ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q3ZBF6 | MAATLLARACGLVRGAPWPWGWRRLHTVYQSVELPETHQMLRQTCRDFAEKELFPIAAQVDKEHRFPAAQVKKMGELGLMAMNVPEELSGAGLDYLAYSIAMEEISRGCASTGVIMSVNNSLYLGPILKFGTKEQKQQWVAPFTSGDKIGCFALSEPGNGSDAGAAATTARADGDSWVLSGTKAWITNAWEASAVVVFASTDRSLHNKGISAFLVPMPTPGLTLGKKEDKLGIRASSTANLIFEDRRIPKDSLLGEPGLGFKIAMQTLDTGRIGIASQALGIAQAALDCAVTYAENRSAFGAPLTKLQAIQFKLADMALA... | Cofactor: Binds 1 FAD per subunit.
Function: Short-chain specific acyl-CoA dehydrogenase is one of the acyl-CoA dehydrogenases that catalyze the first step of mitochondrial fatty acid beta-oxidation, an aerobic process breaking down fatty acids into acetyl-CoA and allowing the production of energy from fats. The first ... |
P16219 | MAAALLARASGPARRALCPRAWRQLHTIYQSVELPETHQMLLQTCRDFAEKELFPIAAQVDKEHLFPAAQVKKMGGLGLLAMDVPEELGGAGLDYLAYAIAMEEISRGCASTGVIMSVNNSLYLGPILKFGSKEQKQAWVTPFTSGDKIGCFALSEPGNGSDAGAASTTARAEGDSWVLNGTKAWITNAWEASAAVVFASTDRALQNKGISAFLVPMPTPGLTLGKKEDKLGIRGSSTANLIFEDCRIPKDSILGEPGMGFKIAMQTLDMGRIGIASQALGIAQTALDCAVNYAENRMAFGAPLTKLQVIQFKLADMALA... | Cofactor: Binds 1 FAD per subunit.
Function: Short-chain specific acyl-CoA dehydrogenase is one of the acyl-CoA dehydrogenases that catalyze the first step of mitochondrial fatty acid beta-oxidation, an aerobic process breaking down fatty acids into acetyl-CoA and allowing the production of energy from fats (By similar... |
P79273 | MAAALLARACGPVRGALWPRDCRRLHTIFQSVELPETYQMLRQTCRDFAEKELVPIAAQVDKEHRFPEAQVKKMGELGLMAMDVPEELSGAGLDYLAYTIAMEEISRGCASTGVIMSVNNFLYLGPILKFGSKEQKQQWITPFTSGDKVGCFALSEPGNGSDAGAAATTAQADHDSWVLSGTKAWITNAWEASAAVVFASTDRSLQNKGISAFLVPMPTAGLTLGKKEDKLGIRASSTANLIFEDCRIPKENLLGEPGMGFKIAMKTLDMGRIGIASKALGISQAALDCAVNYAENRRAFGVPLTKLQGIQFKLADMALA... | Cofactor: Binds 1 FAD per subunit.
Function: Short-chain specific acyl-CoA dehydrogenase is one of the acyl-CoA dehydrogenases that catalyze the first step of mitochondrial fatty acid beta-oxidation, an aerobic process breaking down fatty acids into acetyl-CoA and allowing the production of energy from fats. The first ... |
P15651 | MAAALLARAGGSLGRALRARDWRRLHTVYQSVELPETHQMLRQTCRDFAEKELVPIAAQLDKEHLFPTSQVKKMGELGLLAMDVPEELSGAGLDYLAYSIALEEISRGCASTGVIMSVNNSLYLGPILKFGSSQQKQQWITPFTNGDKIGCFALSEPGNGSDAGAASTTAREEGDSWVLNGTKAWITNSWEASATVVFASTDRSRQNKGISAFLVPMPTPGLTLGKKEDKLGIRASSTANLIFEDCRIPKENLLGEPGMGFKIAMQTLDMGRIGIASQALGIAQASLDCAVKYAENRHAFGAPLTKLQNIQFKLADMALA... | Cofactor: Binds 1 FAD per subunit.
Function: Short-chain specific acyl-CoA dehydrogenase is one of the acyl-CoA dehydrogenases that catalyze the first step of mitochondrial fatty acid beta-oxidation, an aerobic process breaking down fatty acids into acetyl-CoA and allowing the production of energy from fats . The first... |
P48818 | MRAARMAQSTGRQLLRLRGVSSWPGELLGQPRPGPARRPYASGVAQAAVDQSDSQPSEASTREKRANSVSKSFAVGTFKGQLTTDQVFPYPSVLNEDQTQFLKELVGPVTRFFEEVNDAAKNDMLERVEETTMQGLKELGAFGLQVPNELGGVGLCNTQYARLVEIVGMYDLGVGIVLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETIAAFCLTEPSSGSDAASIRSSAVPSPCGKYYTLNGSKIWISNGGLADIFTVFAKTPVTDTATGAVKEKITAFVVERSFGGVTHGPPEKKMGIKASNTAEVYFDGVRVPAE... | Function: Very long-chain specific acyl-CoA dehydrogenase is one of the acyl-CoA dehydrogenases that catalyze the first step of mitochondrial fatty acid beta-oxidation, an aerobic process breaking down fatty acids into acetyl-CoA and allowing the production of energy from fats. The first step of fatty acid beta-oxidati... |
P49748 | MQAARMAASLGRQLLRLGGGSSRLTALLGQPRPGPARRPYAGGAAQLALDKSDSHPSDALTRKKPAKAESKSFAVGMFKGQLTTDQVFPYPSVLNEEQTQFLKELVEPVSRFFEEVNDPAKNDALEMVEETTWQGLKELGAFGLQVPSELGGVGLCNTQYARLVEIVGMHDLGVGITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSPCGKYYTLNGSKLWISNGGLADIFTVFAKTPVTDPATGAVKEKITAFVVERGFGGITHGPPEKKMGIKASNTAEVFFDGVRVPSE... | Function: Very long-chain specific acyl-CoA dehydrogenase is one of the acyl-CoA dehydrogenases that catalyze the first step of mitochondrial fatty acid beta-oxidation, an aerobic process breaking down fatty acids into acetyl-CoA and allowing the production of energy from fats . The first step of fatty acid beta-oxidat... |
P50544 | MQSARMTPSVGRQLLRLGARSSRSTTVLQGQPRPISAQRLYAREATQAVLDKPETLSSDASTREKPARAESKSFAVGMFKGQLTIDQVFPYPSVLSEEQAQFLKELVGPVARFFEEVNDPAKNDALEKVEDDTLQGLKELGAFGLQVPSELGGLGLSNTQYARLAEIVGMHDLGVSVTLGAHQSIGFKGILLYGTKAQREKYLPRVASGQALAAFCLTEPSSGSDVASIRSSAIPSPCGKYYTLNGSKIWISNGGLADIFTVFAKTPIKDAATGAVKEKITAFVVERSFGGVTHGLPEKKMGIKASNTSEVYFDGVKVPS... | Function: Very long-chain specific acyl-CoA dehydrogenase is one of the acyl-CoA dehydrogenases that catalyze the first step of mitochondrial fatty acid beta-oxidation, an aerobic process breaking down fatty acids into acetyl-CoA and allowing the production of energy from fats. The first step of fatty acid beta-oxidati... |
A5PK26 | MTVKLDFEECLKDSPRFRASVELVEAEVSELETRLEKLLKLGNGLLESGRHYLAASRAFIVGICDLAHLGPPEPMMAECLDKFTQSLSHKLDSHAELLDATQHTLQRQIQTLVKEGLRSFREAGRDFWRGAESLEAALTHNAEVPRRRAQEAEEAGAALKVARAGYRGRALDYALQINVIEDKRKFDIMEFVLRLVEAQATHFQQGHEELSQLAQYRKELGGQLHQLVLNSAREKRDMEQRHVLLKQKELGGEEPEPSLKEGPGGLVMEGHLFKRASNAFKTWSRRWFTIQSNQLVYQKRYKDPVTVVVDDLRLCTVKLC... | Function: GTPase-activating protein (GAP) for ADP ribosylation factor 6 (ARF6) required for clathrin-dependent export of proteins from recycling endosomes to trans-Golgi network and cell surface. Required for regulated export of ITGB1 from recycling endosomes to the cell surface and ITGB1-dependent cell migration (By s... |
