ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q5FVE4 | MTGTPKTQEGAKDLEVDMNKTEVTPRLWTTCRDGEVLLRLSKHGPGHETPMTIPEFFRESVNRFGTYPALASKNGKKWEILNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILLVENDQQLQKILSIPQSSLEPLKAIIQYRLPMKKNNNLYSWDDFMELGRSIPDTQLEQVIESQKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKHETVVSYLPLSHIAAQMMDIWVPIKIGALTYFAQADALKGTLVSTLKEVKPTVFIGV... | 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... |
O34847 | MAPRLEFEKPVIELQTKIAELKKFTQDSDMDLSAEIERLEDRLAKLQDDIYKNLKPWDRVQIARLADRPTTLDYIEHLFTDFFECHGDRAYGDDEAIVGGIAKFHGLPVTVIGHQRGKDTKENLVRNFGMPHPEGYRKALRLMKQADKFNRPIICFIDTKGAYPGRAAEERGQSEAIAKNLFEMAGLRVPVICIVIGEGGSGGALGLGVGNHLHMLENSTYSVISPEGAAALLWKDSSLAKKAAETMKITAPDLKELGIIDHMIKEVKGGAHHDVKLQASYMDETLKQSLKTLLKLSEEELVQQRYEKYKAIGKVSVEDQ... | 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)-carboxybiotiny... |
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)-carboxybiotiny... |
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 Activit... |
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 Activit... |
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 Activit... |
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 Activit... |
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 Activit... |
P18823 | MINEDPSSLTDMDNNIDSWKNNSENSSYSHADSLADVSNIDNLLSDKIFSIRDSNSNIYDIYYAYDTNDTNITKYKWTNNINRCIESYLRSQICEDIDFNSDICDKVQRTIIILIRSTNDTNDISDTNDISDTNDTNDTNAIYDPFDISDTNDTNEIYDPFFILDINDTNDTNDIYGIYDPDDIYETNIKDICERYSEIYPRNREKSTFVPIDYSDPNCMEKLARLWVQCETCYGLNFKQFFRPKMNICEHCGEHLKMSSSDRIDLLIDRDTWNPMDEDMVSVDPIKFDSIKELGSEEESSKDRLDEDMLSPDPIELDSE... | 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 Activit... |
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 Activit... |
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 Activit... |
P52769 | MSIKEWFEDKRKITALLKNSVERDSKDANETEKNKNKSIDYAKIKKLWAQCDNCENLLYLRFLRENQSVCKECGYYLQMNSSDRIELLIDRDTWRPMDEDMYTLDVLQFYSENEPSHSDNLNSEDESYKDHITFYQIETGLTDAIQTGIGQLNGLTIALGVMDFQFMGGSMGSVVGEKITRLIERATAESLPLIMVCASGGARMQEGSFSLMQMAKIASALYIHQKEKKLLYISILTSPTTGGVTASFGMLGDIIIAEPKAYIAFAGKRVIEQTLGQKVIEDFQVTEHLFGHGLFDLIVPRNLLKGVLSELFWFYVLRSS... | 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 Activit... |
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 maxi... |
