ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
A1CLG4 | MHPSTFVTTIACLAGLAHGYANPGSCSGACNIHDPALIRRQSDGKYFRFSTGNKISYASSSSIKGPWTVLGSVLPRGSSINLPGKTDLWAPDISLVNGAYHLYYSVSAFGSQDSAIGLATSATMDPNSWTDHGSTGIRSSSSKPYNAIDANLFHDGGNYYMTFGSFWHDIYQAPMNSAATAVSSGPYNIAYNPSGTHAVEGAFMYKFGKYYYLFFSSGICCGYDTSRPAAGKEYKIRVCRSTSATGHFVDKHGVSCTNGGGTVVLESHGHVYGPGGQGVFTDPALGPVLYYHYVDTRIGYADGQKRFGWNKIDFSSGWPV... | Function: Endo-1,5-alpha-L-arabinanase involved in degradation of pectin. Its preferred substrate is linear 1,5-alpha-L-arabinan (By similarity).
Catalytic Activity: Endohydrolysis of (1->5)-alpha-arabinofuranosidic linkages in (1->5)-arabinans.
Sequence Mass (Da): 34386
Sequence Length: 321
Pathway: Glycan metabolism;... |
Q5BA96 | MYLPTLAASASLLVGVAHGYASPGACSGACNIHDPALIRRESDGKYFRFSTGNKISYASASSIEGPWTAIGSVLPGGSSIDLDGNDDLWAPDVQLVNGVYYVLYSVSTFGSQNSAIGLATSDTMDLNTWTDHGSTGIRSDSSKPYNAIDGNLFQDDSGTWYMNFGSFWNDIYQAQMKSPPTAVASSSYQIAYQPAGEHAVEGAYLYKYGNYYYLFFSEGKCCGYDSSRPATGEEYKIKVCRSTTATGNFVDANGVSCTSGGGTIVLESHDNVYGPGGQGVFTDPTLGPVLYYHYVDTTIGYADSQKLFGWNVLDFSSGWP... | Function: Endo-1,5-alpha-L-arabinanase involved in degradation of pectin. Its preferred substrate is linear 1,5-alpha-L-arabinan (By similarity).
Catalytic Activity: Endohydrolysis of (1->5)-alpha-arabinofuranosidic linkages in (1->5)-arabinans.
Sequence Mass (Da): 34488
Sequence Length: 322
Pathway: Glycan metabolism;... |
B8N803 | MVLVATLFSLFTVSLCRSIPRSSPSSSPYTQATDLKIHDPTVINANGAYYAYGVGEHIVIHQAPGLAGPWKQIGSVLDKDSIIPKGDRAKPWAPTTIEVKGTFYCYYSVSNAGCRDSAIGVATSQSPGPGGWTDHGAIVQSGTGQGSDEHPFNEVNAIDPAVLVTGDKGHLVFGSYWSGIWQVPLNEDFSSVGNTTGLNAHHLAKHPKTERVNSQDQNPDPLCRDSSGRRPVEGAYISYHAPYYYLWLSWGQCCDYDPNNLPPSGEEYSIRVGRSESPHGPFVDKQGKELTQGGGELIYGSNNDVYAPGGQGVITVETGD... | Function: Endo-1,5-alpha-L-arabinanase involved in degradation of pectin. Its preferred substrate is linear 1,5-alpha-L-arabinan (By similarity).
Catalytic Activity: Endohydrolysis of (1->5)-alpha-arabinofuranosidic linkages in (1->5)-arabinans.
Sequence Mass (Da): 38848
Sequence Length: 358
Pathway: Glycan metabolism;... |
Q8AVG0 | MEPVSHQDMPRLSWIDTLYSNFNYGTDGYDAEGNEEHKNSREGSETMPYIDESPTMSPQLSARSQDSVDGVSPTPTEVLLPGGESESDKGLLMRKLVLSGVLASEEIYINQLEALLLPMKPLKATASTSQPVLTLQQINDIFYKIEDIYQMHKDFYDKLCPIVQQWDNKTTVGHLFQKLATQLGVYKAFVDNYKFALETAEKCSQCNVQFFKISEDLKVKGPKDSKEQPQSVTMEALLYKPIDRVTRSTLVLHDLLKHTPTDHPDYPLLQDALRISQNFLSSINEDIDPRRTAVTTPKGEPRQLVKDGFLVELSENSRKL... | Function: Protein with a unique structure having two opposing regulatory activities toward small GTP-binding proteins. The C-terminus is a GTPase-activating protein domain which stimulates GTP hydrolysis by RAC1, RAC2 and CDC42. Accelerates the intrinsic rate of GTP hydrolysis of RAC1 or CDC42, leading to down-regulati... |
A4II46 | MEPVSHQGMPRLSWIDTLYSNFNYGTDGYDAEGNEEHKSSREGSETMPYIDESPTMSPQLSARSQDSVDGVSPTPTEVLLPGGESESDKGLLMRKLVLSGVLASEEIYINQLEALLLPMKPLKATASTSQPVLTLQQINDIFYKIEDIYQMHKDFYDKLCPIVLQFDNKTTVGHLFQKLASQLGVYKAFVDNYKFALETAEKCSQCNVQFFKISEDLKVKGPKDSKEQPQSVTMEALLYKPIDRVTRSTLVLHDLLKHTPTDHPDYPLLQDALRISQNFLSSINEDIDPRRTAVTTPKGEPRQLVKDGFLVELSENSRKL... | Function: Protein with a unique structure having two opposing regulatory activities toward small GTP-binding proteins. The C-terminus is a GTPase-activating protein domain which stimulates GTP hydrolysis by RAC1, RAC2 and CDC42. Accelerates the intrinsic rate of GTP hydrolysis of RAC1 or CDC42, leading to down-regulati... |
Q9RBG5 | MSRSAAEFLKPQNVASTHYLDNRVYWDHEIFEEEKKRIFSKVWKFVCHVSEIPSTFDYRTIKVADTPLVVIRGKDEKVRTFVNACSHRGIQIVRRPRGNAKTMECIFHRWNYDSTNGELTGAPRKEAYGPSNFDLKQCGLREVRTETYLGLVFVNLDDSAVSLSEFIGDALEMEKDILGAEELEVFDYYEQVLDTNWKNWQETNLDLYHEFMHFANRKTGLTVKEYYQRAWKLYPNGHAAIERYRAQYSNYAGWQDRDDGIRLPGLHPNEFQLVNLFPDLAINARGTVIRIDSQTPISPGKTLVQYRGLGLKRDSERERV... | Cofactor: Binds 1 [2Fe-2S] cluster per subunit.
