Mass (Da): 68125
Sequence Length: 615
Subcellular Location: Mitochondrion
EC: 6.2.1.2
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Q58DN7 | MPLPYVGMALRRLAWAVASCRLAPWTRGASGPLHSAPAARSDCSAPVFIRAPAFGDRLALIDQHGRHTYKDLYLRSLRLSREICQLRACADGDLREERVSLLCSNDVSFVVAQWAAWMSGGVAVPLYRKHPRAQLEYFIQDSRSSVVLAGPEHVELLSPVAQKLGVPLLPLPPTVYHGVAEDPEEGLVLERNWRDRGAMIIYTSGTTGRPKGVLSTHDNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAQLVWEKFLSSEAPQINVFMAVPTIYSKLMDYYDKHFTQPHVQDFVRAVCEEKIRLMVSGSAALPLPVLEKWKGITGHTLLERYGMTEIGMALSNPLTAARLPGSVGTPLPGVEVRIVSENPQKDSSPYLIHAEGSEENTKVTPGFEEKEGELLVRGPSVFREYWDKPEETKAAFTSDGWFKTGDTVVFKDGCYWIRGRTSVDIIKSGGYKVSALEVERLLLAHPSITDVAVIGVPDMTWGQRVTAVVTLQEGHSLSHRELKEWARGVLAPYAVPSELLLVEEIPRNQMGKVNKRDLVRQLYPHEKGAPEAGSQ | Function: Catalyzes the initial reaction in intramitochondrial fatty acid synthesis, by activating malonate and methylmalonate, but not acetate, into their respective CoA thioester. May have some preference toward very-long-chain substrates.
Catalytic Activity: ATP + CoA + tetracosanoate = AMP + diphosphate + tetracosanoyl-CoA
Sequence Mass (Da): 64990
Sequence Length: 586
Subcellular Location: Mitochondrion
EC: 6.2.1.76
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Q03342 | LKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNCPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTVEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYELPDGQVITIGNERFRCPEALYQPSFLGMEAVGIHETTFNSIMKCDVDIRKDLYANTVLSGGSTMYPGIADRMQKEITALAPSTMKIKIVAPPDGKYSVWIGGSILASLSTFHEMWISKQEYDESGPSIVHRKCF | Function: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 34765
Sequence Length: 309
Subcellular Location: Cytoplasm
EC: 3.6.4.-
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Q25379 | AEREIVRNIKEKLCYVALDFEQEMQTAASSSSLEKSYELPDGQVITIGNERFRCPEALFQPSFLGMESAGIHETCYNSIMKCDVDIRKFLYANTVLSGGSTMFPGIADRMQKEITAFAPPTMKVKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF | Function: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 19379
Sequence Length: 172
Subcellular Location: Cytoplasm
EC: 3.6.4.-
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P30167 | MAEGEDIQPLVCDNGTGMVKAGFAGDDAPRAVFPRIVGRPRHTGVMVGMGQKDAYVGDEAQSKRGILTLKYPIEHGIVSNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDHLMKILTERGYSFTTTAEREIVRDVKEKLSYIALDFEQELETSKTSSSVEKSYELPDGQVITIGAERFRCPEVLFQPSLIGMEAAGIHETTYNSIMKCDVDIRKDLYGNIVLSGGTTMFPGIADRMSKELTALAPSSMKIKVVAPPERKYSVWIGGSILASLSTFQQMWIAKAEYDESGPSIVHRKCF | Function: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Essential component of cell cytoskeleton; plays an important role in cytoplasmic streaming, cell shape determination, cell division, organelle movement and extension growth.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 41786
Sequence Length: 377
Subcellular Location: Cytoplasm
EC: 3.6.4.-