Q06588 | MESFPIINLEKLNGEERAITMEKIKDACENWGFFECVNHGISLELLDKVEKMTKEHYKKCMEERFKESIKNRGLDSLRSEVNDVDWESTFYLKHLPVSNISDVPDLDDDYRTLMKDFAGKIEKLSEELLDLLCENLGLEKGYLKKVFYGSKRPTFGTKVSNYPPCPNPDLVKGLRAHTDAGGIILLFQDDKVSGLQLLKDGEWVDVPPVKHSIVVNLGDQLEVITNGKYKSVEHRVLSQTDGEGRMSIASFYNPGSDSVIFPAPELIGKEAEKEKKENYPRFVFEDYMKLYSAVKFQAKEPRFEAMKAMETTVANNVGPL... | 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 + et... |
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 ... |
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: 1.1... |
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 arom... |
Q54RR5 | MIKKLILDPKNVSIIKNGIRNYSKSKSFIQPITTLSEEETLLKETVANFANEKVRPLVKVMDETSELNKGLLKDLFDMNLMGIDISDSYGGANMNFMGSIIAIEELAKVDPAISVIVDVQNTLVNNCINRYGSIQQREKYLSMLATNTVGSFCLSESGSGSDAFALATRAVRQSDGTFVLNGTKQWITNAKEAGVFIVMANVDPSQGYKGITAFIVESNNPGLRIGKKEDKLGIRASSTCEVILDNCVVKPTDILGELGRGYKIAIEGLNEGRIGIAAQMLGLAQGVFDSTIPYLMERKQFGKPIATFQGMQFTYADLAV... | 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-m... |
P45954 | MEGLAVRLLRGSRLLRRNFLTCLSSWKIPPHVSKSSQSEALLNITNNGIHFAPLQTFTDEEMMIKSSVKKFAQEQIAPLVSTMDENSKMEKSVIQGLFQQGLMGIEVDPEYGGTGASFLSTVLVIEELAKVDASVAVFCEIQNTLINTLIRKHGTEEQKATYLPQLTTEKVGSFCLSEAGAGSDSFALKTRADKEGDYYVLNGSKMWISSAEHAGLFLVMANVDPTIGYKGITSFLVDRDTPGLHIGKPENKLGLRASSTCPLTFENVKVPEANILGQIGHGYKYAIGSLNEGRIGIAAQMLGLAQGCFDYTIPYIKERI... | 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-... |
P70584 | MAVSAFQLWRAGGLLRRNFLTHSSSWKIPPRVLKSSQPEALLSVTNNALCFAPLQTFTDEDIMMQKAVKKFAQEQIAPLVSTMDENSKMEKSVIQGLFQQGMMGIEVEAKYGGTEASFLCSVLVIEELAKVDASVALLCDIQNTVINKLFRKHGTEEQKATYLPKLVTEKLGSFCLSEAGAGSDSFALKTRADKSGNYYVINGSKMWISNAEHAELFLVFANVDPPSGYRGITCFLVDRDTEGFQIGRRENKMGIRASSTCQLTFENVKVPETSVLGKIGHGYKYAIGSLNEGRIGIAAQMLGLAQGCFDYTIPYIKERM... | 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-... |
P52042 | MDFNLTREQELVRQMVREFAENEVKPIAAEIDETERFPMENVKKMGQYGMMGIPFSKEYGGAGGDVLSYIIAVEELSKVCGTTGVILSAHTSLCASLINEHGTEEQKQKYLVPLAKGEKIGAYGLTEPNAGTDSGAQQTVAVLEGDHYVINGSKIFITNGGVADTFVIFAMTDRTKGTKGISAFIIEKGFKGFSIGKVEQKLGIRASSTTELVFEDMIVPVENMIGKEGKGFPIAMKTLDGGRIGIAAQALGIAEGAFNEARAYMKERKQFGRSLDKFQGLAWMMADMDVAIESARYLVYKAAYLKQAGLPYTVDAARAK... | 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
|
Q06319 | MDFNLTDIQQDFLKLAHDFGEKKLAPTVTERDHKGIYDKELIDELLSLGITGAYFEEKYGGSGDDGGDVLSYILAVEELAKYDAGVAITLSATVSLCANPIWQFGTEAQKEKFLVPLVEGTKLGAFGLTEPNAGTDASGQQTIATKNDDGTYTLNGSKIFITNGGAADIYIVFAMTDKSKGNHGITAFILEDGTPGFTYGKKEDKMGIHTSQTMELVFQDVKVPAENMLGEEGKGFKIAMMTLDGGRIGVAAQALGIAEAALADAVEYSKQRVQFGKPLCKFQSISFKLADMKMQIEAARNLVYKAACKKQEGKPFTVDA... | 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
|