Function: Alpha subunit of the oxygenase component of the 2-aminobenzenesulfonate 2,3-dioxygenase system (deaminating) (ABSDOS). Can use 2-aminobenzenesulfonate (ABS), benzenesulfonate (BS), 4-toluenesulfonate (TS), 2-nitrobenzenesulfonate, 3- and 4-aminobenzenesulfonates... |
Q9RBG4 | MDTVSIAEFLYTNADLLNQEQFDSWLEQCSNDFSYRITTFSEELGRPMDWMDKDKSGLAHYLQNANNHERYTGRLRRHLAMPRVTKQADSSFEVRTAVAIYVIEMNGETALYGIGSYVDNVMSESSGLRLTSRVVTLDTRRLQFGPHVPI | Function: Beta subunit of the oxygenase component of the 2-aminobenzenesulfonate 2,3-dioxygenase system (deaminating) (ABSDOS). Can use 2-aminobenzenesulfonate (ABS), benzenesulfonate (BS), 4-toluenesulfonate (TS), 2-nitrobenzenesulfonate, 3- and 4-aminobenzenesulfonates, 4-chloro- and 4-hydroxybenzenesulfonates and py... |
A0A009IHW8 | MSLEQKKGADIISKILQIQNSIGKTTSPSTLKTKLSEISRKEQENARIQSKLSDLQKKKIDIDNKLLKEKQNLIKEEILERKKLEVLTKKQQKDEIEHQKKLKREIDAIKASTQYITDVSISSYNNTIPETEPEYDLFISHASEDKEDFVRPLAETLQQLGVNVWYDEFTLKVGDSLRQKIDSGLRNSKYGTVVLSTDFIKKDWTNYELDGLVAREMNGHKMILPIWHKITKNDVLDYSPNLADKVALNTSVNSIEEIAHQLADVILNR | Function: NAD(+) hydrolase (NADase) that catalyzes cleavage of NAD(+) into ADP-D-ribose (ADPR) and nicotinamide . In addition to ADPR, also generates a cyclization variant of cyclic ADPR (cADPR), termed 2'cADPR (v-cADPR) . Cleaves NADP(+), but does not cyclize the product .
Catalytic Activity: NAD(+) = 2'cADPR + H(+) +... |
Q502L1 | MEGDSNPLYEQRFNAAVKVIQNLPPNGSFQPSHDMMLKFYSYYKQATQGPCNIPRPGFWDPVGKAKWDAWSSLGEMPKEEAMAAYVDDLKLILESMPVSSEVEELLQVIGPFYELVDEKRKITQVSDLSTGFGNLLSSPPKCVTKSIIRTMEMNGNLEGYPIKTAETLKVKSIDLEDREDDDDEDEEGERDEVEEFKEVEKASQPKKRVSAGRPKGPVSNGSISQHKGLSNGTHGSKSDLNRQESEENTEHMNHDGGIVELNGHLNSEKDKEEDVSSSHHVASDSDSEVYCDSVDQFGGEDGSEIHMNRSLEVLEESHST... | Function: Acyl-CoA binding protein which acts as the peroxisome receptor for pexophagy but is dispensable for aggrephagy and nonselective autophagy. Binds medium- and long-chain acyl-CoA esters (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 55489
Sequence Length: 501
Subcellular Lo... |
A5WV69 | MILRGMEDSKSAQKRFEAAVKVIRSLPEDGSYDLSDDMLVLFYSYYKQATEGPCNTLKPNSWDPIGKAKWEAWKDLGNMSKDQAMTEYVQEIQLIIETLPVTDRMAELLDALDPFYEIVEDDDDDDDEGVSKAAPLFTGSTNADKDAERDEEVESESKEGNLDDYMELVEKQKDLSSTTGEKGSLLVFNRSEENSISSLTDGTHSSLNTVDDEEELVYDGSDDEMDSDSMDKPATPEKGSGVRSVRLADGSVVGANMQHGGNREPQCGSQDGKPQGLISPVPHPPTLGTVRNDRISACSGRERGCQGDGGQRGETADRMD... | Function: Binds medium- and long-chain acyl-CoA esters.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 45788
Sequence Length: 410
Subcellular Location: Membrane
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Q9ZAE9 | MSGVETVGVHADAHRDSWQVRAQKQITYEVRFRDDVFGLDSTDLLEAGADGAGSRRRFVVVDSAVDALYGSRIREYFTHHGIDHSILVMRVGETVKDFDTAGRIVAAMDAFGLARRREPMIVVGGGVLMDVAGLVASLYRRGTPFLRVPTTLVGLIDAGVGAKTGVNFNGHKNRLGTYAPADLTLLDRRFLATLDRRHLSNGLAEMLKIALIKDAELFQLLERHGRVLIEERFQGRTGTGDRAAVRALRAATHGMLEELGPNLWESRLERSVDYGHTFSPTIEMRALPALLHGEAVCVDMALTTVLAYRRGLLDVAQRDR... | Cofactor: Divalent metal cation such as Co(2+).
Function: Catalyzes the cyclization of D-sedoheptulose 7-phosphate to 2-epi-5-epi-valiolone. Does not use ido-heptulose 7-phosphate and 3-deoxy-arabino-heptulosonate 7-phosphate. Involved in the biosynthesis of the acarviose moiety of the alpha-glucosidase inhibitor acarb... |
Q5ZHQ6 | MAETGSVHATRFEAAVKVIQSLPKNGSFQPTNEMMLKFYSFYKQATQGPCNIPRPGFWDPIGRYKWDAWSALGDMSKEEAMIAYVEEMKKILESMPMTDKVEELLQVIGPFYEIVEDKKNRGSGLTSDLSNVMNSTPNIKAVNGKAESSDSGAESEEEGLREEEEKELQQNVKDCKSPKTESLAAKDLENSVANDCYKDSFIPDMQNGIQTKSALNGLNVEEEIKKTEPSLEIANNCDHRGANEENTEEVSGTQHLTSDSDSEVYCDSMEQLGLEEPLEIITSAKGSLKRSSHFLDVDHRLQLENTDLPRHACTTAGNLQ... | Function: Acyl-CoA binding protein which acts as the peroxisome receptor for pexophagy but is dispensable for aggrephagy and nonselective autophagy. Binds medium- and long-chain acyl-CoA esters (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 54455
Sequence Length: 492
Subcellular Lo... |