B8ID69 | MRSYLDFEKPVAELEAKLEELRALGARDGAVAISDDVSRLESKAAAALAELYATLTPWQKTQVARHPQRPHFVDYCAGLIEEFTPLAGDRSFGEDEAVVGGFGRFRGRPVCVIGQEKGATTEARIRHNFGMARPEGYRKAVRLMELAGRFGLPVLTFVDTAGAYPGIEAEERGQAEAIARSTEACLALGTPNVALVIGEGGSGGAIALATANRVLMLEHAIYSVISPEGAASILWRDAGRAQDAATAMKITAQDLLRLGVIDGIVPEPTGGAHREPEAAIRAAGDALAEALTGLADLDADALREQRAQKFLEIGRRL | 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... |
B5YIK7 | MTYYLDFEKPIQELEIKIEELKKLSDGSDIDLTQEIKRLNKKLKELKTEVFSNLTPWQKTQIARHPERPYTLDYISIIFEDFIELHGDRRFGDDPAVIAGIGKIDGDPYALVGHQKGRTIKERIYRNFGQAHPEGYRKALRVMKLAEKFSIPVITMIDTPGAFPGIGAEERGQAEAIANNLMEMSLLKIPLIGFVIGEGGSGGALALSVCDKIFMLEHAIYSVISPEGCAAILWKKNSDVGVEDYMRAAEELKLTAQDLKKFGIIDDIISEPLGGAHREPQEVGKRIKAKIVSVATELIKIPPDELIKKRYEKFRKIGNF... | 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... |
Q3SL76 | MKTTFLDFEQPIAELEAKIEELRFVQDDSALDISEEIRRLQKKSQALTKDIYAKLNAWQVSQVARHPQRPYTLDYIQGLFTDFVELHGDRAYADDAAIVGGMARFNGEPVMVIGHQKGRDTKEKIFRNFGMPRPEGYRKALRLMRLAEKFRLPILTFIDTPGAYPGIGAEERGQSEAIARNLYVMAELQTPIVCTIVGEGGSGGALAIGVGDRTLILQYSTYSVISPEGCASILWKSADKASVAAETLGITADRLKANGLVDRIIEEPLGGAQRDWDAMFQSMRRALTDTLAELRKQPTEAMLGARYQRLRAYGSFKEAP... | 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... |
Q73Q55 | MSNKDQTNLLNNLKDIAQKAGLDISEELAKINAKLESSTALSKTWERVELARHSDRPRTLDYINLIFDNFTELHGDRFFGDDPAMIGGIGFIDGMPVTVIGTQKGRNLRETIDRNGGMANPEGYRKAMRLAKQAEKFKRPIITFIDTQGAYPGLGAEERGIGEAIAFNLREFSRLKTPIICIIIGEGGSGGALGIGVGDKIYMLENAIFSVISPEGCASILLRDSSRAKDAAAMLKITSQEVLDLKVINGIIPEPEKGAHTDPKKTADAIKEQILKDLADLTKRDPAVLVKYRSKKIRSIGKYSE | 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... |
B9DY13 | MLNKFFKKTKYITVSQRALGDIHDDFTKKPSIPNGMWVKCDGCGKVLYKNDMEKNNKVCYHCGYHFRMNALERLELILDKESFYEFDKDITAANPIEFKGYEDKIKNMQNKTNIKEAVITGKGTIGREEAVVCIMDSNFMMGSMGSVVGEKITRAVEKSIELKLPLIIFTTSGGARMQEGIFSLMQMAKVSGAISRLNEEGLLYLSVLTDPTTGGVTASFAMIGDIILAEPGALIGFAGKRVIEQTIKQKLPEGFQKAEFLLQHGFIDNIVSRENLKETLRKILVIHGRGN | 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... |
Q8XLG6 | MIKNLLNKRKYITVSSVELNDTELSEDEKPNIPSGMWSKCEKCAKILYTEDLRENFNVCPNCGHHFKLGAYERIKYLTDENTFVEFDKKMIGRNPLDFNGYEEKIKGYQKKSHVIEGVVTGEAYIAQRKVVLCVMDSNFMMGSMGTAVGEKITRAIEYATKNRLPLIIFTCSGGARMQEGIYSLMQMAKVSGAIYRHGRENLLYITVLTNPTTGGVTASFAMEGDIILSEPGCLVGFAGRRVIEGTINEKLPDDFQTAEFLLEKGFIDKIVQRKDLKQVITSLLRMHEVDYE | 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... |
B1VKF0 | MCEENENKDSEYIETTPVENGYNSERFKHLWFLCENCETLIYKKSLLEQKGVCAECGATLQMTSSERIELLIDNGTWRSINTKLSSIDVLEKKHTTFDIKMVRKVSILLYKVISGKYFYKEFFKNKYYNKALRILVAYNNTLVNILKVALGSKFIKYLNLDSKETIKILQDIIDTGLKTAQFALFEIRKKIKNEFYRFALLNKAFENKQISSLLAQNLEDRRDDESEIISIEFDRMAFRVQTFLILESLLKLNTQLADVKEQLLSQDKFLKAVATSLVKKELYFPEDKRKTRKIKKIFPFYPGTDPETDYFLWLRTHMAI... | 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... |
Q2QD80 | MEKRWLNSMLSKGELEYRCRLSKSINSLGPIESEGSIINNMNKNIPSHSDSYNSSYSTVDDLVGIRNFVSDDTFLVRDSNSSSYSIYLDIENQIFEIDNDPSFVSELESSFYSFRNSTYQNNISKNDDSHYDRYMYDTKYSWNNHINSCIDSYLRTQICIDSYILSGSHNYSDSYIYSYICGEGGNSSESESFSIRTSTHGNNLTITESSNDLDNDRTTNYSDFWVICENCHKFNYKRLFKSKMNICEECGYHLKMNSSDRIELLIDPGTWEPMDEDMVSVDPIEWDSEVDPIQWKSQVDPIEGDSEVDLIEGDSEEYKD... | 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... |
A7M907 | MQNWIDNSFQAEFEQESYFGSLGENSTNPSSGGDRYPEALIIRDITGKTSAIYFDITDDILENDPHQTILLSPIENDIWTEKDVIIDTYRYINELIFCDEKSQQKQKDRTEFIKKEQLQLISNRNPDHYRNLWNQCENCFIPNYKKVLKSNMQICEECGSYFKMTSSDRIDLLIDEGTWNPLDQDMVSLDSSEFDSEAELECYEDNIKEWNEEMCQAFMRKLSKDLKEGQALERTANLIEEPWLPEYIQPEEKVEEWTKPDLDEGEESQDEERWIWELDKGEESQEIEDSEANDEDDDDAPYVERLAFYKKETGLLDAVQ... | 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... |
P31562 | MERREGGRDNSSCSNVNQLFGVKDSESLLYDDVFIVRDRNGDSYFAYWDIEKNTFLSEPFYSYRSRNSSYLPKIKAFMSEDRSQIHEVKNGFRSEDHSKINKINGVENLFHNYNMNVLTDDYNFKMGMNGFHRPQSKIHINRFIDSYLQSQICIATTPGSGSDNDSYIHGSRVYGESESYTRSEGRSSSIRTRTKGVELTLRERPGILDRTKKYMYLWLQCDNCYGLNYKKVLKSKMTICEQCGYHLQMSSSDRIELLIDPGTWDPMDEDMVSRDPIKFDSGGGEAYKDRLYFYQRKTGLTEAVQTGIGQLNGIPVAIGV... | 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... |
Q9TLW3 | MPNGTKLAKSFLWKKCDSCNILISKFDFYKHDKVCPECNYHFPMYSSERINHIIDLKSWIPLYNNLLSGDPLGFCDKKPYITRLAENQKITGLDEAVQTGIGRINNISASVAVMDFNFMGGSMGSAVGEKITRLVEFSTKEELPIVIISASGGARMQEGILSLMQMAKISAALERLQSKGLLYISILSSPTTGGVFASFAMLGDIILAEPKAVVGFAGKRVVEQTLNEKLPPNFQSAEYLLDNGFVDLIVKRKQLKKTIHMILDLHN | 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... |
Q87YI2 | MSNWLVDKLIPSIMRSEVKKSSVPEGLWHKCPSCDAVLYRPELEKTLDVCPKCNHHMRIGARARLNIFLDVDGREELGVDLEPVDRLKFRDGKKYKDRLTAAQKQTGEKDALISMSGTLLGMPVVASAFEFSFMGGSMGAIVGERFVRAANYALENRCPMICFAASGGARMQEALISLMQMAKTSAVLARLREEGLPFISVLTDPVYGGVSASLAMLGDVIVAEPKALIGFAGPRVIEQTVREKLPEGFQRSEFLLDHGAIDMIIARSELRPRLGNLLAQMMNLPTPRFVAPVIEPIIVPPAPATI | 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... |
A5WDG8 | MTKNNNDLSNSSSNPPSNRPVAGKEAELEIQRETHAAQSGQSESWLSRPIPTVKRNSLPQLTAVETEPSTECPQCHSMITNTALIFNAYVCPHCDHHLAMTARERLTGFLDHIEAELGQEFSASDPLKFVDSKPYPQRMEQMQTKTGETEALIVLQGKLRDMDVVACAFDFRFMGGSMGSVVGDRFVQAAEVALTNKAPLICFAASGGARMQEGVLSLMQMARTSAAIERLRLAGIPYIVVLTNPVYGGVTASLAMLGDIHIAEPKAMIGFAGKRVIEQTVRETLEEPFQRAEYLLEHGVIDQVVHRHQMNDTVYRLLAK... | 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... |
Q9S7D9 | METRCSLLFLSLILLYLPKPGSGFGSSGPIAASFGGSAFFCAIDASGRQDVICWGKNYSSPSSPSSSSSSSSIASSTSASYNIPSMAVLSGGDGFLCGILSNTSQAFCFSSLGSSSGMDLVPLAYRTTAYSQIAAGNSHVCAVRGAYYSDHDSGTIDCWEITRATNNNSLIAKENPNFYDQIVSNLVFNNIVSGDGFSCGGIRDGGMLCFGPNSSNLGFNTTSDNFQVLAAGKNSVCAILNLSREVKCWGEDESFVNSPMNDSRFVSLTAGPRHFCGIREDNHEVECWGNSNFSLIPKGSGFKAIASSDFIVCGIREEDL... | Function: Serine/threonine-protein kinase with low activity.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 84185
Sequence Length: 775
Subcellular Location: Membrane
EC: 2.7.11.1