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P93373 | AGFAGDDAPRAVFPSIVGRPRHTGVMVGMGQKDAYVGDEAQSKRGILTLKYPIEHGIASNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFSVPAMYVAIQAVLSLYASGRTTGTGIVLDSGDGVSHHVPIYEGYALPHAILRLDLAGRDLTDSLMKILTERGYMFTTTAEREIVRDMKEKLAYVALDYEQELETARSSSSIEKNYELPDGQVITIGAERFRCPEVLFQPSMIGMEAAGIHETTYNSIMKRDVDIRKDLYGNIVLSGGSTMFPGIADRMSKEITALAPSSMKIKVVAPPERKYSVWIGGSILASLSTLQQV | Function: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Essential component of cell cytoskeleton; plays an important role in cytoplasmic streaming, cell shape determination, cell division, organelle movement and extension growth.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 37488
Sequence Length: 339
Subcellular Location: Cytoplasm
EC: 3.6.4.-
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P20111 | MNSMNQIETNMQYTYNYEEDEYMTQEEEWDRDLLLDPAWEKQQRKTFTAWCNSHLRKAGTQIENIEEDFRNGLKLMLLLEVISGERLPKPDRGKMRFHKIANVNKALDYIASKGVKLVSIGAEEIVDGNVKMTLGMIWTIILRFAIQDISVEETSAKEGLLLWCQRKTAPYRNVNIQNFHLSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEIAEKHLDIPKMLDAEDIVNTPKPDERAIMTYVSCFYHAFAGAEQAETAANRICKVLAVNQENERLMEEYERLASELLEWIRRTIPWLENRTPEKTMQAMQKKLEDFRDYRRKHKPPKVQEKCQLEINFNTLQTKLRISNRPAFMPSEGKMVSDIAGAWQRLEQAEKGYEEWLLNEIRRLERLEHLAEKFRQKASTHEQWAYGKEQILLQKDYESASLTEVRAMLRKHEAFESDLAAHQDRVEQIAAIAQELNELDYHDAASVNDRCQKICDQWDSLGTLTQKRREALERTEKLLETIDQLHLEFAKRAAPFNNWMEGAMEDLQDMFIVHSIEEIQSLISAHDQFKATLPEADGERQAILSIQNEVEKVIQSYSMRISASNPYSTVTVEEIRTKWEKVKQLVPQRDQSLQEELARQHANERLRRQFAAQANVIGPWIQTKMEEIARSSIEMTGPLEDQMNQLKQYEQNIINYKHNIDKLEGDHQLIQEALVFDNKHTNYTMEHIRVGWELLLTTIARTINEVETQILTRDAKGITQEQMNDFRASFNHFDRRKNGLMDHDDFRACLISMGYDLGEAEFARIMSLVDPNGQGTVTFQSFIDFMTRETADTDTAEQVIASFRILASDKPYILADELRRELPPEQAQYCIKRMPQYTGPGSVPGALDYTSFSSALYGESDL | Function: F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein (By similarity).
PTM: Ubiquitinated by FBXL22, leading to proteasomal degradation.
Sequence Mass (Da): 104275
Sequence Length: 897
Subcellular Location: Cytoplasm
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P35609 | MNQIEPGVQYNYVYDEDEYMIQEEEWDRDLLLDPAWEKQQRKTFTAWCNSHLRKAGTQIENIEEDFRNGLKLMLLLEVISGERLPKPDRGKMRFHKIANVNKALDYIASKGVKLVSIGAEEIVDGNVKMTLGMIWTIILRFAIQDISVEETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEIAEKHLDIPKMLDAEDIVNTPKPDERAIMTYVSCFYHAFAGAEQAETAANRICKVLAVNQENERLMEEYERLASELLEWIRRTIPWLENRTPEKTMQAMQKKLEDFRDYRRKHKPPKVQEKCQLEINFNTLQTKLRISNRPAFMPSEGKMVSDIAGAWQRLEQAEKGYEEWLLNEIRRLERLEHLAEKFRQKASTHETWAYGKEQILLQKDYESASLTEVRALLRKHEAFESDLAAHQDRVEQIAAIAQELNELDYHDAVNVNDRCQKICDQWDRLGTLTQKRREALERMEKLLETIDQLHLEFAKRAAPFNNWMEGAMEDLQDMFIVHSIEEIQSLITAHEQFKATLPEADGERQSIMAIQNEVEKVIQSYNIRISSSNPYSTVTMDELRTKWDKVKQLVPIRDQSLQEELARQHANERLRRQFAAQANAIGPWIQNKMEEIARSSIQITGALEDQMNQLKQYEHNIINYKNNIDKLEGDHQLIQEALVFDNKHTNYTMEHIRVGWELLLTTIARTINEVETQILTRDAKGITQEQMNEFRASFNHFDRRKNGLMDHEDFRACLISMGYDLGEAEFARIMTLVDPNGQGTVTFQSFIDFMTRETADTDTAEQVIASFRILASDKPYILAEELRRELPPDQAQYCIKRMPAYSGPGSVPGALDYAAFSSALYGESDL | Function: F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein.