Q5T8D3 | MFQFHAGSWESWCCCCLIPADRPWDRGQHWQLEMADTRSVHETRFEAAVKVIQSLPKNGSFQPTNEMMLKFYSFYKQATEGPCKLSRPGFWDPIGRYKWDAWSSLGDMTKEEAMIAYVEEMKKIIETMPMTEKVEELLRVIGPFYEIVEDKKSGRSSDITSVRLEKISKCLEDLGNVLTSTPNAKTVNGKAESSDSGAESEEEEAQEEVKGAEQSDNDKKMMKKSADHKNLEVIVTNGYDKDGFVQDIQNDIHASSSLNGRSTEEVKPIDENLGQTGKSAVCIHQDINDDHVEDVTGIQHLTSDSDSEVYCDSMEQFGQE... | Function: Acyl-CoA binding protein which acts as the peroxisome receptor for pexophagy but is dispensable for aggrephagy and nonselective autophagy. Binds medium- and long-chain acyl-CoA esters.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 60092
Sequence Length: 534
Subcellular Location: Peroxiso... |
Q5XG73 | MLFLAFHAGSWGSWCCCCCVITADRPWDRGRRWQLEMADTPSVYETRFEAAVKVIQSLPKNGSFQPTNEMMLKFYSFYKQATEGPCKLSRPGFWDPIGRYKWDAWSSLGDMTKEEAMIAYVEEMKKIIETMPMTEKVEELLHVIGPFYEIVEDKKSSKSSDLTSDLGNVLTSSNAKAVNGKAESSDSGAESEEEEAQEELKGAEQSGSDDKKTLKKSADKNLEIIVTNGYKGSFVQDIQSDIHTDSSRSTRSSEDEKPGDESSQQTGHTIVCAHQDRNEDPSEDASGIHHLTSDSDSEVYCDSMEQFGQEEYYLGGDPTQ... | Function: Acyl-CoA binding protein which acts as the peroxisome receptor for pexophagy but is dispensable for aggrephagy and nonselective autophagy. Binds medium- and long-chain acyl-CoA esters (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 56614
Sequence Length: 508
Subcellular Lo... |
Q5WEF5 | MSSEQEFEKPVIELRQKIADLRAFAMERDMDLSTEIKKMEARLSELEEEVYANLQPWERVQIARDHERPTTLDYVDVLFEDFLEMHGDRLFGDDKAIVGGIATYKGKPVTVIGHQRGKDTKENIVRYFGSPHPEGYRKALRLMKQAEKFKRPIICFIDTKGAYPGKAAEERGQSEAIARNLLEMAGLKVPTISIVIGEGGSGGALALGVADEIHMLENATYSVISPEGAAAILWKDAGKAKKAAESMRITAPDLYELGIIDSIIPEPRGGAQRNLHQQADEIDRLLEKALTRLAEKPVDVLLDERYEKFMKIGHIPEEAA... | 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... |
O67260 | MILFKVMHLEFEKELLEIKEKIDRLLGLYRLGKEEVLSELDELRKKFKEKARKIYRDLSPWERVQVARHPKRPHTSDYIKYLIKDFEEVHGDTCYGDDKAVIAGFGYFRGKPVAVVGHEKGKDTKEKLERNFGMPHPEGYRKAIKVFKLAERYNIPVITFIDTPGAFPGIGAEERGQSRAIAESMLTMAFLKVPSVAVVIGEGGSGGALAFGVANRVCILENAYYSVISPEGCAAILWKDQSKVKEAAKALRLTAKDLKELGVVDCVIPEPYGAAHWSPRGTAMMVGMTLKKCLDELSKLTEEGVVRSRLEKFKNMGAFK... | 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... |
Q9LD43 | MASISHSSLALGGASSASASDYLRSSSNGVNGVPLKTLGRAVFTTIRRKDLAVTSRLKKGKKFEHPWPANPDPNVKGGVLSYLAEFKPLGDTQKPVTLDFEKPLVELEKKIVDVRKMANETGLDFTEQIITLENKYRQALKDLYTHLTPIQRVNIARHPNRPTFLDHIHNITDKFMELHGDRAGYDDPAIVTGIGTIDGKRYMFIGHQKGRNTKENIMRNFGMPTPHGYRKALRMMYYADHHGFPIVTFIDTPGAYADLKSEELGQGEAIANNLRTMFGLKVPILSIVIGEGGSGGALAIGCANKMLMLENAVFYVASPE... | 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 (By similarity).
Catalytic Activity: acetyl-CoA + N(6... |
Q8KG09 | MAAKVVLDFEKPLYELEEKLNEMRVYLKSGEVDSMSEGRAGLKREIESLEAKVESLRKTIYKNLTRWQKVQLARHPERPYTLDYIYMMMKDFVELSGDRNFGDDKAIIGGFARLEDESAGFSQSVMVIGHQKGRDTKSNLYRNFGMAQPEGYRKALRLMKLAEKFRKPVITLIDTPGAFPGIEAEERGQAEAIARNLYEMAALKVPVICVIIGEGASGGAIGIGVGDRILMAENAWYSVISPESCSSILWRSWNFKEQAAEALKLTADDLLAQGIIDRIVTEPLGGAHHNPEQMASTLKSILIEELQGLLTKDARTLVDE... | 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... |
Q97DB2 | MENSQELTPWQRLTIARMLERPTSLEYIDLIFDSFMEFHGDRAFGDDAAIVGGVAEFNGMPVTVIGQQKGRNTNENIKRNFGMPSPEGYRKALRLMKQAEKFNRPLICFVDTSGAYCGVEAEQRGQGEAIAKNLISMANLKIPVISVVIGEGGSGGALAMAVADEVWMLENSVYSLLSPEGFASILWKDSSRAKEAAEVMKITADDLKGYGIIDKVIKEPDGGAQNDITMVANALRENLKKAIEGLSSTGINELLDNRYNKFRQIGKFIENEDN | 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... |
B2THL2 | MNKEFIKSIVVSSPWEKVEIARHKDRPTGKYYIDNIFKDFIEFHGDRLFGDDKAVIGGIASFEDISVTVIAITKGANTNENIERNFGMPNPEGYRKALRLMKQAEKFNRPVICFIDTPGAFCGVGAEERGQGSAIANNLFELSRLKTPIISIVIGEGGSGGALALTVADKILMLENAVYSILSPEGFASILWKDSKRVKEAANVMKITAQDLNEFGIIDTVIKEPRGGAHKNPQKQVTLIKKELMNAMNEMKNIETNQMINERYDKFRKIGTLE | 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... |
A0KLN6 | MSWLEKILPKSKITTPRRHNIPEGVWTKCSACEQVLYRAELERNLEVCPKCDHHMRISARARLESFLDEQGRTEIGAELEPQDVLKFKDSKRYKDRLSAAQKETGEKDALVVMKGTLKGVPVVACSFEFSFIGGSMSSVVGARFVRAVEESIKEGRGLVCFSTSGGARMQEALFSLMQMAKTSAALDRLSKAGLPYISVLTDPTMGGVSASLAMLGDINVGEPKALIGFAGPRVIEQTVREKLPEGFQRSEFLLEKGAIDLIIDRREMRNRLASLLAKMLNTHVIEE | 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... |
B6JCP4 | MNWLNNVVRPKIRSILKRETPENLWIKCPDSGQLVFYKDVEANQFVIPGSNYHMRMGATARLKSIFDNETWFDVALPDVAADPLKFRDERRYADRIKDARAKTGMNDAVKVGYGRIESTPAVVAVQDFDFMGGSLGMAAGEAIVTGLQLAVEKHAPFIMFAASGGARMQEGILSLMQMPRTTVAIQLLREAGLPYIVVLTNPTTGGVTASYAMLGDVQLAEPGALIGFAGARVIEQTIREKLPEGFQRAEYLKEHGMVDMVVHRHEMRPTLARLCRLLMKVPAPHADEVAAPPPPDVEGPPPAAEPVALPPA | Function: Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA.