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O80963 | MQPNSHIFVIITISSLIITVSAYGSTGTIAAAFGENGFFCAIDASGKQEVICWDRGNTNRSLNRPPGEISGYSPPMTSLSGGEGFLCAITSNTSRAFCWNLEDPSENLVPRAFQYNSYLQIASGNNHVCAISGLYYSGPDYGPVHCWEYSDNTNFTSGLLWNSSFHNPYIDSLMFRKIVSGDGFSCGVTKDGDLVCWGPKSNLLNFSNNEEFEVLASGRNSVCGVSKDSGQLHCFGDETEFGSLPNRPRFIALSAGANHYCGIREDDHGVECWGRNLNSSSSSSAPNTSGFVAISSSDSTTCGVRELDLVLDCWRVHDSS... | Function: Serine/threonine-protein kinase with low activity.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 85303
Sequence Length: 776
Subcellular Location: Membrane
EC: 2.7.11.1
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Q9LY50 | MKRFINSTVTFSVTVTIAVIIFFLLSPVTSLGSGSTYAVVYGSDTVCALISGQPTQRILCYDTRLNINVTLNPGVSFSSIAAGDNFLCGIRSGGYSLLCWDNIGSYSPNRKRIYQNDNVLLETLSVGDKQICATVNGTNSLKCWRGSVSDQSKPPNERFRSISSGVGFSCGVSIRNNRILCWGTDPVKSNQIQTGFGNTPMVTISAGKSHACGLNTTGNLICIGNNDSGQLNVIAPDQPNLYSSSLSLGSNFTCAMRISNNSVVCWGGGAERFNNVTDSISFESISSGPGLICGLISSNLSIMCWNPTNFSRIFLPFPEV... | Function: Serine/threonine-protein kinase.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 87682
Sequence Length: 814
Subcellular Location: Membrane
EC: 2.7.11.1
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Q9FIJ6 | MALTISISCFSSYFVSLLLLVLSSFSFVCFSLSTVSISHISNQTLVCALNNHSYLQCSSFPLNSIPFSLTGNLRNRRFSGVVSGNGFVCGLISRLDSNTSTLLCWRFSVDGTNMLHKRIYHGPELEELEAGNFRICGVERVSRRLRCWQPYYLPRPDNYRSIALGDNFFCGLSQPPGMISCEGIAKVPSGDHYIAIAAGSRQACAITVDNDVECWGQTQSLPREKFLALAVGEDRGCGVRWSNGTVVCWGNNNNFSLPQTLKDIHFTSIYAKGPMFCGVATRNYTLICWGNENFKSGVFTPFQGLISQVVMPGPCRRECP... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 83774
Sequence Length: 751
Subcellular Location: Membrane
EC: 2.7.11.1
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Q8S4Y1 | MAHTSESVNPRDVCIVGVARTPMGGFLGSLSSLPATKLGSLAIAAALKRANVDPALVQEVVFGNVLSANLGQAPARQAALGAGIPNSVICTTVNKVCASGMKAVMIAAQSIQLGINDVVVAGGMESMSNTPKYLAEARKGSRFGHDSLVDGMLKDGLWDVYNDCGMGSCAELCAEKFQITREQQDDYAVQSFERGIAAQEAGAFTWEIVPVEVSGGRGRPSTIVDKDEGLGKFDAAKLRKLRPSFKENGGTVTAGNASSISDGAAALVLVSGEKALQLGLLVLAKIKGYGDAAQEPEFFTTAPALAIPKAIAHAGLESSQ... | Function: Catalyzes the condensation of two molecules of acetyl-CoA to produce acetoacetyl-CoA . Generates the bulk of the acetoacetyl-CoA precursor required for the cytosol-localized, mevalonate-derived isoprenoid biosynthesis . The generated isoprenoids are required for normal growth and development . Essential prote... |
Q709F0 | MKPGATGESDLAEVLPQHKFDSKSLEAYLNQHLSGFGAEREATLTIAQYRAGKSNPTFYLQKGFQTYVLRKKPPGSLLPKAHQIDREFKVQKALFSIGFPVPKPILYCSDTSVIGTEFYVMEHVQGRIFRDLTIPGLSPAERSAIYVATVETLAQLHSLNIQSLQLEGYGIGAGYCKRQVSTWTKQYQAAAHQDIPAMQQLSEWLMKNLPDNDNEENLIHGDFRLDNIVFHPKECRVIAVLDWELSTIGHPLSDLAHFSLFYFWPRTVPMINQGSYSENSGIPSMEELISIYCRCRGINSILPNWNFFLALSYFKMAGIA... | Function: Acyl-CoA dehydrogenase, that exhibits maximal activity towards saturated C22-CoA . Probably participates in beta-oxydation and energy production but could also play a role in the metabolism of specific fatty acids to control fatty acids composition of cellular lipids in brain (Probable).
Catalytic Activity: a... |
B3DMA2 | MEMDVTRDTVEVLPQHKFDIRSLEAYLNQHLPGFGSDHRAVLTVTQYRSGQSNPTFFLQKGSQAYVLRKKPPGSLLPKAHKIDREFKVQKALFSVGFPVPKPLLYCSNASIIGTEFYVMEHVQGRIFRDFSIPGVSPAERAAIYVSLVETLAWLHSLDIHSLGLDRYGTGVGYCKRQVSTWTKQYQASAHQSIPAMDQLSTWLMRNLPDSDNEECLVHGDFKLDNIVFHPKECRVIAVLDWELSTFGHPLSDLAHLSLFYFWPRTLPMINRGSHIQENTGIPLMEELISIYCRRRGIDPNLPNWNFFMALSFFKLAGIAQ... | Function: Acyl-CoA dehydrogenase, that exhibits maximal activity towards saturated C22-CoA. Probably participates in beta-oxydation and energy production but could also play a role in the metabolism of specific fatty acids to control fatty acids composition of cellular lipids in brain.
Catalytic Activity: a 2,3-saturat... |
O29057 | MERLFYPKVVAVIGASPQEGKVGNTIMKNLRNFSGTVYAVNPKYREILGFPCYPSVLKIPENVDLAIIVVPAKLVPKAVEECGRKDVEGAVVISAGFKEAGIEGAKLERELVEVAERYGVKLVGPNCLGMINTEIAMNATFSRVAPEKGRIAFLSQSGAFILAVLEWSKRNGVGFSKVVSLGNKAMLDESDFLEYLAKDDSTDVILIYMEGVEDGRKFMRVAKSVARRKPVVVMKAGKSQSGAKAASSHTGSLAGSYEAYRAAFRQSGVIEASSVEELFDFALLLLKYRKAGNLAILTNSGGPGVMAADACDQFGVPLAN... | Function: Catalyzes the reversible formation of acetate and ATP from acetyl-CoA by using ADP and phosphate. Can use other substrates such as propionyl-CoA and butyryl-CoA, but not phenylacetyl-CoA. Seems to be involved primarily in the conversion of acetyl-CoA to acetate. Participates in the degradation of branched-cha... |
Q6BZP5 | MLRTRFINSVNSARAMSRNINTLSQFPYPTLQQEESFFKSQVEDIEKWWASPRYEGIKRPYTAEKVAIHRGTLPQTYASSVQAEKLFNIFTERGKQGLPVHTTGSVDPVQMTQSAPHQEVVYISGWACSSLLTTTNEVSPDFGDYPYDTVPNQVDRIFRAQGLHDKKAWHEWMSLSHEERVKRDQEGKGRIDYLRPIIADADTGHGGLSAVMKLAKLFAERGAAAIHLEDQLHGGKKCGHLAGKVIVPTGSHISRLNATRMQWDIMGCSNLVIARTDSESAKLLSSAADPSDHEYILGVVKPIKPLAEVLLTAEANGATA... | Function: Component of the methylcitrate cycle that catalyzes the formation of pyruvate and succinate from 2-methylisocitrate during the metabolism of endogenous propionyl-CoA.
Catalytic Activity: (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = pyruvate + succinate
Sequence Mass (Da): 63005
Sequence Length: 565
Pathway:... |
Q12031 | MITMINNKTFNRKTTGTLKKLVLSSDKSLRRSFNGASSTKDFVFSESSKVEEWWESARFKNISRPYSATDVVKHRGSLPANTSIYPSSYQARKLFNLLEENFKNGTPLHTLGVIDPVQMSQLARCRNIKVAYISGWACSSTLVGSTNEVSPDFGDYPYDTVPNQVERIFKAQQLHDRKAFLEASIKGSTPVDYLKPIIADADMGHGGPTTVMKVAKLFAEKGAAGIHLEDQMVGGKRCGHLSGAVLVPTATHLMRLISTRFQWDIMGTENLVIARTDSCNGKLLSSSSDPRDHEFIRGIIRDNVVPWSEKLIEMEDKKIP... | Function: Catalyzes the formation of pyruvate and succinate from 2-methylisocitrate during the metabolism of endogenous propionyl-CoA. Does not act on isocitrate.