PTM: Ubiquitinated by FBXL22, leading to proteasomal degradation.
Sequence Mass (Da): 103854
Sequence Length: 894
Subcellular Location: Cytoplasm
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O43707 | MVDYHAANQSYQYGPSSAGNGAGGGGSMGDYMAQEDDWDRDLLLDPAWEKQQRKTFTAWCNSHLRKAGTQIENIDEDFRDGLKLMLLLEVISGERLPKPERGKMRVHKINNVNKALDFIASKGVKLVSIGAEEIVDGNAKMTLGMIWTIILRFAIQDISVEETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAFEVAEKYLDIPKMLDAEDIVNTARPDEKAIMTYVSSFYHAFSGAQKAETAANRICKVLAVNQENEHLMEDYEKLASDLLEWIRRTIPWLEDRVPQKTIQEMQQKLEDFRDYRRVHKPPKVQEKCQLEINFNTLQTKLRLSNRPAFMPSEGKMVSDINNGWQHLEQAEKGYEEWLLNEIRRLERLDHLAEKFRQKASIHEAWTDGKEAMLKHRDYETATLSDIKALIRKHEAFESDLAAHQDRVEQIAAIAQELNELDYYDSHNVNTRCQKICDQWDALGSLTHSRREALEKTEKQLEAIDQLHLEYAKRAAPFNNWMESAMEDLQDMFIVHTIEEIEGLISAHDQFKSTLPDADREREAILAIHKEAQRIAESNHIKLSGSNPYTTVTPQIINSKWEKVQQLVPKRDHALLEEQSKQQSNEHLRRQFASQANVVGPWIQTKMEEIGRISIEMNGTLEDQLSHLKQYERSIVDYKPNLDLLEQQHQLIQEALIFDNKHTNYTMEHIRVGWEQLLTTIARTINEVENQILTRDAKGISQEQMQEFRASFNHFDKDHGGALGPEEFKACLISLGYDVENDRQGEAEFNRIMSLVDPNHSGLVTFQAFIDFMSRETTDTDTADQVIASFKVLAGDKNFITAEELRRELPPDQAEYCIARMAPYQGPDAVPGALDYKSFSTALYGESDL | Function: F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein (Probable). Probably involved in vesicular trafficking via its association with the CART complex. The CART complex is necessary for efficient transferrin receptor recycling but not for EGFR degradation . Involved in tight junction assembly in epithelial cells probably through interaction with MICALL2. Links MICALL2 to the actin cytoskeleton and recruits it to the tight junctions (By similarity). May also function as a transcriptional coactivator, stimulating transcription mediated by the nuclear hormone receptors PPARG and RARA .
Sequence Mass (Da): 104854
Sequence Length: 911
Domain: Contains one Leu-Xaa-Xaa-Leu-Leu (LXXLL) motif that mediates interaction with nuclear receptors.