Catalytic Activity: acetyl-CoA + N(6)-carboxybiotinyl-L-l... |
A0ZZ44 | MEKSWFNLILSKGELEYRCGLSKSMDSRLGPVENTTVNEDPTRNDTDKNIHDCSDSSSYYSKVDHLVDVKDIRNFISDDTFLIRDSNQDRYSIYFDSENQIFELNNDHSFLSELESFFYSYHNSSYMNNGSKNDEPHYHFNLYDNDTNCGWNNHINSCIDSYLRSQICIDSSILSGSDNSNDNYISNYICGEGGNSSEGKNFDIITRENGNDLTLKESSNDLDLYKDLWVQCECENCYGVNYKKSLNSKMNICEQCGYHLKMRSSDRIELSIDPGTWGPMDEDMISLDPIEFQSEEELYKDRIDFYQRKTGLTEAIQTGT... | 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... |
A1WY04 | MSWFQKLMPRRIRTDAGPRSRSVPEGLWTKCESCQGILYRPDLERNLEVCPKCGAHMRISARQRLRLFLDESCEAVEIGAELQPSDFLRFRDSKRYRDRLNQAQKATGENDALVAMRGAVHQRPVVVCAFEFGFMGGSMGTIVGERFCRAAEEARANDIPLVCFSASGGARMQEALFSLMQMAKTSAAISRLNEARVPYISVLTDPTMGGVSASLATLGDVIIAEPGALIGFAGPRVIEQTVRETLPEGFQRAEFLLDHGAIDMIVDRRDMRDEIASLMGKLGGDVSVAPAPAPAATVDPEPESAEPEAPAEEAGPAGAA... | 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... |
B0TI33 | MDGLWVKCKQCQQILLTKELEKNLKVCRCGYHFRMTAQERIVMLVDENSFIEWDRELVSKDPLQFPGYAQKIQKCQIETSMSEAITTGQGRICDIPVVLGVMDPRFIMASMGAVVGEKIVRAAERALKLRLPLVLFSASGGARMQEGVLSLMQMARTSAALTRLSKAGLPFFSVLTDPTTGGVTASFAMLGDLIIAEPGALIGFTGPRVIEQTIRQKLPEGFQRSEFLQKHGMVDIIIERPKMREQLAALLALHCGNSLEGVES | 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... |
Q2EEX4 | MTILAWIKDKKNKAILNTPEYSSQSSLSWCFTHKEAASNKAVSFINLSKRRALWTRCEKCGMIQFMRFFKENANLCLSCSYHHIMTSDERIALLVEKGTWYPLNETISPKDPIKFTDTQSYAQRIQSTQEKLGMQDAVQTGTGLINGIPFAIGIMDFRFMGGSMGSVVGEKLTRLIEYATKQGLFLLIVSASGGARMQEGIYSLMQMAKISAALNVYQNEANLLYISLCTSPTTGGVTASFAMLGDIIFSEPEAIIGFAGRRVIQQTLQQELPEDFQTSESLLHHGLIDAIVPRCFLVNAISEVASIFAYAPSKYKKLGN... | 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... |
A9B536 | MKDFFRRAPLPFTSSRREQQIPDNVWAKCANCGELTYQKQFNDALKVCPKCSYHSRISSREWIEVLADADSFVEYDADLQGIDILGFVSPKDNYEAKLAATSERTGTNDVVMSGSASIEGLPFEIAACNFEFMGGSMGSVFGEKVARAVERAADRGVPVLTINASGGARMHEGIFALMQMAKVSVALTRLARVRQPHISLLVDPCYGGVSASYASVADIILAEPGANIGFAGRRVIEQTIRQKLPPNFQTAEFFLEHGMIDAVVPRSDMRATIGRLLRLYQRPTSSADHREHVVAGHQ | 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... |
B2FNY8 | MSWLSKLMPSGIRTDNTPSKKRSVPEGLWEKCSNCGSALYRPELEENLEVCPKCGHHMAIRARARLAALFDADSTTEIGARLGPTDLLKFKDQKKYSERIKIAQKNTGEYDALIAMRGLLKGRALVASSFDFAFMGGSMGSVVGERFALAAETAVEIGAPYVCFSQSGGARMQEGLFSLMQMAKTSAALGKLRETGLPYISVLTHPTTGGVSASFAMLGDINIAEPQALIGFAGPRVIEQTVREKLPEGFQRSEFLLEHGAIDQICDRREMRDRLSDLLAMLGRQPAPEVA | 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... |
A6TAC5 | MRKRKVAIIGSGNIGTDLMIKILRHGQHLEMAVMVGIDPQSDGLARARRLGVATTHEGVGGLMQMAEFADIDFVFDATSAGAHIKNDAALREAKPGIRVIDLTPAAIGPYCVPVVNLADNLHQGNVNMVTCGGQATIPMVAAVSRVAKVHYAEIVASIASQSAGPGTRANIDEFTETTSQAIEKVGGAGKGKAIIVLNPAEPPLMMRDTVYILSELASQEAIAASIAEMAAAVQAYVPGYRLKQQVQFEVIPEDRPVNLPGVGCFSGLKTAVYLEVEGAAHYLPAYAGNLDIMTSAALATAEQMAGAMHSAAGATA | Function: Catalyzes the conversion of acetaldehyde to acetyl-CoA, using NAD(+) and coenzyme A. Is the final enzyme in the meta-cleavage pathway for the degradation of aromatic compounds.
Catalytic Activity: acetaldehyde + CoA + NAD(+) = acetyl-CoA + H(+) + NADH
Sequence Mass (Da): 32915
Sequence Length: 316
Pathway: Ar... |
Q7TTR4 | MPSKAKVAIVGSGNISTDLLYKLLRSEWLEPRWMVGIDPESDGLARAAKLGLETTHEGVDWLLAQPDKPDLVFEATSAYVHRDAAPKYAEAGIRAIDLTPAAVGPAVIPPANLREHLDAPNVNMITCGGQATIPIVYAVSRIVEVPYAEIVASVASVSAGPGTRANIDEFTKTTARGVQTIGGAARGKAIIILNPADPPMIMRDTIFCAIPTDADREAIAASIHDVVKEVQTYVPGYRLLNEPQFDEPSINSGGQALVTTFVEVEGAGDYLPPYAGNLDIMTAAATKVGEEIAKETLVVGGAR | Function: Involved in cholesterol degradation. Catalyzes the conversion of propanal to propanoyl-CoA, using NAD(+) and coenzyme A.
Catalytic Activity: CoA + NAD(+) + propanal = H(+) + NADH + propanoyl-CoA
Sequence Mass (Da): 32009
Sequence Length: 303
EC: 1.2.1.87
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Q6NCX0 | MTATASHTRARPLGASEIEHATRIAEPDFDLLDALYRTDDPDDQARLLARVVLSAFDNYYAVSRRIPALAQAAFEARDWPVTVRLSKIRIGLYTACIDQLVPLLKAGLPELTTDEQLWPTAEAELLAAIEGRYEADFAFAFWQSLRRKLVSDEWRPVSYDAGSTARRTTSPAAVLKTTATTLPITAEVIAGILDEAGFRVPWRDRDGDAALAAQAIETALEPLSPRPGEPVKIEIADSGFLRNRGACLVGRIKLRDRGDMPMRNLPLLIALLNEKDGLVVDAVLTDSDELQYAFSSTLANYHATNPRYHELARLLYELMP... | 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... |
P49582 | MCGRRGGIWLALAAALLHVSLQGEFQRRLYKELVKNYNPLERPVANDSQPLTVYFSLSLLQIMDVDEKNQVLTTNIWLQMSWTDHYLQWNMSEYPGVKNVRFPDGQIWKPDILLYNSADERFDATFHTNVLVNASGHCQYLPPGIFKSSCYIDVRWFPFDVQQCKLKFGSWSYGGWSLDLQMQEADISSYIPNGEWDLMGIPGKRNEKFYECCKEPYPDVTYTVTMRRRTLYYGLNLLIPCVLISALALLVFLLPADSGEKISLGITVLLSLTVFMLLVAEIMPATSDSVPLIAQYFASTMIIVGLSVVVTVIVLRYHHH... | Function: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. The channel is blocked by alpha-bungarotoxin.