Catalytic Activity: (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = pyruvate + succinate
Sequence Mass (Da): 64976
Sequence Length: 575
Pathway: Organic acid ... |
Q3IKY9 | MPDTITNKLQNSTVQDVIATKLARAVFAGFEAMFATFLNITLGAQSRFEQRQYHEVQSAMRERLQVYERQVKSVSEAVKVIAYAELSCPQTWQLAKNIYGNMVKNHENEPIAHTFFNSTFGAIWDDKKIRTVHLFVLKAKYRTQPRPYDSLVKRISLQHGFNSAIKTLITNQVFRVPFSNLNQDVATLQATLTQGAKQQCRQVYELINLNDGYIEYAYSHFYRNKACYLIGRCIAKNGDNMPFAIAILNTPKGLKIDAVMMGADQLSLLFGFARTYFMVDTDQPARYVDYLSVLMPHKQRFELFNAIGFIKHAKTEFYRY... | Function: Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is f... |
Q3IHD9 | MQPRHIAELILTGFKKHYLLFQKTTAKAPLAFAKRDWQAINDISRLRISHYDDRVNETTATLRQQQTEQLDEQLWLEVKKLYQHFLCFHPQAELAETFYNSVFCRLYHRRYFHNDFIFVEATLKDAPAVPVEAEYRSYFPVVDGLKPTIKQIINHFDFKAPFVNLERDIRLLVKAFYKQAPDTHHKAWQMRFDILHTPFYRNKAAYIVGRVVSQSGVQPFIIAVLHHEDKGLYLDALLTKSSQMRVIFGFARAYFMVETHAPCALVRFLNQLMPNKTIAELYNAIGFHKQGKTEFYREFLNHLTHSNDEFTIAPGTPGMV... | Function: Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is f... |
Q2IJI0 | MLDERGALARGAAEAIRAGYEAYQAERARITARARGRFEARDWAGAQRDARERLDLRDGVVHRTVGEVRAELGGAVQDREVWRRAKEAFEAVAAARPDAEIAGSFFNSVTRRVLTTVGVDPAIEFLAADAPPPREDPPQHRAFAREATTEALLARILRAAPISAPFEDLARDARLAALELDAHVRGLPDRQPIDAVELARPVFYRGKGAYLVGRIRRGRHLTPLVLALAHGDRGVALDAVLFTEEDVSIVFGFTRSYFHVALERPRAMVAFLSTLLPLKRRSELYTGLGYHKHGKAELYREVAQHLAEGDDRFVPARGDR... | Function: Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is f... |
Q7WDP2 | MIYSGDVQRIEPAPVAGPAPLDVAHLILAGFDRHYALFRYSAQRAKSLFESGDWHGMQRLSRERIEYYDMRVRECATQLDSALRGSDARTADGSRANGSAALSEAQTAFWQAVKQEFVGLLADHRQPECAETFFNSVSCRILHRDYFHNDFLFVRPAIATDYLDSRIPSYRVYYPVAEGLHKSLIRMVADFGLAVPYADLPRDARLLARAAVRQLRGQLPRHAGPRLASDCQIQVLGSLFFRNTGAYIVGRLINQGTVYPFAVALRRNPAGQVCLDALLLGADDLSTLFSFTRAYFLVDMETPAAVVNFLASLLPRKPKA... | Function: Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is f... |
Q0BBE2 | MNHFPKLLSSQIGFDVAQTMLENFDRHYRIFREAAVDAKTLYERADWHGLQRLARERITSYDDRVQECVEVLQDEYDAENIDDEVWQQIKLHYIGLLTSHRQPECAETFFNSVCCKILHRSYFSNDFIFVRPAISTEYLENDEPAAKPTYRAYYPGTDGLAATLERIVTNFQLEPPFEDLTRDIGCVMQAITDEFGEFDAAPNFQIHVLSSLFFRNKSAYIVGRIINADRVLPFAVPIRHVRPGLLALDTLLLRRDLLQIIFSFSHSYFLVDMGVPSAYVEFLCTIMPGKPKAEIYTSVGLQKQGKNLFYRDLLHHLSHS... | Function: Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is f... |
Q86GC8 | MEIRGLITRLLGPCHLRHLILCSLGLYSILVQSVHCRHHDIGSSVAHQLGSKYSQSSSLSSSSQSSSSLAEEATLNKDSDAFFTPYIGHGDSVRIVDAELGTLEREHIHSTTTRRRGLTRRESSSDATDSDPLVITTDKGKIRGTTLEAPSGKKVDAWMGIPYAQPPLGPLRFRHPRPAERWTGVLNATKPPNSCVQIVDTVFGDFPGATMWNPNTPLSEDCLYINVVVPRPRPKNAAVMLWIFGGGFYSGTATLDVYDHRTLASEENVIVVSLQYRVASLGFLFLGTPEAPGNAGLFDQNLALRWVRDNIHRFGGDPSR... | Function: Rapidly hydrolyzes choline released into the synapse.
Catalytic Activity: acetylcholine + H2O = acetate + choline + H(+)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 78179
Sequence Length: 702
Subcellular Location: Synapse
EC: 3.1.1.7
|
P07140 | MAISCRQSRVLPMSLPLPLTIPLPLVLVLSLHLSGVCGVIDRLVVQTSSGPVRGRSVTVQGREVHVYTGIPYAKPPVEDLRFRKPVPAEPWHGVLDATGLSATCVQERYEYFPGFSGEEIWNPNTNVSEDCLYINVWAPAKARLRHGRGANGGEHPNGKQADTDHLIHNGNPQNTTNGLPILIWIYGGGFMTGSATLDIYNADIMAAVGNVIVASFQYRVGAFGFLHLAPEMPSEFAEEAPGNVGLWDQALAIRWLKDNAHAFGGNPEWMTLFGESAGSSSVNAQLMSPVTRGLVKRGMMQSGTMNAPWSHMTSEKAVEI... | Function: Rapidly hydrolyzes choline released into the synapse. It can hydrolyze butyrylthiocholine.
PTM: Proteolytic cleavage into the 16 kDa subunit and the 55 kDa subunits originates from the hydrophilic peptide, aa 148-180, and is associated with excretion out of the cell.
Location Topology: Lipid-anchor
Catalytic ... |
P22303 | MRPPQCLLHTPSLASPLLLLLLWLLGGGVGAEGREDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMGPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGTEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGFYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPGSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGESAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGEARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVNHEWHVL... | Function: Hydrolyzes rapidly the acetylcholine neurotransmitter released into the synaptic cleft allowing to terminate the signal transduction at the neuromuscular junction. Role in neuronal apoptosis.
Catalytic Activity: acetylcholine + H2O = acetate + choline + H(+)
Location Topology: Peripheral membrane protein
Sequ... |
Q27677 | MGQLSILCLFVTVCASVCGYSWPSDETTTKPSQFKDFHTDPLVVETTSGLVRGYSKTVLGREVHVFTGIPFAKPPIEQLRFKKPVPIDPWHGILDATKQPNSCFQERYEYFPGFEGEEMWNPNTNISEDCLYLNIWVPQRLRIRHHADKPTIDRPKVPVLIWIYGGGYMSGTATLDVYDADIIAATSDVIVASMQYRLGSFGFLYLNRYFPRGSDETPGNMGLWDQILAIRWIKDNAAAFGGDPDLITLFGESAGGGSISIHLISPVTKGLVRRGIMQSGTMNAPWSYMSGERAEQIGKILIQDCGCNVSLLENSPRKVM... | Function: Rapidly hydrolyzes choline released into the synapse.
PTM: The N-terminus is blocked.
Location Topology: Lipid-anchor
Catalytic Activity: acetylcholine + H2O = acetate + choline + H(+)
Sequence Mass (Da): 71142
Sequence Length: 629
Subcellular Location: Synapse
EC: 3.1.1.7
|
Q92081 | VPSPRPQNATVMVWIFGGGFAYGTSSLNVYDGRYLAQAEGAIVVSMNYRVGALGFLSLPGSPVPGNAGLFDQQLALRWVHGNIHRFGGNPQSVTLFGESAGSASVAPHLLSRHSQQFFQRAILQSGTLNAPWATVEDTEARRRAEALAQALGCPTDDDNELLNCLYARPPQEIVSKEGDVVIEPSIFRFPFVPVVDGHFIIDSPIVLLQQGIFKKTDLLLGVNRNEGSFFLIYGAPGFSKDHESLISREDFLENIPMIVPQGNEVSVDAIVLQYTDWLAQNDALKNRDAIEDIVGDYNVICPVVEMATRYAEFGNNVYFY... | Function: Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft.
Catalytic Activity: acetylcholine + H2O = acetate + choline + H(+)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 37300
Sequence Length: 338
Subcellular L... |
Q7LZG1 | SELKVATQTGFVRGLSLPVLAGHVSAHLGVPFAEPFLRPEPVKPGAEMWNPNLNIWVPSGRVGAFXFLTVTLFGESAGAASVGMXLLSTQRAILQSGAPNAPWAQVQPAESRFPFVPVIDGEFFPLGVNKDEGSFGVPGFSKXXESLINQAVPHANDIYTDWQDQDNGGLPLTGNPTXPHN | Function: In venom, its toxic role is unclear: it could result in less musculatory control by rapidly hydrolyzing acetylcholine, or that it works synergistically with alkaline phosphatase (ALP) in paralyzing prey through hypotension. In muscle, it terminates signal transduction at the neuromuscular junction by rapid hy... |
P04058 | MNLLVTSSLGVLLHLVVLCQADDHSELLVNTKSGKVMGTRVPVLSSHISAFLGIPFAEPPVGNMRFRRPEPKKPWSGVWNASTYPNNCQQYVDEQFPGFSGSEMWNPNREMSEDCLYLNIWVPSPRPKSTTVMVWIYGGGFYSGSSTLDVYNGKYLAYTEEVVLVSLSYRVGAFGFLALHGSQEAPGNVGLLDQRMALQWVHDNIQFFGGDPKTVTIFGESAGGASVGMHILSPGSRDLFRRAILQSGSPNCPWASVSVAEGRRRAVELGRNLNCNLNSDEELIHCLREKKPQELIDVEWNVLPFDSIFRFSFVPVIDGE... | Function: Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft. May be involved in cell-cell interactions.
PTM: An interchain disulfide bond is present in what becomes position 593 of the T isoform.