Subcellular Location: Nucleus
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P00785 | MGLPKSFVSMSLLFFSTLLILSLAFNAKNLTQRTNDEVKAMYESWLIKYGKSYNSLGEWERRFEIFKETLRFIDEHNADTNRSYKVGLNQFADLTDEEFRSTYLGFTSGSNKTKVSNQYEPRVGQVLPSYVDWRSAGAVVDIKSQGECGGCWAFSAIATVEGINKIVTGVLISLSEQELIDCGRTQNTRGCNVGYITDGFQFIINNGGINTEENYPYTAQDGECNVDLQNEKYVTIDTYENVPYNNEWALQTAVTYQPVSVALDAAGDAFKHYSSGIFIGPCGTAIDHAVTIVGYGTEGGIDYWIVKNSWDTTWGEEGYMRILRNVGGAGTCGIATMPSYPVKYNNQNHPKSYSSLINPPAFSMSNDGPVGVDDGQRYSA | Function: Cysteine protease responsible for the cleavage of kiwellin into kissper and KiTH.
Catalytic Activity: Specificity close to that of papain.
Sequence Mass (Da): 42098
Sequence Length: 380
EC: 3.4.22.14
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O62140 | MVHLNKTIQEGDNPDLTAERLTATFDTHAMAAQIYGGEMRARRRREITAKLAEIPELHDSMPLPYMTREEKIMESARKLTVLTQRMSEIIDPTDAGELYHLNNEVLGIEGNPMALHGVMFIPALNAQASDEQQAKWLIRALRREIIGTYAQTEMGHGTNLQNLETTATYDIGTQEFVLHTPKITALKWWPGNLGKSSNYAVVVAHMYIKGKNFGPHTFMVPLRDEKTHKPLPGITIGDIGPKMAYNIVDNGFLGFNNYRIPRTNLLMRHTKVEADGTYIKPPHAKINYSAMVHVRSYMLTGQAIMLSYALNIATRYSAVRRQGQIDKNEPEVKVLEYQTQQHRLFPFIARAYAFQFAGAETVKLYERVLKEMKSGNVSLMADLHALTSGLKSVVTHQTGEGIEQARMACGGHGYSMASYISEIYGVAIGGCTYEGENMVMLLQLARYLVKSAALVKSGKASQLGPLVAYLGARSEPTSLIDRVPNGGITEYIKTFQHIAKRQTLKAANKFFGLMENGEKREIAWNKSSVELNRASRLHTRLFIVEAFARRVNEIGDITIKEALSDLLHLHVNYELLDVATYALEDGFMSSTQLDYVRDQLYFYLQKIRPNAVSLLDSWEFSDRELRSVLGRRDGHVYENLFKWAKESPLNKTDVLPSVDTYLKPMMEKARQSKL | Function: Involved in the first step of peroxisomal beta-oxidation by catalyzing the desaturation of fatty acid-derived side chains . Specifically, catalyzes the desaturation of fatty acids heptanoyl-CoA (C7), nonanoyl-CoA (C9), dodecanoyl-CoA (C12) and to a lesser extent pentanoyl-CoA (C5) and hexadecanoyl-CoA (C16), and hydroxylated fatty acid hydroxynonanoyl-CoA . Also, catalyzes the desaturation fatty acid-derived side chains of ascaroside pheromones, which regulates development and behavior . Specifically, shortens ascaroside with 5-carbon omega side chain (asc-omega-C5), 7-carbon side chain (asc-C7), 9-carbon side chain (asc-C9), 11-carbon side chain (asc-C11), 13-carbon side chain (asc-C13), 15-carbon side chain (asc-C15) and to a lesser extent ascarosides with 7-omega-carbon side chain (asc-omega-C7) . Also shortens indol-3-carbonyl(IC)-ascarosides with 7-carbon side chain (IC-asc-C7) and to a lesser extent (IC)-ascarosides with 9-carbon side chain (IC-asc-C9) . May associate and regulate the folding and/or the catalytic activity of other acyl-coenzyme A oxidases including acox-1.2, acox-1.3, acox-1.4 and acox-3 modulating the type of ascarosides produced . In association with acox-1.3, catalyzes the desaturation of asc-C7-CoA but not of fatty acids or hydroxylated fatty acids . Involved in the biosynthesis of asc-C6-MK (daumone 2) and asc-delta-C9 (daumone 3) but not asc-C7 (daumone 1); daumones are pheromones produced during unfavourable growth conditions which promote entry into the dauer stage .