C3UVB0 | MDFNLSKELQMLQKEVRNFVNKKIVPFADQWDNENHFPYEEAVRPMGELGFFGTVIPEEYGGEGMDQGWLAAMIVTEEIARGSSALRVQLNMEVLGCAYTILTYGSEALKKKYVPKLSSAEFLGGFGITEPDAGSDVMAMSSTAEDKGDHWLLNGSKTWISNAAQADVLIYYAYTDKAAGSRGLSAFVIEPRNFPGIKTSNLEKLGSHASPTGELFLDNVKVPKENILGKPGDGARIVFGSLNHTRLSAAAGGVGLAQACLDAAIKYCNERRQFGKPIGDFQMNQDMIAQMAVEVEAARLLAYKAAAAKDEGRLNNGLDV... | 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
|
Q58010 | MWGRDYELKYISYPKSVAIIGASKTEGKVGYAIMKNLKDFNGKIYPINPKYDEIFGIKCYKSVLDVEDDIDLAVIVVPNIVVPKVLEECGKKGVKGAVIITAGFSEVGNYELENKIKEIAKRYNIRIIGPNCLGIMNTHINLNATFAKVFPPKGGVSIISQSGAVLNAILDIAPLLNIGFSKVVSIGNKADIQESDLLEYFLDDEDTKIVVLYIEGLKDKRFLKVAKKLSKKKPIIALKSGRTEVGKKAAKSHTGSLAGEDVIYEAAFKEAGIIRAYTFEELVDLIHLFSTQPTISSNEIGIITNAGGFGVLAADSCVDY... | 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
|
Q10714 | MRLFLLALLATLAVTQALVKEEIQAKEYLENLNKELAKRTNVETEAAWAYGSNITDENEKKKNEISAELAKFMKEVASDTTKFQWRSYQSEDLKRQFKALTKLGYAALPEDDYAELLDTLSAMESNFAKVKVCDYKDSTKCDLALDPEIEEVISKSRDHEELAYYWREFYDKAGTAVRSQFERYVELNTKAAKLNNFTSGAEAWLDEYEDDTFEQQLEDIFADIRPLYQQIHGYVRFRLRKHYGDAVVSETGPIPMHLLGNMWAQQWSEIADIVSPFPEKPLVDVSAEMEKQGYTPLKMFQMGDDFFTSMNLTKLPQDFW... | 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, oli... |
Q6Q4G4 | MNLINFSYLNLLFGAGLFSVLESATILNTESDAKKWLTTYNDEAGKYIYDATEAEWNYNTNLTDHNLGISIKKSNDLATFTEQKAIEANKKFVWKNFTDPLLKREFSKITDIGTASLSDEDFQKMSGLNSDLTKIYSTAKVCNKPNDPSGKCYPLDPDLSDIISKSNDLEELTWAWKGWRDASGKHMPDKYDEFVQLLNKAANINGYEDNGDYWRSWYESPTFRKDCEDLWQEIKPFYEQLHAYVRRKLQKKYPQIAFPKEGHIPAHLLGNMWAQSWENIEYLLRPAPDLPSMDITEELVKQNYTALKLFQLSDTFFKSL... | 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):... |
P58382 | MEALLVINAGSSSLKFQIFGIATAGLERQVRAKLDGIATQPRLKATAADGTELINRRLDATAVPDLPEALSVARDWLATLRGFDLRAIGHRVVHGGPDYVRPVLIETTVLDRLASYQDLAPLHQPNNLAPIRLAMDIKPDVPQVACFDTAFHRGRTEHTDCYALPRTFYEQGVRRYGFHGISYEYIAGRLREVAPEVARGRVIVAHLGSGASMCALKDGRSVETTMGFTALDGLPMGTRPGQLDPGVVLHLLTDQGMSAQAVSDLLYHRSGLKGLSGISNDMRELLGSDDPRASFAIDHFVHRCALDAGMLAAALGGLDA... | 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... |
Q9X449 | MDALLVVNAGSSSLKFQVFGIVGMDLTRQIRGKVDGIGTRPRLQATAADGTQLIDQTYDAKAVRDLPAAITEARRWLLTLEGFELQAVGHRVVHGGPDYTRPVLIDATVLDHLAGYQDLAPLHQPNNLAPIRLAMEINPDVPQVACFDTAFHRGHAKHTDCYALPRSFYDEGVRRYGFHGLSYEYIAERLREVASRAAKGRVVVAHLGSGASMCGLRDGRSIESTMLHRPSTGCRWDTPGQLDPGVVLYLILQKGMKAQAVSDLLYHDAGLKGLSGLSNDMRDLLASDDPHAALSVAHFVYRCVLNGGMLAAALGGIDAF... | 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... |