Location Topology: Lipid-anchor
Catalyt... |
W4VSJ0 | MMLPRCFVTVLLMSSVLYIGGETSSEVLGPVVSTEAGSFQGMELTTHGERVIYAFLGIPYAKPPTGLLRFKKPQPADFIQGTYKATEKPPSCFQLDSDLQLPWADPDSPMKEDCLFLNLWTPASLSTEEEELKSVMVWIHGGGYTSGSSALDVYDGQTLSSSGDVVVVTMNYRLDAFGFLNSLTEDAPGNMALYDQLLALQWVHTNIKYFGGDPNKVTLFGESVGAFATSFLALSPLTKGLFQKIMLESGSAYNKLTVNSIDQAKNNNQLATLVGCANETFTLISNPEEVVACMREVAPAKFTQTYYKELGSEREKINFI... | Function: Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft.
Catalytic Activity: acetylcholine + H2O = acetate + choline + H(+)
Sequence Mass (Da): 62782
Sequence Length: 559
Subcellular Location: Secreted
EC: 3.1.1.7
|
Q6I681 | MGLGLGVRAAPFTYAAHALAVAAAAMVLVWSIQFRGGLAIESTNKNLIFNVHPVLMLIGYVIIGGEAIMVYRVLPTSNHDTTKLIHLILHGIALVLGAVGIYFAFKNHNESGIANLYSLHSWIGIGTITLYGIQWIIGFVTFFFPGAAPNVKKGVLPWHVLFGLFVYILALANAELGFLEKLTFLESSGLDKYGTEAFLVNFTALVVVLFGASVVVAAIAPVRLEEPQGYDPIPEN | Cofactor: Binds 2 heme b groups non-covalently.
Function: Two-heme-containing cytochrome. Catalyzes ascorbate-dependent trans-membrane electron transfer by utilizing a concerted H(+)/e(-) transfer mechanism.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 25425
Sequence Length: 236
Subcellular Locati... |
Q5DZD2 | MNNEYVLVINSGSSSLKFAVIDSVSGDAVLSGLGECFGLEDARMSWKYQGQKTEIAIEGNENHHKIAIGKLVGLTEELGFTDGIVAIGHRIVHGGEKFTKTVRINEEVTKEIESLSDLAPLHNPAGAIGIRAAVEAFPSLPQFAVFDTAFHQTMPKRAYTGAIAKELYTDFGVRRYGFHGTSHYFVSREAAKMINKPIEESNFISVHLGNGASVCAIKDGNSVDTSMGFTPLSGLMMGTRCGDLDPGIIEYLLKKGWSQEQVFNSLNKESGFLGVSGLTSDARGILEAMEEGHEGATLAFQVFTYRVAKYVASYLAALDS... | 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): 42742
Sequence Length: 397
Pathway: Metabolic intermediate biosynthesis; acetyl-CoA... |
Q9CE36 | MEKTLAVNAGSSSLKWQLYEMPEETVIAKGIFERIGLSGSISTTKFNNEEHFRKQEIVDHRQAVLLLMDELIHFKLIHEFREITGIGHRVVAGGEFFKTSTVISPEVLAEIKNLSTLAPLHNPANVLGIEAFQRLLPDALAVAVFDTAFHSTLPEKAYRYPIPTKYYEDYSIRKYGAHGTSHMYVAQEAEKVLGKPLEDLKLITAHIGNGASITAIEAGKSVDTSMGFTPLAGVMMGTRAGEMDASVIPYMLESDPSLRNAQDVIDILNKDSGVLGVSELSSDMRDLSEAVAKGNPKAILAYEMYVDRLKKFIAQYFGVL... | 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): 43225
Sequence Length: 395
Pathway: Metabolic intermediate biosynthesis; acetyl-CoA... |
A5FE24 | MKILIINSGSSSIKYQLMVMPANEVICSGMIDRIGLETSNITFKTVSNSFEEILPVPTHKVGLQKVADMLLDAETGVIKTTSEITAVGHRVVHGGSYFSNTTVITEEVKEKIKELSELAPLHNPAHLVGINVAEEIFASAKQVAVFDTAFHQTIPVEAHKYAIPNFLLTEHKVRVYGFHGTSHKYVSEKAINYLEKGSKIITIHLGNGCSMTAVKDGKSIDTTMGFSPANGLVMGTRAGDIDQSVIFYMVKSLGYTPDEVNSILLKQSGMLGLTGYSDLRDIESKASEGNKDCQLALLMNAYRIRKTIGSYAAALNGLDA... | 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): 43237
Sequence Length: 394
Pathway: Metabolic intermediate biosynthesis; acetyl-CoA... |
Q0BPA5 | MSEILVLNCGSSSVKFALINPHTSQSLVTGLAENIATKNCKVVFKAEHKIEKYLENGSYKDVFEMLKDFLVENKHLEKIVAIGHRVVHGGQYFSKSVLINADSLEKIKACIALAPLHNPAHIEGIRFCQQIFPELPQVAVFDTAFHQTVPSYIAEYAIPYELTHKHNIRKYGAHGTSHKYVSEQAAKILTQQKANVIVAHLGNGCSITAVVDGKSIDTSMGLTPLDGLVMGTRSGCIDPSIFAYIISDNLGWSVTEITNMLNKQSGLLGICGHNDMREVSQLAAKGDSLAKLAIEIFSHRVAKFVASYMIYFNKLDALVF... | 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): 42303
Sequence Length: 385
Pathway: Metabolic intermediate biosynthesis; acetyl-CoA... |
Q8RED7 | MKILVINCGSSSLKYQLINPETEEVFAKGLCERIGIDGSKLEYEVVAKDFEKKLETPMPSHKEALELVISHLTDKEIGVIASVDEVDAIGHRVVHGGEEFAQSVLINDAVLKAIEANNDLAPLHNPANLMGIRTCMELMPGKKNVAVFDTAFHQTMKPEAFMYPLPYEDYKELKVRKYGFHGTSHLYVSGIMREIMGNPEHSKIIVCHLGNGASITAVKDGKSVDTSMGLTPLQGLMMGTRCGDIDPAAVLFVKNKRGLTDAQMDDRMNKKSGILGLFGKSSDCRDLENAVVEGDERAILAESVSMHRLRSYIGAYAAIM... | 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): 43625
Sequence Length: 398
Pathway: Metabolic intermediate biosynthesis; acetyl-CoA... |
Q7NLW9 | MKVLVLNAGSSSQKSCLYDLPHTQLPQEPPQPLWEAQIDWPHGGDGAKLKIKTVHHRHEKTLQGGSRSEDSARMLETLYSGETRVIADPSEIEMVGHRVVHGGEAYRESTRITPEVKAAIDQLARFAPVHNPANLAGIEALEALLGPQVPQIAVFDTAFHSRLPAAAYVYPGPYEWLDQGIRRYGFHGISHRYCAERAAQILGRDLAQLRLITCHLGNGCSLAAVQGGFSIDTTMGFTPLEGLMMGSRSGSVDPGILIHLMRQADYTVDKLDHILNQASGLEGVSGISNDLRPLFKAIDEGNARAKLALDIYIHRLRAGI... | 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): 43835
Sequence Length: 405
Pathway: Metabolic intermediate biosynthesis; acetyl-CoA... |
Q16570 | MGNCLHRAELSPSTENSSQLDFEDVWNSSYGVNDSFPDGDYGANLEAAAPCHSCNLLDDSALPFFILTSVLGILASSTVLFMLFRPLFRWQLCPGWPVLAQLAVGSALFSIVVPVLAPGLGSTRSSALCSLGYCVWYGSAFAQALLLGCHASLGHRLGAGQVPGLTLGLTVGIWGVAALLTLPVTLASGASGGLCTLIYSTELKALQATHTVACLAIFVLLPLGLFGAKGLKKALGMGPGPWMNILWAWFIFWWPHGVVLGLDFLVRSKLLLLSTCLAQQALDLLLNLAEALAILHCVATPLLLALFCHQATRTLLPSLP... | Function: Atypical chemokine receptor that controls chemokine levels and localization via high-affinity chemokine binding that is uncoupled from classic ligand-driven signal transduction cascades, resulting instead in chemokine sequestration, degradation, or transcytosis. Also known as interceptor (internalizing recept... |
Q9QUI6 | MGNCLYPVETLSLDKNGTQFTFDSWNYSFEDNYSYELSSDYSLTPAAPCYSCNLLDRSSLPFFMLTSVLGMLASGSILFAILRPFFHWQICPSWPILAELAVGSALFSIAVPILAPGLHSAHSTALCNLGYWVWYTSAFAQALLIGCYACLNPRLNIGQLRGFTLGLSVGLWGAAALSGLPVALASDVYNGFCTFPSSRDMEALKYTHYAICFTIFTVLPLTLLAAKGLKIALSKGPGPWVSVLWIWFIFWWPHGMVLIFDALVRSKTVLLYTCQSQKILDAMLNVTEALSMLHCVATPLLLALFCHQTTRRSLSSLSLP... | Function: Atypical chemokine receptor that controls chemokine levels and localization via high-affinity chemokine binding that is uncoupled from classic ligand-driven signal transduction cascades, resulting instead in chemokine sequestration, degradation, or transcytosis. Also known as interceptor (internalizing recept... |
O00590 | MAATASPQPLATEDADSENSSFYYYDYLDEVAFMLCRKDAVVSFGKVFLPVFYSLIFVLGLSGNLLLLMVLLRYVPRRRMVEIYLLNLAISNLLFLVTLPFWGISVAWHWVFGSFLCKMVSTLYTINFYSGIFFISCMSLDKYLEIVHAQPYHRLRTRAKSLLLATIVWAVSLAVSIPDMVFVQTHENPKGVWNCHADFGGHGTIWKLFLRFQQNLLGFLLPLLAMIFFYSRIGCVLVRLRPAGQGRALKIAAALVVAFFVLWFPYNLTLFLHTLLDLQVFGNCEVSQHLDYALQVTESIAFLHCCFSPILYAFSSHRFR... | Function: Atypical chemokine receptor that controls chemokine levels and localization via high-affinity chemokine binding that is uncoupled from classic ligand-driven signal transduction cascades, resulting instead in chemokine sequestration, degradation, or transcytosis. Also known as interceptor (internalizing recept... |