PTM: Glycosylations at Asn-46, Asn-90 and Asn-133 are essential for TMEM35... |
Q9UGM1 | MNWSHSCISFCWIYFAASRLRAAETADGKYAQKLFNDLFEDYSNALRPVEDTDKVLNVTLQITLSQIKDMDERNQILTAYLWIRQIWHDAYLTWDRDQYDGLDSIRIPSDLVWRPDIVLYNKADDESSEPVNTNVVLRYDGLITWDAPAITKSSCVVDVTYFPFDNQQCNLTFGSWTYNGNQVDIFNALDSGDLSDFIEDVEWEVHGMPAVKNVISYGCCSEPYPDVTFTLLLKRRSSFYIVNLLIPCVLISFLAPLSFYLPAASGEKVSLGVTILLAMTVFQLMVAEIMPASENVPLIGKYYIATMALITASTALTIMV... | Function: Ionotropic receptor with a probable role in the modulation of auditory stimuli. Agonist binding induces a conformation change that leads to the opening of an ion-conducting channel across the plasma membrane . The channel is permeable to a range of divalent cations including calcium, the influx of which may a... |
P43144 | MNRPHSCLSFCWMYFAASGIRAVETANGKYAQKLFSDLFEDYSSALRPVEDTDAVLNVTLQVTLSQIKDMDERNQILTAYLWIRQTWHDAYLTWDRDQYDRLDSIRIPSDLVWRPDIVLYNKADDESSEPVNTNVVLRYDGLITWDSPAITKSSCVVDVTYFPFDSQQCNLTFGSWTYNGNQVDIFNALDSGDLSDFIEDVEWEVHGMPAVKNVISYGCCSEPYPDVTFTLLLKRRSSFYIVNLLIPCVLISFLAPLSFYLPAASGEKVSLGVTILLAMTVFQLMVAEIMPASENVPLIGKYYIATMALITASTALTIMV... | Function: Ionotropic receptor with a probable role in the modulation of auditory stimuli. Agonist binding induces a conformation change that leads to the opening of an ion-conducting channel across the plasma membrane. The channel is permeable to a range of divalent cations including calcium, the influx of which may ac... |
P09479 | MELCRVLLLIFSAAGPALCYEHETRLVDDLFREYSKVVRPVENHRDAVVVTVGLQLIQLINVDEVNQIVTTNVRLKQQWTDINLKWNPDDYGGVKQIRIPSDDIWRPDLVLYNNADGDFAIVKYTKVLLEHTGKITWTPPAIFKSYCEIIVTYFPFDQQNCSMKLGTWTYDGTMVVINPESDRPDLSNFMESGEWVMKDYRGWKHWVYYACCPDTPYLDITYHFLMQRLPLYFIVNVIIPCLLFSFLTGFVFYLPTDSGEKMTLSISVLLSLTVFLLVIVELIPSTSSAVPLIGKYMLFTMVFVIASIIITVIVINTHHR... | Function: Upon acetylcholine binding, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 52183
Sequence Length: 456
Subcellular Location: Posts... |
P54251 | AIFKSYCEIIVTHFPFDEQNCSMKLGTWTYDSSVVVINPESDQPDLSNFMESGEWVIKEARGWKHNVTYACCLTTHYLDITYHF | Function: Upon acetylcholine binding, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 9803
Sequence Length: 84
Subcellular Location: Postsyn... |
P02708 | MEPWPLLLLFSLCSAGLVLGSEHETRLVAKLFKDYSSVVRPVEDHRQVVEVTVGLQLIQLINVDEVNQIVTTNVRLKQQWVDYNLKWNPDDYGGVKKIHIPSEKIWRPDLVLYNNADGDFAIVKFTKVLLQYTGHITWTPPAIFKSYCEIIVTHFPFDEQNCSMKLGTWTYDGSVVAINPESDQPDLSNFMESGEWVIKESRGWKHSVTYSCCPDTPYLDITYHFVMQRLPLYFIVNVIIPCLLFSFLTGLVFYLPTDSGEKMTLSISVLLSLTVFLLVIVELIPSTSSAVPLIGKYMLFTMVFVIASIIITVIVINTHH... | Function: Upon acetylcholine binding, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 51839
Sequence Length: 457
Subcellular Location: Posts... |
P14143 | NPPAIFKSYCEIIVTYFPFDEQNCSMKLGTWTYDGTVVAIYPEGPRPDLSNYMQSGEWTLKDYRGFWHSVNYSCCLDTPYLDITYHFILLRLPLYFIVNVIIPC | Function: Upon acetylcholine binding, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 12194
Sequence Length: 104
Subcellular Location: Posts... |
B5Y7W0 | MKILVLNAGSSSLKFQLFDMEDESVMAKGIVERIGLDKPFLSYSKGTDKIKFDKEEPINHKDALQWVLNTLTSHEYGVITTLQEIGAVGHRVVHGGEEFTGSVLITEEVIEALERNKNLAPLHNPPNLTGIYATKAVLPEVPMVGVFDTAFHATMPERAYLYALPIELYEKYKVRRYGFHGTSHRYVAMEAARRLGKTLSELRIISAHLGNGASVCAIQGGKSIDTSMGFTPLEGLVMGTRSGDLDPAIPIWMMRELGMSFDEVDNLLNKKSGVFGLVRGRSFDMRDIEDWMAAGDEEAKKAMEVYCYRLKKYIGGYAAV... | 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): 44202
Sequence Length: 400
Pathway: Metabolic intermediate biosynthesis; acetyl-CoA... |
P77845 | MALALVLNSGSSSIKFQLVNPENSAIDEPYVSGLVEQIGEPNGRIVLKIEGEKYTLETPIADHSEGLNLAFDLMDQHNCGPSQLEITAVGHRVVHGGILFSAPELITDEIVEMIRDLIPLAPLHNPANVDGIDVARKILPDVPHVAVFDTGFFHSLPPAAALYAINKDVAAEHGIRRYGFHGTSHEFVSKRVVEILEKPTEDINTITFHLGNGASMAAVQGGRAVDTSMGMTPLAGLVMGTRSGDIDPGIVFHLSRTAGMSIDEIDNLLNKKSGVKGLSGVNDFRELREMIDNNDQDAWSAYNIYIHQLRRYLGSYMVAL... | 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): 43092
Sequence Length: 397
Pathway: Metabolic intermediate biosynthesis; acetyl-CoA... |
P0CL99 | MPDKTEYLLAINCGSSSIKGKLFAIPSFELLANLAVTNISSADERVKIRITWEEGKGKNSEEEADYGDKIRYASLVPILLDHLTNSTHVEKEEIKYVCHRVVHGGTHDRGIRVVKGHEEGLIEMDKLSEFAPLHNHRAVLAVKSCLDALPHHTSLLLFDTIFHQTIAPEVYTYALPPSDNELSMPLRKYGFHGLSYASIVRSLAEHLKKPSDQVNVVVAHLGSGSSSCCIKNGKSVDTSMGLTPLEGLLGGTRSGTIDPTAIFHHTKDAASDANVGDFTVSKAEIILNKNSGLKALAGTTNFGHIIQNLDPSKCSKEDHE... | Catalytic Activity: acetate + ATP = acetyl phosphate + ADP
Sequence Mass (Da): 46972
Sequence Length: 430
Pathway: Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis; acetyl-CoA from acetate: step 1/2.