Catalytic Activity: nonanoyl-CoA + O2 = (2E)-nonenoyl-CoA + H2O2
Sequence Mass (Da): 76074
Sequence Length: 674
Pathway: Lipid metabolism; peroxisomal fatty acid beta-oxidation.
Subcellular Location: Peroxisome
EC: 1.3.3.-
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P34355 | MPLNKLIQDGDNQDLTDERFKATFDTDALAAVFHGGEDALKRIRELRDEVTKRWHLFDALPGAHRTRAERMEDVSRKLKNLMESVGEFADFTNNLDMLVIIRDVMGIEGFPLALHNLMFVPTIQNQADDEQTEWWLMDALQGKIIGTYAQTELGHGTNLGAIETTATYDKLTEEFIIHTPTTTATKWWPGGLGTSCTHVVLVANLIIDTKNYGLHPFFVPIRDRNSYSVMSGVRVGDIGTKMGVNCVDNGFLAFDNYRIPRRNMLMKHSKVSKEGLYTAPSHPKVGYTTMLYMRSEMIYHQAYYLAMAMAISIRYSAVRRQGEIKPGTQEVQILDYQTQQYRIFPGLARCFAFNTAAATVRQMTENCIKQLSHGNSDVLADLHALSCGLKAVVTHQASQSIDQARQACGGHGYSDASYLPTLYTCSVGACTYEGENMVMLLQLSKYLMKAAAKAEKGEEMAPLVAYLVKPDITETNDKFAKMLSHFEHIARHRVMHAYRQMIEEEKQGIERDYAFANHSVDWTKAARAHTKLFIARGFVKSVQEVSDEAVHDVLTTLAELYLSYELIEMSADLTANGYLSESDVQQIRHQIYDSMRKTRRNAVSIVDSFDICDRELRSVLGRRDGHVYENLYKWAQMSPLNERNLPHVEKYLKPMTSKL | Function: Involved in the first step of peroxisomal beta-oxidation by catalyzing the desaturation of fatty acid-derived side chains.
Sequence Mass (Da): 74714
Sequence Length: 659
Pathway: Lipid metabolism; peroxisomal fatty acid beta-oxidation.
Subcellular Location: Peroxisome
EC: 1.3.3.-
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Q20992 | MSAPLIDKYRKMATFDWKKLKAAVEGEEHVRLKSEVVAKMKSEPVFHRDYRVLSREEQREVVHQRWKKIVEWGLFKDPYSDLENFHALTETLEAYDQGTSARLFLHGNVFGAAVKSMGTDRHKDLIQKTENNEIVGAFCLTEVGHGSNTAEIQTTATFDNGELVFNTPSVSAIKCWAGNLAHSATHVVVYAQLHVEGKNEGFHGFVIQVRCPRTFQTLPGITIGDMGSKPGCWQGVENGWMEFKNHRAPLSALLNKGCDITPDGKYVTSFKSASEKQSVSLGTLSVGRLGIIAKGMMACTFASTIAIRYSVARRQFGPVKGAENEIPVLEYPLQQYRLFPYLSAAICIRIFQKKFVGHFTEYMMRVIMGEKSDELSEFSKEVHALSSGAKPVATWLGVESLGEARKACGGHGYLQMSRLNTLRDDNDPSQTFEGENFMILQQTSNILLGKAQSIGSIETPMSTMSFLNQKPSKFSSWSSNPVNDVLSAYRYLTYHLLQTTSAEAYRLKASGKNSFEVRNEIQIHRAVNLSVAYTEHTMIHWVQQFLKEIEDQSVKPVLQKVLNLFSLFLLERHLATLYITGYASGGKFGEDLREKLRLAVAELKPEAIALVDSIAPDDFILHSALGASDGKAYEHIMEEFRKYTNEQPRWVCDLAQFLQKRSQGSKL | Function: Involved in the first step of peroxisomal beta-oxidation by catalyzing the desaturation of fatty acid-derived side chains of ascaroside pheromones, which regulates development and behavior . Specifically, shortens indol-3-carbonyl(IC)-ascarosides with 7-carbon (IC-asc-C7) or 9-carbon (IC-asc-C9) side chains and contributes to the shortening of ascarosides with 13-carbon (asc-C13) and 15-carbon (asc-C15) side chains .