Q6N143 | MSDVLLVLNAGSSSIKFALYEAHTEPTADHLICEGGIGSLGHRPHFKVVNSDGSTRYDTYLPEGTSHDDAMAVLIGWIETTFPEHRLSAVGHRVVHGGALFDGPVDVTPEVIAQLRAFDRLAPLHQPHNVSAIEALAKLHPSLPQIACFDTAFHHRLPEVATAFALPRELTEQGVRRYGFHGLSYEYIAGRLPDVAGQAVADGRVVVAHLGAGASMCAMLRCRSIATTMGFTALDGLMMGSRCGELDPGVVLYLLEEKSMTAREIEDLLYRESGLLGVSGISDDMRTLLASDDPHACEAIELFVYRIARELGSLAAALGG... | 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... |
Q54YA0 | MTNSNFNHGNHGSNLPARLFTKQSQALIYNYKEAAVQRMLDFDNVSQRDTPSVGGLIHPGSDGGMYKAFFGFKELVIPVYNSVSEACQQCPNADVFLNFASHRSAYQSSLLALREPSIQTVVIIAEGVPENEARSLISIAKKLGKVIIGPATVGGIQAGCFKIGNTAGTIVYIMACKLYRSGSVGFVSKSGGLSNEMYNVLSRCTDGIYEGIAIGGDAFPGSTLTDHALRYEKLPEVQMIVILGELGGWDEYGIVEALKKGEITKPICAWVSGTVAKIFPTEVQFGHAGAKSGGETESADAKNKALREAGAVVPTSFEDF... | 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 | MPNYTVPPDPADTSWDSPYSIPVQIVVWIIIIVLSLETIIGNAMVVMAYRIERNISKQVSNRYIVSLAISDLIIGIEGFPFFTVYVLNGDRWPLGWVACQTWLFLDYTLCLVSILTVLLITADRYLSVCHTAKYLKWQSPTKTQLLIVMSWLLPAIIFGIMIYGWQAMTGQSTSMSGAECSAPFLSNPYVNMGMYVAYYWTTLVAMLILYKGIHQAAKNLEKKAKAKERRHIALILSQRLGTQVGVSLMLQSKAEKEKAEEAQKDSGYTSNQAGDANNLRRFGFSEPETSQFRVDPNSNNNLNVEGSLNTENDQNLGVIE... | 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
... |
P16395 | MEPVMSLALAAHGPPSILEPLFKTVTTSTTTTTTTTTSTTTTTASPAGYSPGYPGTTLLTALFENLTSTAASGLYDPYSGMYGNQTNGTIGFETKGPRYSLASMVVMGFVAAILSTVTVAGNVMVMISFKIDKQLQTISNYFLFSLAIADFAIGAISMPLFAVTTILGYWPLGPIVCDTWLALDYLASNASVLNLLIISFDRYFSVTRPLTYRAKRTTNRAAVMIGAAWGISLLLWPPWIYSWPYIEGKRTVPKDECYIQFIETNQYITFGTALAAFYFPVTIMCFLYWRIWRETKKRQKDLPNLQAGKKDSSKRSNSSD... | 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 ... |
P11229 | MNTSAPPAVSPNITVLAPGKGPWQVAFIGITTGLLSLATVTGNLLVLISFKVNTELKTVNNYFLLSLACADLIIGTFSMNLYTTYLLMGHWALGTLACDLWLALDYVASNASVMNLLLISFDRYFSVTRPLSYRAKRTPRRAALMIGLAWLVSFVLWAPAILFWQYLVGERTVLAGQCYIQFLSQPIITFGTAMAAFYLPVTVMCTLYWRIYRETENRARELAALQGSETPGKGGGSSSSSERSQPGAEGSPETPPGRCCRCCRAPRLLQAYSWKEEEEEDEGSMESLTSSEGEEPGSEVVIKMPMVDPEAQAPTKQPPR... | 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
... |
Q09388 | MAVASVLLALFMLFLSIVTVIGNLAVLLSYYLDKNIRQPTNYFIFSLAISDLLIGLEGIPVYTAFYLNNNEWIWGDVLCDLWLSIDYIVCLASIYTVLGITVDRYYSVKKPATYRNWRTPGRVVLIIIFIWLVPSILFSVSIFGYGTFTGTGRILKETECYVQFMTNPYLNMGMYISYYWTTLFVMLYLYWGIYRAAKKLALKSDQKTKRLALLTEMRRPEVSVRTSDAGNSSSDSPNDTSNSSKCFRTAPPTTTVQTTQTNVGTPPPVFRNHMTLHNNNMDFTKDNEIVRPPTPPDDNTYSNPNFSMISEQLTNGFSRQ... | 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 vent... |
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; bac... |
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 ele... |