O08707 | MPTVASPLPLTTVGSENSSSIYDYDYLDDMTILVCRKDEVLSFGRVFLPVVYSLIFVLGLAGNLLLLVVLLHSAPRRRTMELYLLNLAVSNLLFVVTMPFWAISVAWHWVFGSFLCKVISTLYSINFYCGIFFITCMSLDKYLEIVHAQPLHRPKAQFRNLLLIVMVWITSLAISVPEMVFVQIHQTLDGVWHCYADFGGHATIWKLYLRFQLNLLGFLLPLLAMIFFYSRIGCVLVRLRPPGQGRALRMAAALVIVFFMLWFPYNLTLFLHSLLDLHVFGNCEISHRLDYTLQVTESLAFSHCCFTPVLYAFCSHRFRR... | Function: Atypical chemokine receptor that controls chemokine levels and localization via high-affinity chemokine binding that is uncoupled from classic ligand-driven signal transduction cascades, resulting instead in chemokine sequestration, degradation, or transcytosis. Also known as interceptor (internalizing recept... |
P25106 | MDLHLFDYSEPGNFSDISWPCNSSDCIVVDTVMCPNMPNKSVLLYTLSFIYIFIFVIGMIANSVVVWVNIQAKTTGYDTHCYILNLAIADLWVVLTIPVWVVSLVQHNQWPMGELTCKVTHLIFSINLFGSIFFLTCMSVDRYLSITYFTNTPSSRKKMVRRVVCILVWLLAFCVSLPDTYYLKTVTSASNNETYCRSFYPEHSIKEWLIGMELVSVVLGFAVPFSIIAVFYFLLARAISASSDQEKHSSRKIIFSYVVVFLVCWLPYHVAVLLDIFSILHYIPFTCRLEHALFTALHVTQCLSLVHCCVNPVLYSFINR... | Function: Atypical chemokine receptor that controls chemokine levels and localization via high-affinity chemokine binding that is uncoupled from classic ligand-driven signal transduction cascades, resulting instead in chemokine sequestration, degradation, or transcytosis. Also known as interceptor (internalizing recept... |
P56485 | MDVHLFDYAEPGNYSDINWPCNSSDCIVVDTVQCPTMPNKNVLLYTLSFIYIFIFVIGMIANSVVVWVNIQAKTTGYDTHCYILNLAIADLWVVITIPVWVVSLVQHNQWPMGELTCKITHLIFSINLFGSIFFLACMSVDRYLSITYFTGTSSYKKKMVRRVVCILVWLLAFFVSLPDTYYLKTVTSASNNETYCRSFYPEHSIKEWLIGMELVSVILGFAVPFTIIAIFYFLLARAMSASGDQEKHSSRKIIFSYVVVFLVCWLPYHFVVLLDIFSILHYIPFTCQLENVLFTALHVTQCLSLVHCCVNPVLYSFINR... | Function: Atypical chemokine receptor that controls chemokine levels and localization via high-affinity chemokine binding that is uncoupled from classic ligand-driven signal transduction cascades, resulting instead in chemokine sequestration, degradation, or transcytosis. Also known as interceptor (internalizing recept... |
Q9NPB9 | MALEQNQSTDYYYEENEMNGTYDYSQYELICIKEDVREFAKVFLPVFLTIVFVIGLAGNSMVVAIYAYYKKQRTKTDVYILNLAVADLLLLFTLPFWAVNAVHGWVLGKIMCKITSALYTLNFVSGMQFLACISIDRYVAVTKVPSQSGVGKPCWIICFCVWMAAILLSIPQLVFYTVNDNARCIPIFPRYLGTSMKALIQMLEICIGFVVPFLIMGVCYFITARTLMKMPNIKISRPLKVLLTVVIVFIVTQLPYNIVKFCRAIDIIYSLITSCNMSKRMDIAIQVTESIALFHSCLNPILYVFMGASFKNYVMKVAKK... | Function: Atypical chemokine receptor that controls chemokine levels and localization via high-affinity chemokine binding that is uncoupled from classic ligand-driven signal transduction cascades, resulting instead in chemokine sequestration, degradation, or transcytosis. Also known as interceptor (internalizing recept... |
A5D6U8 | MAAAPPPPPPLLLLLLCVCAVFADVPIGTQPEQVHISYPGVQNSMLVTWSSANKTDSVVEYGLWGGKLFSHSATGNSSIFINEGAEYRVMYIHRVLLTDLRPAASYVYHCGSGAGWSELFFFTALNESVFFSPGFALFGDLGNENPQSLSRLQKETQIGTYDVILHIGDFAYDLYEDNGRIGDEFMKQIQSIAAYVPYMTCPGNHEWAFNFSQYRARFSMPGDTEGLWYSWNVGPAHIISFSTEVYFYYLEYGLDLLFRQYEWLRADLQEANRPENRAERPWIITMGHRPMYCSNDDDDDCTHFQSYVRLGRNDTKPPAP... | Cofactor: Binds 1 Fe cation per subunit.
Catalytic Activity: a phosphate monoester + H2O = an alcohol + phosphate
Sequence Mass (Da): 50745
Sequence Length: 443
Subcellular Location: Secreted
EC: 3.1.3.2
|
Q6ZNF0 | MHPLPGYWSCYCLLLLFSLGVQGSLGAPSAAPEQVHLSYPGEPGSMTVTWTTWVPTRSEVQFGLQPSGPLPLRAQGTFVPFVDGGILRRKLYIHRVTLRKLLPGVQYVYRCGSAQGWSRRFRFRALKNGAHWSPRLAVFGDLGADNPKAVPRLRRDTQQGMYDAVLHVGDFAYNLDQDNARVGDRFMRLIEPVAASLPYMTCPGNHEERYNFSNYKARFSMPGDNEGLWYSWDLGPAHIISFSTEVYFFLHYGRHLVQRQFRWLESDLQKANKNRAARPWIITMGHRPMYCSNADLDDCTRHESKVRKGLQGKLYGLEDL... | Cofactor: Binds 1 Fe cation per subunit.
Catalytic Activity: a phosphate monoester + H2O = an alcohol + phosphate
Sequence Mass (Da): 50480
Sequence Length: 438
Subcellular Location: Secreted
EC: 3.1.3.2
|
Q5B2K4 | MSAEQNHGLEKDVGGPAAPAAAAPNAPAAAPGAPPAGMSAEEHRSRFGYGPLSHVNTKEAILPPFGGEFQPGLYKSVEARKFANPAPLGLSAFALTTFVLSCINMGARDITHPNIVIALAFGYGGLVQLLAGMWEMAVGNTFGATALSSYGGFWIAFAIVLTPGGFNIQTALTAENGDEAMFYNSFGLFLMGWFIFTTIMLFCTLRSTVAFFLLFLFLDLAFLLLGVGYIQRDDAGQPNPPVIKAGGFFGLLAAFAAWYNALAGIADSSNSFFIIPVAHFPWSPTGRARREKTERETV | Function: High affinity monocarboxylate transporter (MCT) involved in acetate uptake. Unlike other activities involved in acetate utilization, acpA is dispensable for growth on the acetate precursor ethanol.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31646
Sequence Length: 298
Subcellular Locati... |
Q5BLY5 | MSVIAILAMVVGVQAELKQINVIFRHGDRIPDEKNEMYPKDPYLYYDFYPLERGELTNSGKMREYQLGQFLRERYGDFLGDIYTEESVSALSSFYDRTKMSLQLVLAALYPPNKLQQWNEDLNWQPIATKYLRRYEDNIFLPEDCLLFTIELDRVLESPRGKYEFSKYDKLKKKLEEWTGKNITTPWDYYYIYHTLVAEQSYGLTLPSWTNNIFPRGELFDATVFTYNITNSTPLLKKLYGGPLLRIFTKHMLDVVSGTQKKKRKIYLFSGHESNIASVLHALQLYYPHVPEYSSSIIMELHNIEGTHYVKIVYYLGIPS... | Catalytic Activity: a phosphate monoester + H2O = an alcohol + phosphate
Sequence Mass (Da): 45389
Sequence Length: 388
Subcellular Location: Secreted
EC: 3.1.3.2
|
P80227 | MERQVLLSEPEEAAALYRGLSRQPALSAACLGPEVTTQYGGRYRTVHTEWTQRDLERMENIRFCRQYLVFHDGDSVVFAGPAGNSVETRGELLSRESPSGTMKAVLRKAGSTGEEKQFLEVWEKNRKLKSFNLSALEKHGPVYEDDCFGCLSWSHSETHLLYVAEKKRPKAESFFQTKALDISGSDDEMARPKKPDQAIKGDQFLFYEDWGENMVSKGSPVLCVLDIESGNISVLEGVPESVSPGQAFWAPGDTGVVFAGWWHEPFRLGIRFCTNRRSALYYVDLTGGNCELLSDDSLAVTSPRLSPDQCRIVYLQFPSL... | Function: This enzyme catalyzes the hydrolysis of the N-terminal peptide bond of an N-acetylated peptide to generate an N-acetylated amino acid and a peptide with a free N-terminus . It preferentially cleaves off Ac-Ala, Ac-Met and Ac-Ser (By similarity). Also, involved in the degradation of oxidized and glycated prote... |
Q97HJ4 | MRELTSEIKKEIRDIVYDFFSEECEVDINELNDNTSVVDDLDGDSLMLIELVDILKKKYSLNIQLQSIGKYLLKNPAETLEKVVQTTYLLYEYENDITNVGEK | Function: Acyl carrier protein.
PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine of the apo-ACP-like protein.
Sequence Mass (Da): 12000
Sequence Length: 103
Subcellular Location: Cytoplasm
|
A8FA63 | MIKGIGLDIVEINRLAHVLSRQPRLPERILTLNEQDIFHALSEKRQLEFLAGRFAAKEAFAKAYGTGIGRHLSFHDIEIQKDEHGKPFIKSEKTKDDQVHVSITHTKEYAAAQVLIERLSS | 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): 13757
Sequence Length: 121
Subcellular Location: Cytoplasm
EC: 2.7.8.7
|
P96618 | MIYGIGLDITELKRIASMAGRQKRFAERILTRSELDQYYELSEKRKNEFLAGRFAAKEAFSKAFGTGIGRQLSFQDIEIRKDQNGKPYIICTKLSQAAVHVSITHTKEYAAAQVVIERLSS | Function: Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of fatty acid acyl-carrier-protein ACP. Also modifies the D-alanyl carrier protein but fails to recognize PCP and AcpK, an acyl carrier protein of secondary metabolism.
Catalytic Activity: apo-[ACP] + CoA = adenosine 3',5'-bisphosphate + H(+)... |
A7Z1L9 | MIFGIGIDIVELHRIENMLSRQARFPQRILTEAEYARFTLLSDKRKIEFLAGRFAAKEAFSKAYGTGIGKELSFQDIETGNDKAGKPVLACAKLDCATVHVSITHTKEYAAAQVVIERLSR | 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): 13503
Sequence Length: 121
Subcellular Location: Cytoplasm
EC: 2.7.8.7
|
B8DVV4 | MLGLGHDVVDVGAFAEQLEMPGTRMTRLFSARECRQASLRASIKHDGEALHLAAKWAAKESVVKAWCEALVGRGITERPYTVDDTPWSRIEIVDDATGCPRVVMAAEVHVELCRSLAVTESAEPVWHVSISHDGGIASAVAVLDMRE | 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): 15978
Sequence Length: 147
Subcellular Location: Cytoplasm
EC: 2.7.8.7
|
A1A005 | MLGLGHDVVDVPAFAKQLNEPGTRMRNLFSMREIWQTAQRSQLKHDDEAVHLAARWAGKEAFLKAWCAAISRHAKDGAEVAYPYTLDNFPWVRIEILDDSHGVPRVILSSEVQRKVQQSLGLPLDPVCQSYDISISISHDGPIASAVVMLEI | 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): 16959
Sequence Length: 152
Subcellular Location: Cytoplasm
EC: 2.7.8.7
|
O51043 | MKSIGCDIIKVERFKNFLENKKKMERFFTHKEIENFKLKGGSIIESLAGKFAAKESLIKALSPLLQYKINYTLKDIEVIKSLKGNAEFCLHNEVEKFAIKMNLKLYLTISHEKEYAIAFVIVEN | 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): 14376
Sequence Length: 124
Subcellular Location: Cytoplasm
EC: 2.7.8.7
|
Q7NE72 | MAGQTFLHRIGTDLVHIPRIEGMLERYGKQFLNRVYTEGEQHYCLASKPHRANRLAGRWAAKEAVTKALGTGWRGVGYRDIEVVRLASGEPTICLNGRAVLLVERFGRLDWQVSFSHDREYAVATVSVIGFF | 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): 14919
Sequence Length: 132
Subcellular Location: Cytoplasm
EC: 2.7.8.7
|
Q0BTG4 | MIIGIGSDICDIRRIETVLERHGERFLSRVFTTAERAKAERRNGRMRMGTYAKRFAAKEACAKALGTGFAGGVFMSDLGVVNLSSGQPTLRLTGGAAARLSAMTPSGMGAQVLLTMTDEYPYAYAQVVISAVPLPTSLIGGRGLP | 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): 15398
Sequence Length: 145
Subcellular Location: Cytoplasm
EC: 2.7.8.7
|
Q9KFG1 | MIIGTGIDIVELERIQSMVEKHPRFVKKILTENEQEVFARLSRRRRLEYIAGRFAAKEAFVKAVGTGISAEYGWHDLEVLSDERGKPVLSVNLDATIHVSISHSQSYAIAQVILERLSS | 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): 13421
Sequence Length: 119
Subcellular Location: Cytoplasm
EC: 2.7.8.7
|
A1WT13 | MIAGIGTDIVAVVRLERALERHGERFAQRILAPTELLNFREGGATAAFLARRFAAKEAASKALGTGFSDGVTLRDLEVVHDVRGQPSLRFHGAAAERAVALGVSEAALSLSDEREYAVAFVILVTG | 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): 13389
Sequence Length: 126
Subcellular Location: Cytoplasm
EC: 2.7.8.7
|
B8D0V9 | MIRGIGIDIVEVNRISDMVDKWGERFLNKVYTPYEVNYCKFKSNTYECLAGRFAAKEAFVKMLGTGFKHIYFKDIEVRSDEKGKPYLRIKGNADRLTKESGIKRIHLSISHERKFAIAFVVGEEG | 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): 14429
Sequence Length: 125
Subcellular Location: Cytoplasm
EC: 2.7.8.7
|
O25488 | MIGIDIVSIARIEKCVKRFKMKFLERFLSPSEIVLCKDKSSSIAGFFALKEACSKALQVGIGKELSFLDIKISKSPKNAPLITLSKEKMDYFNIQSLSASISHDAGFAIAVVVVSSSNE | 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): 13004
Sequence Length: 119
Subcellular Location: Cytoplasm
EC: 2.7.8.7
|
A9B2B6 | MLVTGVDLIEIDRINQAVSRWGQRFARRVWTEAEWLRCRDSAQSLAARWAAKEAAAKALGVGLKGIGHPACAVAWREIEVANDTQGKPLLRLHGAAQQRANELGIRHWSVSLSHSGDQAIAFVVGMG | 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): 13865
Sequence Length: 127
Subcellular Location: Cytoplasm
EC: 2.7.8.7
|
Q31HN9 | MIVGIGTDLVEIARIAALMTKRNEVFAKRILAQQELERFKQHGQPEKFLAKRWAAKEAISKALGTGFTQGVCFTDMIIGHTDQGQPLIELTGKTAEIAQQLGIENWSISISDEAHYAVAFVIAESRS | 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): 14000
Sequence Length: 127
Subcellular Location: Cytoplasm
EC: 2.7.8.7
|
B4U7U7 | MLGIDIIKNIRIAKALERFGYHFLNRVYTEYEINLCKMNVECLSGRFAAKEASIKAFSFLSIRRFSFRDFEVVKSKNGIPELRIKDAYINDFLKAQKLKPFISISHEKEFSVAVCYITKEERIC | 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): 14526
Sequence Length: 124
Subcellular Location: Cytoplasm
EC: 2.7.8.7
|
G2TRL9 | MGLGIDILKISRISRLIQRSPEWEKNFLKKCLCENEIKKYNLIKSNSSLPRLSEQAKWLAVRWCVKEAVFKALQPNFRVYMSMMEYVRTPTGYPSVVIHDPRFPLSPVMVSVSHEEDLVVANALYLPSMPKT | 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): 15271
Sequence Length: 132
EC: 2.7.8.7
|
Q12KI5 | MAIIGIGTDIVEIERIREQRDRLGDKLAKRVLTLDELAIYAAVNMPERYLAKRFAAKEAAAKALGTGIGRGVSFQHIHISNDDNGAPLVNFTDGAALRLAQLGGCKGHISIADEKHYAIATVILES | 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): 13581
Sequence Length: 126
Subcellular Location: Cytoplasm
EC: 2.7.8.7
|
Q8EH77 | MAIVGLGTDIVEIERISAHVARSGDKLAKRVLTEAEFEIYQQHSQPSRYLAKRFAAKEAAAKALGTGIGRGVSFQHIHIGNTPDGAPTIDFTEGAQQRLTLLNGVVGHISIADEKSYAIATVILESR | 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): 13639
Sequence Length: 127
Subcellular Location: Cytoplasm
EC: 2.7.8.7
|
P80643 | MADTLERVTKIIVDRLGVDEADVKLEASFKEDLGADSLDVVELVMELEDEFDMEISDEDAEKIATVGDAVNYIQNQQ | 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... |
A1US60 | MSDTEERVKKIIVEHLGVDADKVVQNASFIDDLGADSLDTVELVMAFEEEFGIEIPDDAAETIFTVNDAVKFIDKASS | 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... |
Q7V9R0 | MSQEAILEKVRSIVAEQLSVEASEIKPDSNFQNDLGADSLDTVELVMALEEAFDIEIPDEAAEGITTVGDAVKYIEDKQS | 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... |
P80923 | MSTIEERVKKIVAEQLGVKSEEVVNTASFVEDLGADSLDTVELVMALEEEFETEIPDEEAEKITTVQAAIDYVNSHQA | 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... |
Q8NEB7 | MRKPAAGFLPSLLKVLLLPLAPAAAQDSTQASTPGSPLSPTEYERFFALLTPTWKAETTCRLRATHGCRNPTLVQLDQYENHGLVPDGAVCSNLPYASWFESFCQFTHYRCSNHVYYAKRVLCSQPVSILSPNTLKEIEASAEVSPTTMTSPISPHFTVTERQTFQPWPERLSNNVEELLQSSLSLGGQEQAPEHKQEQGVEHRQEPTQEHKQEEGQKQEEQEEEQEEEGKQEEGQGTKEGREAVSQLQTDSEPKFHSESLSSNPSSFAPRVREVESTPMIMENIQELIRSAQEIDEMNEIYDENSYWRNQNPGSLLQLP... | Function: Acrosomal protein that maintains proacrosin (pro-ACR) as an enzymatically inactive zymogen in the acrosome. Involved also in the acrosome formation.