Catalytic Activity: IC-asc-C7-CoA + O2 = H2O2 + IC-asc-DeltaC7-CoA
Sequence Mass (Da): 74887
Sequence Length: 667
Pathway: Lipid metabolism; peroxisomal fatty acid beta-oxidation.
Subcellular Location: Peroxisome
EC: 1.3.3.-
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Q8RM04 | MNVPVGHLRNVQVLGIDAGGTMTDTFFVDQDGDFVVGKAQSTPQNEALGLIASSEDGLANWGMSLHEALAQLQTGVYSGTAMLNRVVQRKGLKCGLIVNRGMEDFHRMGRAVQSHLGYAYEDRIHLNTHRYDPPLVPRHLTRGVVERTDMIGTQVIPLREDTARDAARDLIAADAEGIVISLLHSYKNPENERRVRDIVLEEVEKSGKKIPVFASADYYPVRKETHRTNTTILEGYAAEPSRQTLSKISNAFKERGTKFDFRVMATHGGTISWKAKELARTIVSGPIGGVIGAKYLGEVLGYKNIACSDIGGTSFDVALITQGEMTIKNDPDMARLVLSLPLVAMDSVGAGAGSFIRLDPYTRAIKLGPDSAGYRVGVCWKESGIETVTISDCHMVLGYLNPDNFLGGAVKLDRQRSVDAIKAQIADPLGLSVEDAAAGVIELLDSDLRDYLRSMISGKGYSPASFVCFSYGGAGPVHTYGYTEGLGFEDVIVPAWAAGFSAFGCAAADFEYRYDKSLDINMPTETPDTDKEKAAATLQAAWEELTKNVLEEFKLNGYSADQVTLQPGYRMQYRGQLNDLEIESPLAQAHTAADWDQLTDAFNATYGRVYAASARSPELGYSVTGAIMRGMVPIPKPKIPKEPEEGETPPESAKIGTRKFYRKKRWVDAQLYHMESLRPGNRVMGPAVIESDATTFVVPDGFETWLDGHRLFHLREV | Cofactor: Zn(2+). The heterohexamer contains tightly bound iron, manganese and zinc ions.
Function: Catalyzes the carboxylation of acetone to form acetoacetate. Has a reduced activity on butanone, and no activity on 2-pentatone, 3-pentatone, 2-hexanone, chloroacetone, pyruvate, phosphoenolpyruvate, acetaldehyde, propionaldehyde and propylene oxide.
PTM: The N-terminus is blocked.