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 ele... |
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 ele... |
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 ... |
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... |
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 Mas... |
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 Mas... |
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 Mas... |
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 Mas... |
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 Mas... |
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 Mas... |
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 Mas... |
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 Mas... |
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 Mas... |
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 Mas... |
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 Mas... |
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 Mas... |
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 Mas... |
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 Mas... |
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 Mas... |
Q8YJ48 | MSEKLYPVLPEAKKNTLIDNETYLEWYEESVSDPDGFWAKHGRRIDWFKPFTKVKNTDFNGDVTIKWYEDGVTNVSYNCIDRHLKSRGDKVAIIWEGDNPYIDKKITYRELYENVCRMANVLKKHGVKKGDRVTIYLPMIPEAAYAMLACARIGAVHSVVFAGFSPEALAGRIVDCESTFVITADEGVRGGKPVALKENTDTAIDIAAKQYVMVNKVLVVRRTGGKVSWGRGRDLWYHQEVASVEPHCEPEPMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYASMTHQYVFDYHDGEIYWCTADVGWVTGHSYIVYGP... | 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, ... |
Q9PMD2 | MLNQNNQELFKPSKEFSRNARIKNLCEYYDLCDEAKEDFEGFWKRQAFEKIEWFSPFSRVLNEDKAPFYKWFEGGTLNVSYQCLDRHMKTRRNKAALIFEGEMGDYEVYTYRRLLHETCKAANLLKKFGVKKGDRVVIYMPMIPETAIVMLACARIGAIHSVVFGGFSPEALRDRIIDAGAKLVVTADGAFRRGKPYMLKPAVDKALSEGCESVEKVLIVIRNNEPIEYIKGRDYVYNELVKNESYKCEPEIMDSEDLLFLLYTSGSTGKPKGVMHASAGYILWAQMTMEWVFDIKDYDNYWCSADVGWITGHTYVVYGP... | 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, ... |
Q554Z5 | MFSNGLSKLIKSKIASTSIITTKNNYSISKLSFSSTSILLNKKYKLSEPFNYEQDCEYALKEPIQFWDEVASKYVHWNKRYEKVYSGDEYNPEWFKGGVLNACYNALDVHAKDPITKNRIAIIHETPSKNNTNKLTYGELWDEVCIFARGLHNLGVEKGDRVVIYMPMINQALIAMLACARLGATHSVVFGGFASPQLAQRIEHFKPKVVISANFGVEGHKINCYTPLLSKALELSSHKPNHTIVYNRLDVKLDAGEVLPPRVEGSLDWSELIKNIAPYRDYALVDSTHPLYILYTSGTTGMPKGVVRDTGGYSVALNYS... | 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 Activi... |