EC: 2.7.2.1
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B1W052 | MEPHRVLVLNSGSSSVKYQLLDMRDRSRLASGLVERIGEETSRLAHTPSAGGGAEPRERTGRIPDHDAALKAAAEELAADGLGLDSPELAAIGHRVVHGGLRFSAPTVITDEVLEEIERLVPVAPLHNPANITGIVTARALRPDLPQVAVFDTAFHTTMPEAAARYAIDVETADAHRIRRYGFHGTSHAYVSRKTAELLGRAPEDVNVIVLHLGNGASASAVAGGRCVDTSMGLTPLEGLVMGTRSGDIDPAVTFHLKRVAGMSADEIDVLLNQRSGLVGLCGDNDMRVIRRRIDEGDERAALAFDIYIHRLKKYIGAYT... | 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): 43870
Sequence Length: 412
Pathway: Metabolic intermediate biosynthesis; acetyl-CoA... |
P30544 | MENDTWENESSASNHSIDETIVEIPGKYQTMEMIFIATVTGSLSLVTVVGNILVMLSIKVNRQLQTVNNYFLFSLACADLIIGVFSMNLYSLYIIKGYWPLGPIVCDLWLALDYVVSNASVMNLLIISLERXFCVTKPLTYPARRTTKMAGLMIAAAWLLSFELWAPAILFWQFIVGQRTVPSGECYIQFLSNPAVTFGTAIAAFYLPVVIMTILYIHISLASRSRVRRHCPETRQEKKKPISSMKSLLIKQTKNIPKQDAGDKVVEKKNGVSNGKIEKSMTNLQTAEEKETSNESSSASLSHNPPEKQPLSEASSGVVL... | 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 inhibition of adenylate cyclase.
Location Topology: Multi-pa... |
P08912 | MEGDSYHNATTVNGTPVNHQPLERHRLWEVITIAAVTAVVSLITIVGNVLVMISFKVNSQLKTVNNYYLLSLACADLIIGIFSMNLYTTYILMGRWALGSLACDLWLALDYVASNASVMNLLVISFDRYFSITRPLTYRAKRTPKRAGIMIGLAWLISFILWAPAILCWQYLVGKRTVPLDECQIQFLSEPTITFGTAIAAFYIPVSVMTILYCRIYRETEKRTKDLADLQGSDSVTKAEKRKPAHRALFRSCLRCPRPTLAQRERNQASWSSSRRSTSTTGKPSQATGPSANWAKAEQLTTCSSYPSSEDEDKPATDPV... | 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
... |
A1IHE6 | MSTTTLDAAVIGTGVAGLYELHMLREQGLEVRAYDKASGVGGTWYWNRYPGARFDSEAYIYQYLFDEDLYKGWSWSQRFPGQEEIERWLNYVADSLDLRRDISLETEITSAVFDEDRNRWTLTTADGDTIDAQFLITCCGMLSAPMKDLFPGQSDFGGQLVHTARWPKEGIDFAGKRVGVIGNGATGIQVIQSIAADVDELKVFIRTPQYALPMKNPSYGPDEVAWYKSRFGELKDTLPHTFTGFEYDFTDAWEDLTPEQRRARLEDDYENGSLKLWLASFAEIFSDEQVSEEVSEFVREKMRARLVDPELCDLLIPSDY... | Cofactor: Binds 1 FAD per subunit.
Function: Plays an important role in the metabolism of acetone derived from propane oxidation . Catalyzes the oxidation of acetone to methyl acetate . Exhibits high catalytic efficiency towards various linear and cyclic ketones, such as butanone, 2-pentanone, 2-heptanone, 2-octanone, ... |
A2RHZ5 | MPVSRVKVKNRHLKKKTKKPLAFYKPATKFAGAVLIAGTLTTTHELLLQQTSPMVQAATNSSEVFIESIAASAKPVADANGLYPSVMIAQAILESNWGSSQLSRAPYYNLFGIQGTYQGKSVVFKTQEYLNGKWVTKDMPFRVYPSFNQSFQDNAYVLKTTNFGNGPYYAKAWRANAATYQDATAALTGRYATDPSYGASLNRIISQYNLTRFDGASSAGNTNSGGSTTTITNNNSGTNSSSTTYTVKSGDTLWGISQRYGISVAQIQSANNLKSTIIYIGQKLVLTGSASSTNSGGSNNSASTTPTTSVTPAKPTSQTT... | Function: Hydrolyzes the cell wall of L.lactis and M.lysodeikticus. Required for cell separation during growth.
Catalytic Activity: Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.
Sequenc... |
A1IHE7 | MTSTFSSLDVSAFTSAADRILAEAVTGDARVPGVVAMVTDRDRTVYSGAAGQRSLGGSAPMTTDDVFAIFSTTKAITATAALQLVEEGLLDLDAPASTYAPAIGTLQVIEGFDDAGEPILRAPKSVPTTRQLLTHTGGFGYDFFDEIYNRLAEEKGQPSVTTASRAALMTPLLFDPGERWQYGTNIDWVGQVVEGLRGKRLGEVFAERIFAPLGIENMSFILREDFRSHLTEIHARNADGSLTPMGLELPSPPEVDFGGHGLYGTVGEYMKFIRMWLNDGVGEGGRVLKAETVEMALRNHLGDLPVTMLPGVIPSLSNDA... | Function: Plays an important role in the metabolism of acetone derived from propane oxidation . Catalyzes the hydrolysis of methyl acetate to acetate and methanol .
Catalytic Activity: H2O + methyl acetate = acetate + H(+) + methanol
Sequence Mass (Da): 43457
Sequence Length: 401
EC: 3.1.1.114
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D6R237 | MISKDDIRAILAEGTDLGPPEQFPDDADVVMDSFTLIVLQHGLEERHGVVIDPHFEDMEQFTSIDGIHAYLTALPAER | Function: Involved in the biosynthesis of actinomycin . Acts as a carrier in the transfer and thioesterification of 4-methyl-3-hydroxyanthranilic acid (4-MHA) .
PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine of the apo-form of this carrier protein.
Sequence Mass (Da): 8691
Sequence Length: 78
P... |
Q0II68 | MKIDIHTHILPREWPDLKKRFGYGGWVQLQHNGKGEAKMLKDGKVFRVVQENCWDPEARLREMDQTGVTVQALSTVPVMFSYWAKPQDTLDLCQLLNNDLAATIASHPRRFVGLGTLPMQAPELAVKEMERCVRKLGFPGVQIGSHINEWDLNARELFPVYAEAERLNCSLFVHPWDMQMDGRMAKYWFPWLIGMPAETTAAICSMIMGGVFEKFPKLKVCFAHGGGSFPFTVGRISHGFSMRPDLCAQDNPTNPKKYLGSFYTDSLVHDPLALKLLTDVIGKDKVILGTDYPFPLGELEPGKLIESMGEFDAETKDKLK... | Function: Converts alpha-amino-beta-carboxymuconate-epsilon-semialdehyde (ACMS) to alpha-aminomuconate semialdehyde (AMS). ACMS can be converted non-enzymatically to quinolate (QA), a key precursor of NAD, and a potent endogenous excitotoxin of neuronal cells which is implicated in the pathogenesis of various neurodege... |
Q8T8B9 | MPICEFSATSKSRKIDVHAHVLPKNIPDFQEKFGYPGFVRLDHKEDGTTHMVKDGKLFRVVEPNCFDTETRIADMNRANVNVQCLSTVPVMFSYWAKPADTEIVARFVNDDLLAECQKFPDRLVPLGTLPMNDVQRAVEIFGKRIFFFEIWSPAKKSPEEVKRCVSMGIKGFEVGSHVAEKSLDHRDFWPLYKLTESFKLSTIMPGFCEFFENWGLTTKTPGICEELSVVLFVHPWDMHMWDGRLDKYWMPWLVGMPSETAQAICSVLMGNILVLFPKLKLCFAHGGGAYPQIRGRVSHGWNVRPDLCAGKCKVAPNKLD... | Function: Converts alpha-amino-beta-carboxymuconate-epsilon-semialdehyde (ACMS) to alpha-aminomuconate semialdehyde (AMS).