Catalytic Activity: acetone + 2 ATP + 3 H2O + hydrogencarbonate = acetoacetate + 2 AMP + 4 H(+) + 4 phosphate
Sequence Mass (Da): 78509
Sequence Length: 717
EC: 6.4.1.6
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Q8RM03 | MNVTVDQSTLAGATRGIVRGGETLKEHRDRLMAATKATGRYAGLKTLELREREPILYNKLFSRLRAGVVDARETAKKIAASPIVEQEGELCFTLYNAAGDSLLTSTGIIIHVGTMGAAIKYMIENNWEANPGVHDKDIFCNNDSLIGNVHPCDIHTIVPIFWEGELIGWVGGVTHVIDTGAVGPGSMATGQVQRFGDGYSITCRKVGANDTLFRDWLHESQRMVRTTRYWMLDERTRIAGCHMIRKLVEEVVAEEGIEAYWKFAYEAVEHGRLGLQARIKAMTIPGTYRQVGFVDVPYAHEDVRVPSDFAKLDTIMHAPCEMTIRRDGTWRLDFEGSSRWGWHTYNAHQVSFTSGIWVMMTQTLIPSEMINDGAAYGTEFRLPKGTWMNPDDRRVAFSYSWHFLVSAWTALWRGLSRSYFGRGYLEEVNAGNANTSNWLQGGGFNQYDEIHAVNSFECAANGTGATAVQDGLSHAAAIWNPEGDMGDMEIWELAEPLVYLGRQIKASSGGSGKYRGGCGFESLRMVWNAKDWTMFFMGNGHISSDWGLMGGYPAASGYRFAAHKTNLKELIASGAEIPLGGDTDPENPTWDAMLPDAQIKRDKQAITTEEMFSDYDLYLNYMRGGPGFGDPLDREPQAVADDINGGYVLERFAGEVYGVVVRKGADGQYGVDEAGTAAARAQIRKDRLAKSVPVSEWMKGEREKILAKDAGTQVRQMFAASFKLGPRFEKDFRTFWSLPDSWTLPEEEIGVPTYGSRYSMDISELPDVHTVQFVEE | Cofactor: Zn(2+). The heterohexamer contains tightly bound iron, manganese and zinc ions.
Function: Catalyzes the carboxylation of acetone to form acetoacetate. Has a reduced activity on butanone, and no activity on 2-pentatone, 3-pentatone, 2-hexanone, chloroacetone, pyruvate, phosphoenolpyruvate, acetaldehyde, propionaldehyde and propylene oxide.
PTM: The N-terminus is blocked.
Catalytic Activity: acetone + 2 ATP + 3 H2O + hydrogencarbonate = acetoacetate + 2 AMP + 4 H(+) + 4 phosphate
Sequence Mass (Da): 86342
Sequence Length: 776
EC: 6.4.1.6
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Q8RM02 | MAYTRSKIVDLVDGKIDPDTLHQMLSTPKDPERFVTYVEILQERMPWDDKIILPLGPKLFIVQQKVSKKWTVRCECGHDFCDWKDNWKLSARVHVRDTPQKMEEIYPRLMAPTPSWQVIREYFCPECGTLHDVEAPTPWYPVIHDFSPDIEGFYQEWLGLPVPERADA | Cofactor: Zn(2+). The heterohexamer contains tightly bound iron, manganese and zinc ions.
Function: Catalyzes the carboxylation of acetone to form acetoacetate. Has a reduced activity on butanone, and no activity on 2-pentatone, 3-pentatone, 2-hexanone, chloroacetone, pyruvate, phosphoenolpyruvate, acetaldehyde, propionaldehyde and propylene oxide.
Catalytic Activity: acetone + 2 ATP + 3 H2O + hydrogencarbonate = acetoacetate + 2 AMP + 4 H(+) + 4 phosphate
Sequence Mass (Da): 19774
Sequence Length: 168
EC: 6.4.1.6
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Q6PTT0 | MTSKGPEEEHPSVTLFRQYLRIRTVQPKPDYGAAVAFFEETARQLGLGCQKVEVAPGYVVTVLTWPGTNPTLSSILLNSHTDVVPVFKEHWSHDPFEAFKDSEGYIYTRGAQDMKCVSIQYLEAVKRLKVEGHRFPRTIHMTFVPDEEVGGHQGMELFVQRHEFHALRAGFALDEGLANPTDAFTVFYSERSPWWVRVTSTGRPGHASRFMEDTAAEKLHKVVNSILAFREKEWQRLQSNPHLKEGSVTSVNLTKLEGGVAYNVVPATMSACFDFRVAPDVDMKAFEEQLQSWCQEAGEGVTFEFAQKFTEPRMTPTDDTDPWWAAFSGACKEMTLTLEPEIFPAATDSRYIRAVGIPALGFSPMNRTPVLLHDHNERLHEAVFLRGVDIYTRLVAALASVPALPGES | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Involved in the hydrolysis of N-acylated or N-acetylated amino acids (except L-aspartate).