PTM: Phosphorylated on Tyr residues in capacitated sperm.
Sequence Mass (Da): 61359
Sequence Length: 543
Subcellular Location: Secreted
|
Q3V140 | MMNLAAGFLLMLLEVLLLPGTPLSAEESPASTPGSPLSSTEYERFFALLTPTWKAETTCRLRATHGCRNPTLVQLDQYENHGLVPDGAVCSDLPYASWFESFCQFAQYRCSNHVYYAKRVRCSQPVSILSPNTLKEVESSAEVPPTSMTTPIVSHATATEHQAFQPWPERLNNNVEELLQSSLSLGGKDQQSSRRPGQEQRKQEQIQEHKLEEAQEQEEQEEEEEEEEAKQEEGQGTEAGLESVSRLQSDSEPKFQSQSLSSNPSFFTPRVREVESAPLMMKNIQELIRSAQEMDEMNELYDDSWRSQSTGSLQQLPHME... | Function: Acrosomal protein that maintains proacrosin (pro-ACR) as an enzymatically inactive zymogen in the acrosome. Involved also in the acrosome formation.
PTM: The N-terminus is blocked.
Sequence Mass (Da): 61141
Sequence Length: 540
Subcellular Location: Cytoplasmic vesicle
|
Q876Q0 | MPRSSATARKSHSNRQDHGGGGSGKKPSKQKSSGHLNATYNGTAGSETGPSSQVDWPSHRSGDQSIAAAAAKSNGPVDSLKADTNGRGYPGGYAKGNADMSYGQTNGGVSPNGGLAGPASRRTDKSVTGTKRTTSNASVNPFQLASTILRSCPMYDTIAILIFLLQLPPMVLTLVQFLFASLTFMPPSGTASGSFTSNFDIFQGPAGTPSLGTMIAMDGFCLLVWGLFMWTWAQNFALDLAHVQVAITLGGGGAGKNGGVNALCVGIVLILHLIRSKGIQDFVVGHLVSAKIISPDLLSHYSYLMPAEFKRTESQSSPSW... | Function: component of the regulatory network controlling carbon source utilization through ubiquitination and deubiquitination involving creA, creB, creC, creD and acrB. Involved in resistance to acriflavine, and required for normal growth on a range of sole carbon sources, including fructose, cellobiose, raffinose, a... |
Q9X928 | MSNESLANLLKEERRFAPPADLAANANVTAEAYEQAKADRLGFWAEQARRLTWAKEPTETLDWSNPPFAKWFKDGTLNVAYNCVDRHVEAGNGDRVAIHFEGESGDSRALTYAQLKDEVSKAANALLELGVQKGDRVAIYMPMIPETAIAMLACARIGAAHSVVFGGFSSDALATRIQDADARVVITADGGYRRGKPSALKPAVDEAVERAGIVEHVLVVRRTGQDVAWDDSRDKWWHETVDGQSAEHTPEAFDAEHPLFILYTSGTTGKPKGILHTSGGYLTQTAYTHWAVFDLKPETDVFWCTADVGWVTGHSYIVYG... | 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, ... |
Q55404 | MSDTIESILQEERLFDPPTEFSERAYVRSGREYEQLYSRAASNPEKFWGELAEQELHWFKKWDQVLDWQPPFAKWFVGGQLNISHNCLDRHLTTWRRNKAAIIWEGEPGDSRIITYAQLHREVCQFANALKSLGVQKGDRVAIYLPMIPEAAITMLACSRIGAPHSVVFGGFSAEALRDRLVDAEAKLVITADGGFRKDKAIALKQEVDKALEHGAPSVENVIVVQRTKADVTMTAGRDHWWHELQPQQSAHCPAEPIDSEDMLFILYTSGSTGKPKGVVHTTGGYNLYTHMTTKWIFDLKDTDVYWCTADVGWITGHSY... | 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, ... |
Q5SIW6 | MDRLESVLKEERVFYPSEEFRKQAHIKSEEEYQRLYEESVRDPEGFWGRVASELHWFEPWRKVLEGDLPHPKWFVGGKTNLSYNALDRHVKTWRRNKAAIVWEGEPGEERVLTYHDLWREVQRFANVLKRLGVKKGDRVTIYLPMIPEAAIAMLACTRIGAVHSVVFGGFSAGALADRIKDAEAKVLITADGGFRRGGIVPLKQNADEALKDATSVEHVVVVRRTGEEVPWTPGRDHWWHELMEAAPDRCDPEPMEAEEPLFILYTSGSTGKPKGVLHTTGGYMTYVYYTTKLVFDLKDEDVYWCTADVGWITGHSYVVY... | 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, ... |
Q9Y896 | MDDEIQAVVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHHGVMVGLSNKDSYVGDEAQAKRGVLTLKYPIEHGTVTNWDDMEKIWHHTYYNELRVAPEEHPVLLTEAPLNPKTNREKMTQIMFETFNVPAFHVSIQAVLSLYASGRTTGIVLDSGDGVTHTVPIYEGFSLPHAIQRLDLAGRDLTERLVLHLTERGYTFTTSAEKEVVRDIKERLCYVALDFDQELITAAQSSALEKNYELPDGQIITIGNERFRAPEVFFQPSFAGMESGGIADLVYTSIQRCDLDIRRELYGNIVMSGGTTMFPGISDRMQRELSNM... | 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): 41794
Sequence Length: 375
Subcellular Location: Cytoplasm
EC: 3.6.4.-
|
Q96483 | AGFAGDDAPRAVFPSIVGRPRHTGVMVGMGQKDAYDGDEAQSKRGILTLKYPIEHGIVSNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDNLMKILTERGYMFTTTAEREIVRDMKEKLAYVALDYEQEIETARSSSSIEKNYELPDGQVITIGAERFGCPEVLFQPSMIGMEAAGIHETTYNSIMKCDVDIRKDLYGNIVLSGGSTMFPGIADRMSKEITALAPSSMKIKVVAPPERKYS... | 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... |
P93374 | AGFAGDDAPRAVFPSIVGRPRYTGVMVGMGQKDAYVGDEAQSKRGILTLKYPIEHGIVSNWDDMEKIWHHTFYNELRVAPEEHPLLLTEAPLNPKANREKMTEIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTAAEREIVRDLKEKLAYVSLVFEQELETSKNSKDVEKSYELPDGQIITIGAERFRCPEVLFQPSFIGMEAVGIHETTYNSIMKCDVDIRKDLYGNVVLSGGSTMFPGITDRMSKEISALAPNSMKIKVVAPPERKYS... | 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... |
P20399 | MCDDEETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVLSGGTTMYPGIADRMQKEIT... | Function: Actins are highly conserved proteins that are involved in various types of cell motility.
PTM: Oxidation of Met-46 and Met-49 by MICALs (mical1, mical2 or mical3) to form methionine sulfoxide promotes actin filament depolymerization. Mical1 and mical2 produce the (R)-S-oxide form. The (R)-S-oxide form is reve... |
P18602 | QKDSYVGDEAQSKRGILTLKYPIEHGVVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYTFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSTSLEKSYELPDGQIITIGNERFRCPEALFQPSFLGMETCGIHETAYNSIMKCDVDIRKDLYANTVLSGGTTMFPGIADRMQKEITMLAPSSMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPS... | 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): 36891
Sequence Length: 327
Subcellular Location: Cytoplasm
EC: 3.6.4.-
|
P45886 | MCDDEVAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAAASTSLEKSYELPDGQVITIGNERFRCPESLFQPSFLGMESSGIHETVYNSIMKCDVDIRKDLYANIVMSGGTTMYPGIADRMQKEITA... | Function: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
PTM: Oxidation of Met-45 to form methionine sulfoxide promotes actin filament depolymerization. Methionine sulfoxide is produced stereospecifically, but it is not kn... |
Q8BFZ3 | MVDDELTALVVDNGSGMCKAGFGGDDAPRAVFPSMVGRPRHQGVMVGMGQKDCYVGDEAQSKRGILTLKYPIEHGVVTNWDDMEKIWYHTFYNELRVAPDEHPILLTEAPLNPKINREKMTQIMFEAFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYNFTTTAEREIVRDVKEKLCYVALDFEQEMVTAAASSSLERSYELPDGQVITIGNERFRCPEAIFQPSFLGIESRGIHETTFNSIMKCDVDIRKDLFANTVLSGGSTMYPGIADRMQKEIVT... | Function: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
PTM: Oxidation of Met-45 and Met-48 by MICALs (MICAL1, MICAL2 or MICAL3) to form methionine sulfoxide promotes actin filament depolymerization. MICAL1 and MICAL2 pro... |
P84856 | MCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVYNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANLEKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERYGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYELPDGQVITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPE... | Function: Actin is a highly conserved protein that polymerizes to produce filaments that form cross-linked networks in the cytoplasm of cells. Actin exists in both monomeric (G-actin) and polymeric (F-actin) forms, both forms playing key functions, such as cell motility and contraction. In addition to their role in the... |
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