Catalytic Activity: 2-amino-3-carboxymuconate 6-semialdehyde + H(+) = 2-aminomuconate 6-semialdehyde + CO2
Sequence Mass (Da): 45746
Sequence Length: 401
Pathway: Secondary metabolite metabolism; q... |
Q54LN9 | MENKETTTTTTTTNNGSDKKKRSLKIDLHTHILPKNWPNLKEKYGYGGWVSLDHHCSCKAKMMIDGKFFREIDSNCWDPDVRIQELNRDDVDIQVLSTVPVMFGYWAKPQDALDLAQYLNDHIAQVVSENPKRFIGLGSLPMQCTESSIQELRRCILELGLPGIQIGSNVNGKNLDDPSLFPIFEECEKLGAAVFIHPWEMVGKDRMPQYWLPWLVGMPAETCLAICSMIFGGVFQRLPNLKVCFAHGGGSFPFTIGRIEHGFNARPDLCAVVNPINPREYIGKFWVDSLVHDEEALKFLVNLMGEKKVTLGTDYPFPLG... | Function: Converts alpha-amino-beta-carboxymuconate-epsilon-semialdehyde (ACMS) to alpha-aminomuconate semialdehyde (AMS).
Catalytic Activity: 2-amino-3-carboxymuconate 6-semialdehyde + H(+) = 2-aminomuconate 6-semialdehyde + CO2
Sequence Mass (Da): 40451
Sequence Length: 359
Pathway: Secondary metabolite metabolism; q... |
Q8TDX5 | MKIDIHSHILPKEWPDLKKRFGYGGWVQLQHHSKGEAKLLKDGKVFRVVRENCWDPEVRIREMDQKGVTVQALSTVPVMFSYWAKPEDTLNLCQLLNNDLASTVVSYPRRFVGLGTLPMQAPELAVKEMERCVKELGFPGVQIGTHVNEWDLNAQELFPVYAAAERLKCSLFVHPWDMQMDGRMAKYWLPWLVGMPAETTIAICSMIMGGVFEKFPKLKVCFAHGGGAFPFTVGRISHGFSMRPDLCAQDNPMNPKKYLGSFYTDALVHDPLSLKLLTDVIGKDKVILGTDYPFPLGELEPGKLIESMEEFDEETKNKLK... | Function: Converts alpha-amino-beta-carboxymuconate-epsilon-semialdehyde (ACMS) to alpha-aminomuconate semialdehyde (AMS). ACMS can be converted non-enzymatically to quinolate (QA), a key precursor of NAD, and a potent endogenous excitotoxin of neuronal cells which is implicated in the pathogenesis of various neurodege... |
P83662 | MKIDIHSHILPKEWPDLKKRFGYXGWVELQHHSEGEAKMLKDGKVFRVVQERFVGLGTLPMQAPXSLFVHPWDMQYWFPWLIGMPAETTTAXESMMMGGVFEKVXFAHGGGSFPFTVGRIVILGTDYPFPLGELEPGK | Function: Converts alpha-amino-beta-carboxymuconate-epsilon-semialdehyde (ACMS) to alpha-aminomuconate semialdehyde (AMS). ACMS can be converted non-enzymatically to quinolate (QA), a key precursor of NAD, and a potent endogenous excitotoxin of neuronal cells which is implicated in the pathogenesis of various neurodege... |
Q4WLN1 | MISTRLARAGALAPKSRLFLGTRAFATVGDSPLDKKVEMANTEKGNYINYKKMSENLDIVRRRLQRPLTYAEKVLYSHLDDPHGQEIERGKSYLKLRPDRVACQDATAQMAILQFMSAGMPSVATPTTVHCDHLIEAQVGGDKDLARANEINKEVYDFLASATAKYNIGFWKPGSGIIHQIVLENYAFPGGLMIGTDSHTPNAGGLAMAAIGVGGADAVDVMAGLPWELKAPKVIGVKLTGEMSGWTTPKDVILKVAGLLTVKGGTGAIIEYHGPGVTSLSCTGMGTICNMGAEIGATTSMFPFNDRMYDYLKATKRQHI... | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the isomerization of citrate to isocitrate via cis-aconitate, a step in the citric acid cycle. Also catalyzes the reversible dehydration of (R)-homocitrate to cis-homoaconitate, a step in the alpha-aminoadipate pathway for lysine biosynthesis.
Catalyti... |
Q99798 | MAPYSLLVTRLQKALGVRQYHVASVLCQRAKVAMSHFEPNEYIHYDLLEKNINIVRKRLNRPLTLSEKIVYGHLDDPASQEIERGKSYLRLRPDRVAMQDATAQMAMLQFISSGLSKVAVPSTIHCDHLIEAQVGGEKDLRRAKDINQEVYNFLATAGAKYGVGFWKPGSGIIHQIILENYAYPGVLLIGTDSHTPNGGGLGGICIGVGGADAVDVMAGIPWELKCPKVIGVKLTGSLSGWSSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPYNHRMKKYLSKTGREDIANLAD... | Cofactor: Binds 1 [4Fe-4S] cluster per subunit. Binding of a [3Fe-4S] cluster leads to an inactive enzyme.
Function: Catalyzes the isomerization of citrate to isocitrate via cis-aconitate.
PTM: Forms covalent cross-links mediated by transglutaminase TGM2, between a glutamine and the epsilon-amino group of a lysine resi... |
P37032 | MKVGQDSLSTKSQLTVDGKTYNYYSLKEAENKHFKGINRLPYSLKVLLENLLRFEDGNTVTTKDIKAIADWLHNKTSQHEIAFRPTRVLMQDFTGVPAVVDLAAMRTAIVKMGGNADKISPLSPVDLVIDHSVMVDKFASADALEVNTKIEIERNKERYEFLRWGQKAFSNFQVVPPGTGICHQVNLEYLGKTVWNSENDGQLYAYPDTLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPVSMLIPEVIGFKLSGKLKEGITATDLVLTVTQMLRKKGVVGKFVEFYGPGLNDLPLADRATISNMAPEYGATCGFFP... | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and probably the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the reversible isomerization of citrate to isocitrate via c... |
P16276 | MAPYSLLVTRLQKALGVRQYHVASVLCQRAKVAMSHFEPHEYIRYDLLEKNIDIVRKRLNRPLTLSEKIVYGHLDDPANQEIERGKTYLRLRPDRVAMQDATAQMAMLQFISSGLPKVAVPSTIHCDHLIEAQLGGEKDLRRAKDINQEVYNFLATAGAKYGVGFWRPGSGIIHQIILENYAYPGVLLIGTDSHTPNGGGLGGICIGVGGADAVDVMAGIPWELKCPKVIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPYNHRMKKYLSKTGRADIANLAD... | Cofactor: Binds 1 [4Fe-4S] cluster per subunit. Binding of a [3Fe-4S] cluster leads to an inactive enzyme.
Function: Catalyzes the isomerization of citrate to isocitrate via cis-aconitate.