Catalytic Activity: an N-acyl-L-amino acid + H2O = a carboxylate + an L-alpha-amino acid
Sequence Mass (Da): 45823
Sequence Length: 408
Subcellular Location: Cytoplasm
EC: 3.5.1.14
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Q55DP8 | MNSIQENEHVTVFREFLKIRTDHPTPDYESSTKFLVEKAKEYNIPYEVYRETGTPIVLMKIEGLEPNLKTVLLNSHVDVVPAVHDSWKVDPFSAWKDESGNIFGRGTQDMKCVCMQFLEVARRIVQSGQKLKRTLHLSFVPDEEIGGSGKGMEKFVYTEKFRQLNIGLCLDEGLASPTNDFTVFYGERAPWWVHITAVGNAGHGSRFIEGTAIEKLMRTINKMLAFRQEQFESLHHGQHECGKKLGDVTSLNLTVLKAGIPIDHSNNFSYNVIPTQAEAGFDIRIPPTVNLDQFLDQIKEWTAEEGLSFKFASYIPKNEMTKLDSDNKWWENFKESCKKMDINLVTEIFPAATDSRFIRNLGIPAFGFSPINNTPILLHDHNEFLNEKVYLRGIDIFMGIIPNLVNME | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Involved in the hydrolysis of N-acylated or N-acetylated amino acids (except L-aspartate).
Catalytic Activity: an N-acyl-L-amino acid + H2O = a carboxylate + an L-alpha-amino acid
Sequence Mass (Da): 46568
Sequence Length: 408
Subcellular Location: Cytoplasm
EC: 3.5.1.14
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Q03154 | MTSKGPEEEHPSVTLFRQYLRIRTVQPKPDYGAAVAFFEETARQLGLGCQKVEVAPGYVVTVLTWPGTNPTLSSILLNSHTDVVPVFKEHWSHDPFEAFKDSEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFVPDEEVGGHQGMELFVQRPEFHALRAGFALDEGIANPTDAFTVFYSERSPWWVRVTSTGRPGHASRFMEDTAAEKLHKVVNSILAFREKEWQRLQSNPHLKEGSVTSVNLTKLEGGVAYNVIPATMSASFDFRVAPDVDFKAFEEQLQSWCQAAGEGVTLEFAQKWMHPQVTPTDDSNPWWAAFSRVCKDMNLTLEPEIMPAATDNRYIRAVGVPALGFSPMNRTPVLLHDHDERLHEAVFLRGVDIYTRLLPALASVPALPSDS | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Catalyzes the hydrolysis of N-acetylated amino acids to acetate and free amino acids.
Catalytic Activity: an N-acyl-L-amino acid + H2O = a carboxylate + an L-alpha-amino acid
Sequence Mass (Da): 45885
Sequence Length: 408
Subcellular Location: Cytoplasm
EC: 3.5.1.14
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A8KB34 | MSSRTNISCLQEAKRVAIFGGTHGNEMSGIVLANMWIQNATEIERKGLVCKPFITNPRAVEKCTRYIDTDLNRAFTPENLSASELEALPYEVQRAKEINQMFGPKGGSDAYDVIFDLHNTTSNMGSTLILESSTDLFNLQMVHYIKKAMAPHTCSVLLNEHPQLKYSTTRSVAKHPVGLEVGPQPQGVLRSNVFESMRTILKHALDFIELFNNGVEFPPCTVNVFRVQERMDYPRDTNGNITAMVHPHLQDCDWEPLNRGDPMFLTFDGRTILYEGANTVYPTFINEAAYYEKQQAFVTTCREILAANAIRKAFK | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the deacetylation of N-acetylaspartic acid (NAA) to produce acetate and L-aspartate.
Catalytic Activity: H2O + N-acyl-L-aspartate = a carboxylate + L-aspartate
Sequence Mass (Da): 35535
Sequence Length: 315
Subcellular Location: Cytoplasm
EC: 3.5.1.15
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