Q17QJ1 | MAVYVGMLRVARLCARSPRVLGARVGLSRVWQEARLWGVRPLSSGELDHTVPLPVGGFSYVQGHVGLHLSNKTVGRCLDATAQRVPDQEALVVHHENIRLTFAQLKEEVDKAASGLLSIGLRKGDRLGMWGPNSYAWVLMQLATAQAGIILVSVNPAYQAMELEYALKKVGCKALVFPKQFKTQQYYNILKQICPEVEKAQPGALKSQRLPDLTTVISVDAHLPGTLLLDEVVAAGSQEQNLTRLRHTQQFLSCHDPINIQFTSGTTGSPKGATLSHYNIVNNANMIGQRLRLHQKTPEESRVVLPSPLYHCLGSVGGTM... | 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 + diphospha... |
Q0P4F7 | MSSKILLTNLRTSASFCKTLKFPQRPRTPFIASQQSCAIHVDNPPSIPTLTTSYVHGLSSHPLQSSTVDQCLQATVERYPDREAMVFVQDGIRKTFAEFYQDVEKAAAGLLAAGLKRGDRLGMWGPNIYEWVLMQFATAKAGIILVAVNPAYQLQEVEFALRKVQCNAVVCPTKFKSQHYCDMLKQLCPEMETASPGGIKSSRLPDLHTVIVTDSQQPGSFLLKDLMQAGSSQHYQQLQDLQKKLVCDDPINIQFTSGTTGKPKGATLSHHNIVNNAYFTGMRIGYNWRKNVRICLPVPLYHCFGSVGGGVIMALYGTTV... | 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 + diphospha... |
Q96CM8 | MAVYVGMLRLGRLCAGSSGVLGARAALSRSWQEARLQGVRFLSSREVDRMVSTPIGGLSYVQGCTKKHLNSKTVGQCLETTAQRVPEREALVVLHEDVRLTFAQLKEEVDKAASGLLSIGLCKGDRLGMWGPNSYAWVLMQLATAQAGIILVSVNPAYQAMELEYVLKKVGCKALVFPKQFKTQQYYNVLKQICPEVENAQPGALKSQRLPDLTTVISVDAPLPGTLLLDEVVAAGSTRQHLDQLQYNQQFLSCHDPINIQFTSGTTGSPKGATLSHYNIVNNSNILGERLKLHEKTPEQLRMILPNPLYHCLGSVAGTM... | 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 + diphos... |
Q58DN7 | MPLPYVGMALRRLAWAVASCRLAPWTRGASGPLHSAPAARSDCSAPVFIRAPAFGDRLALIDQHGRHTYKDLYLRSLRLSREICQLRACADGDLREERVSLLCSNDVSFVVAQWAAWMSGGVAVPLYRKHPRAQLEYFIQDSRSSVVLAGPEHVELLSPVAQKLGVPLLPLPPTVYHGVAEDPEEGLVLERNWRDRGAMIIYTSGTTGRPKGVLSTHDNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSAQLVWEKFLSSEAPQINVFMAVPTIYSKLMDYYDKHFTQPHVQDFVRA... | 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 + tetracosa... |
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.-
|
P30167 | MAEGEDIQPLVCDNGTGMVKAGFAGDDAPRAVFPRIVGRPRHTGVMVGMGQKDAYVGDEAQSKRGILTLKYPIEHGIVSNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDHLMKILTERGYSFTTTAEREIVRDVKEKLSYIALDFEQELETSKTSSSVEKSYELPDGQVITIGAERFRCPEVLFQPSLIGMEAAGIHETTYNSIMKCDVDIRKDLYGNIVLSGGTTMFPGIADRMSKELT... | 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... |
P93373 | AGFAGDDAPRAVFPSIVGRPRHTGVMVGMGQKDAYVGDEAQSKRGILTLKYPIEHGIASNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFSVPAMYVAIQAVLSLYASGRTTGTGIVLDSGDGVSHHVPIYEGYALPHAILRLDLAGRDLTDSLMKILTERGYMFTTTAEREIVRDMKEKLAYVALDYEQELETARSSSSIEKNYELPDGQVITIGAERFRCPEVLFQPSMIGMEAAGIHETTYNSIMKRDVDIRKDLYGNIVLSGGSTMFPGIADRMSKEITALAPSSMKIKVVAPPERK... | 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... |
P20111 | MNSMNQIETNMQYTYNYEEDEYMTQEEEWDRDLLLDPAWEKQQRKTFTAWCNSHLRKAGTQIENIEEDFRNGLKLMLLLEVISGERLPKPDRGKMRFHKIANVNKALDYIASKGVKLVSIGAEEIVDGNVKMTLGMIWTIILRFAIQDISVEETSAKEGLLLWCQRKTAPYRNVNIQNFHLSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEIAEKHLDIPKMLDAEDIVNTPKPDERAIMTYVSCFYHAFAGAEQAETAANRICKVLAVNQENERLMEEYERLASELLEWIRRTIPWLENRTPEKTMQAMQ... | 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
|
P35609 | MNQIEPGVQYNYVYDEDEYMIQEEEWDRDLLLDPAWEKQQRKTFTAWCNSHLRKAGTQIENIEEDFRNGLKLMLLLEVISGERLPKPDRGKMRFHKIANVNKALDYIASKGVKLVSIGAEEIVDGNVKMTLGMIWTIILRFAIQDISVEETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEIAEKHLDIPKMLDAEDIVNTPKPDERAIMTYVSCFYHAFAGAEQAETAANRICKVLAVNQENERLMEEYERLASELLEWIRRTIPWLENRTPEKTMQAMQKKL... | 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
|
O43707 | MVDYHAANQSYQYGPSSAGNGAGGGGSMGDYMAQEDDWDRDLLLDPAWEKQQRKTFTAWCNSHLRKAGTQIENIDEDFRDGLKLMLLLEVISGERLPKPERGKMRVHKINNVNKALDFIASKGVKLVSIGAEEIVDGNAKMTLGMIWTIILRFAIQDISVEETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAFEVAEKYLDIPKMLDAEDIVNTARPDEKAIMTYVSSFYHAFSGAQKAETAANRICKVLAVNQENEHLMEDYEKLASDLLEWIRRTIPWLEDRV... | 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 n... |
P00785 | MGLPKSFVSMSLLFFSTLLILSLAFNAKNLTQRTNDEVKAMYESWLIKYGKSYNSLGEWERRFEIFKETLRFIDEHNADTNRSYKVGLNQFADLTDEEFRSTYLGFTSGSNKTKVSNQYEPRVGQVLPSYVDWRSAGAVVDIKSQGECGGCWAFSAIATVEGINKIVTGVLISLSEQELIDCGRTQNTRGCNVGYITDGFQFIINNGGINTEENYPYTAQDGECNVDLQNEKYVTIDTYENVPYNNEWALQTAVTYQPVSVALDAAGDAFKHYSSGIFIGPCGTAIDHAVTIVGYGTEGGIDYWIVKNSWDTTWGEEGYM... | 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
|
O62140 | MVHLNKTIQEGDNPDLTAERLTATFDTHAMAAQIYGGEMRARRRREITAKLAEIPELHDSMPLPYMTREEKIMESARKLTVLTQRMSEIIDPTDAGELYHLNNEVLGIEGNPMALHGVMFIPALNAQASDEQQAKWLIRALRREIIGTYAQTEMGHGTNLQNLETTATYDIGTQEFVLHTPKITALKWWPGNLGKSSNYAVVVAHMYIKGKNFGPHTFMVPLRDEKTHKPLPGITIGDIGPKMAYNIVDNGFLGFNNYRIPRTNLLMRHTKVEADGTYIKPPHAKINYSAMVHVRSYMLTGQAIMLSYALNIATRYSAVR... | 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), ... |
P34355 | MPLNKLIQDGDNQDLTDERFKATFDTDALAAVFHGGEDALKRIRELRDEVTKRWHLFDALPGAHRTRAERMEDVSRKLKNLMESVGEFADFTNNLDMLVIIRDVMGIEGFPLALHNLMFVPTIQNQADDEQTEWWLMDALQGKIIGTYAQTELGHGTNLGAIETTATYDKLTEEFIIHTPTTTATKWWPGGLGTSCTHVVLVANLIIDTKNYGLHPFFVPIRDRNSYSVMSGVRVGDIGTKMGVNCVDNGFLAFDNYRIPRRNMLMKHSKVSKEGLYTAPSHPKVGYTTMLYMRSEMIYHQAYYLAMAMAISIRYSAVRR... | 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.-
|
Q20992 | MSAPLIDKYRKMATFDWKKLKAAVEGEEHVRLKSEVVAKMKSEPVFHRDYRVLSREEQREVVHQRWKKIVEWGLFKDPYSDLENFHALTETLEAYDQGTSARLFLHGNVFGAAVKSMGTDRHKDLIQKTENNEIVGAFCLTEVGHGSNTAEIQTTATFDNGELVFNTPSVSAIKCWAGNLAHSATHVVVYAQLHVEGKNEGFHGFVIQVRCPRTFQTLPGITIGDMGSKPGCWQGVENGWMEFKNHRAPLSALLNKGCDITPDGKYVTSFKSASEKQSVSLGTLSVGRLGIIAKGMMACTFASTIAIRYSVARRQFGPVK... | 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 a... |
Q8RM04 | MNVPVGHLRNVQVLGIDAGGTMTDTFFVDQDGDFVVGKAQSTPQNEALGLIASSEDGLANWGMSLHEALAQLQTGVYSGTAMLNRVVQRKGLKCGLIVNRGMEDFHRMGRAVQSHLGYAYEDRIHLNTHRYDPPLVPRHLTRGVVERTDMIGTQVIPLREDTARDAARDLIAADAEGIVISLLHSYKNPENERRVRDIVLEEVEKSGKKIPVFASADYYPVRKETHRTNTTILEGYAAEPSRQTLSKISNAFKERGTKFDFRVMATHGGTISWKAKELARTIVSGPIGGVIGAKYLGEVLGYKNIACSDIGGTSFDVALI... | 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, propio... |
Q8RM03 | MNVTVDQSTLAGATRGIVRGGETLKEHRDRLMAATKATGRYAGLKTLELREREPILYNKLFSRLRAGVVDARETAKKIAASPIVEQEGELCFTLYNAAGDSLLTSTGIIIHVGTMGAAIKYMIENNWEANPGVHDKDIFCNNDSLIGNVHPCDIHTIVPIFWEGELIGWVGGVTHVIDTGAVGPGSMATGQVQRFGDGYSITCRKVGANDTLFRDWLHESQRMVRTTRYWMLDERTRIAGCHMIRKLVEEVVAEEGIEAYWKFAYEAVEHGRLGLQARIKAMTIPGTYRQVGFVDVPYAHEDVRVPSDFAKLDTIMHAPC... | 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, propio... |
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, propio... |
Q6PTT0 | MTSKGPEEEHPSVTLFRQYLRIRTVQPKPDYGAAVAFFEETARQLGLGCQKVEVAPGYVVTVLTWPGTNPTLSSILLNSHTDVVPVFKEHWSHDPFEAFKDSEGYIYTRGAQDMKCVSIQYLEAVKRLKVEGHRFPRTIHMTFVPDEEVGGHQGMELFVQRHEFHALRAGFALDEGLANPTDAFTVFYSERSPWWVRVTSTGRPGHASRFMEDTAAEKLHKVVNSILAFREKEWQRLQSNPHLKEGSVTSVNLTKLEGGVAYNVVPATMSACFDFRVAPDVDMKAFEEQLQSWCQEAGEGVTFEFAQKFTEPRMTPTDDT... | 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.... |
Q55DP8 | MNSIQENEHVTVFREFLKIRTDHPTPDYESSTKFLVEKAKEYNIPYEVYRETGTPIVLMKIEGLEPNLKTVLLNSHVDVVPAVHDSWKVDPFSAWKDESGNIFGRGTQDMKCVCMQFLEVARRIVQSGQKLKRTLHLSFVPDEEIGGSGKGMEKFVYTEKFRQLNIGLCLDEGLASPTNDFTVFYGERAPWWVHITAVGNAGHGSRFIEGTAIEKLMRTINKMLAFRQEQFESLHHGQHECGKKLGDVTSLNLTVLKAGIPIDHSNNFSYNVIPTQAEAGFDIRIPPTVNLDQFLDQIKEWTAEEGLSFKFASYIPKNEM... | 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.... |
Q03154 | MTSKGPEEEHPSVTLFRQYLRIRTVQPKPDYGAAVAFFEETARQLGLGCQKVEVAPGYVVTVLTWPGTNPTLSSILLNSHTDVVPVFKEHWSHDPFEAFKDSEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFVPDEEVGGHQGMELFVQRPEFHALRAGFALDEGIANPTDAFTVFYSERSPWWVRVTSTGRPGHASRFMEDTAAEKLHKVVNSILAFREKEWQRLQSNPHLKEGSVTSVNLTKLEGGVAYNVIPATMSASFDFRVAPDVDFKAFEEQLQSWCQAAGEGVTLEFAQKWMHPQVTPTDDS... | 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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