PTM: Forms covalent cross-links mediated by transglutaminase TGM2, between a glutamine and the epsilon-amino group of a lysine resi... |
O13966 | MFCKISRAPARMGSRIFTQSTLRSFSCAPVAANIDAKKVAMSNFEKNKFINYQRIKDNLEIVKKRLNRPLTYSEKILYGHLDDPVNQDIERGVSYLKLRPDRVACQDATAQMAILQFMSAGMPEVAVPVTVHCDHLIEAYEGGPIDLERANVTNKEVYDFLQTACAKYNIGFWRPGSGIIHQIVLENYAFPGGLLIGTDSHTPNAGGLGMVAIGVGGADAVDVMANLPWELKCPKVIGVKLTGQLKGWTSPKDVILKVAGILTVKGGTGAIVEYFGPGVESLSCTGMGTICNMGAEIGATTSIFPFNPRMSEYLRATNRS... | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the isomerization of citrate to isocitrate via cis-aconitate, a step in the citric acid cycle.
Catalytic Activity: citrate = D-threo-isocitrate
Sequence Mass (Da): 86113
Sequence Length: 789
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; i... |
P19414 | MLSARSAIKRPIVRGLATVSNLTRDSKVNQNLLEDHSFINYKQNVETLDIVRKRLNRPFTYAEKILYGHLDDPHGQDIQRGVSYLKLRPDRVACQDATAQMAILQFMSAGLPQVAKPVTVHCDHLIQAQVGGEKDLKRAIDLNKEVYDFLASATAKYNMGFWKPGSGIIHQIVLENYAFPGALIIGTDSHTPNAGGLGQLAIGVGGADAVDVMAGRPWELKAPKILGVKLTGKMNGWTSPKDIILKLAGITTVKGGTGKIVEYFGDGVDTFSATGMGTICNMGAEIGATTSVFPFNKSMIEYLEATGRGKIADFAKLYHK... | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the isomerization of citrate to isocitrate via cis-aconitate, a step in the citric acid cycle. Can also provide minor contributions to the reversible dehydration of (R)-homocitrate to cis-homoaconitate, a step in the alpha-aminoadipate pathway for lysi... |
O55137 | MEATLNLEPSGRSCWDEPLSIAVRGLAPEQPVTLRSVLRDEKGALFRAHARYRADSHGELDLARTPALGGSFSGLEPMGLLWAMEPDRPFWRLVKRDVQTPFVVELEVLDGHEPDGGQRLAHAVHERHFLAPGVRRVPVREGRVRATLFLPPEPGPFPGIIDLFGVGGGLLEYRASLLAGKGFAVMALAYYNYDDLPKNMETMHMEYFEEAVNYLRSHPEVKGPGIGLLGISKGGELGLAMASFLKGITAAVVINGSVAAVGNTISYKDETIPPVTILRNQVKMTKDGLKDVVDALQSPLVDKKSFIPVERSDTTFLFLV... | Function: Catalyzes the hydrolysis of acyl-CoAs into free fatty acids and coenzyme A (CoASH), regulating their respective intracellular levels. More active towards saturated and unsaturated long chain fatty acyl-CoAs (C12-C20).
Catalytic Activity: H2O + hexadecanoyl-CoA = CoA + H(+) + hexadecanoate
Sequence Mass (Da): ... |
P49753 | MSNKLLSPHPHSVVLRSEFKMASSPAVLRASRLYQWSLKSSAQFLGSPQLRQVGQIIRVPARMAATLILEPAGRCCWDEPVRIAVRGLAPEQPVTLRASLRDEKGALFQAHARYRADTLGELDLERAPALGGSFAGLEPMGLLWALEPEKPLVRLVKRDVRTPLAVELEVLDGHDPDPGRLLCQTRHERYFLPPGVRREPVRVGRVRGTLFLPPEPGPFPGIVDMFGTGGGLLEYRASLLAGKGFAVMALAYYNYEDLPKTMETLHLEYFEEAMNYLLSHPEVKGPGVGLLGISKGGELCLSMASFLKGITAAVVINGSV... | Function: Catalyzes the hydrolysis of acyl-CoAs into free fatty acids and coenzyme A (CoASH), regulating their respective intracellular levels . Displays higher activity toward long chain acyl CoAs (C14-C20) . The enzyme is involved in enhancing the hepatic fatty acid oxidation in mitochondria (By similarity).
Catalyti... |
A9WE63 | MLYHGVDLVEVARIRHAVVRYGQRFVQRVYTATEQADCLAGSGDVRYEALAARWAAKEACAKALGIGLRGLGALAVADRPRAGFHEIEVVRDNDGRPVLRLSGFAAEQAAALGICALAVSLSHTDELALASVVAWAG | 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): 14528
Sequence Length: 137
Subcellular Location: Cytoplasm
EC: 2.7.8.7
|
Q820E7 | MQTAHIGTDIIEISRIRKAIKAHSQRILNKIFTKREQEYCLSLTNPYPSFAARFAAKEAVAKALGTGIGKVVRWKDIEILKSSKHPEVYLPERVYKELGISKVLLSISHSREYATAVAVTLI | 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): 13722
Sequence Length: 122
Subcellular Location: Cytoplasm
EC: 2.7.8.7
|
Q254H8 | MQMAHIGTDIIEIARIRKAIETHNQRMLNKIFTKKEQEYCLRLTNPYPSFAARFAGKEAVAKALGTGIGKVIGWKDIEILTSPKQPKVHLPPRVYKELGISKVLLSISHSREYATAMAVALV | 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): 13657
Sequence Length: 122
Subcellular Location: Cytoplasm
EC: 2.7.8.7
|
Q9PKT6 | MFGIGTDIIEIDRIRRAYHTYGDRFLNKIFTKGEQAYCFSKSDPYASLAVRFAAKEAVSKALGTGIGKSLKWKEIEISRGTQHPQVSVPESLLALLEVKRILLSMSHCREYATAVAIAEVTNSSK | 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): 13897
Sequence Length: 125
Subcellular Location: Cytoplasm
EC: 2.7.8.7
|
Q9Z8M5 | MEIIHIGTDIIEISRIREAIATHGNRLLNRIFTEAEQKYCLEKTDPIPSFAGRFAGKEAVAKALGTGIGSVVAWKDIEVFKVSHGPEVLLPSHVYAKIGISKVILSISHCKEYATATAIALA | 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): 13227
Sequence Length: 122
Subcellular Location: Cytoplasm
EC: 2.7.8.7
|
B3QTH9 | MQVGIDIIEISRIKRAYERYNRLFLKRILTESEIEWCLNKPRPFESVAVRFACKEAFAKAMGTGISGELSWQSIEILNDKEGKPTLFLKQPFNGLKSEQVKLSLSHTHEYAVAVVIIEPDK | 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): 13883
Sequence Length: 121
Subcellular Location: Cytoplasm
EC: 2.7.8.7
|
Q3KMS0 | MFGVGIDIIEIDRIRKSYQTYGDRFLKKIFTEGERVYCFSKSNPYASLAARFAAKEAVAKALGTGIGKLLKWKEIEMCRDSRQPQVVVPEALLCSLGVKRVLLSVSHSREYATAVAIAE | 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): 13275
Sequence Length: 119
Subcellular Location: Cytoplasm
EC: 2.7.8.7
|
Q8KB56 | MEIGVDIVEIARIRSSYDRFGEAFMKKILTSAEMAQCLSKPDPVASLAGRFAAKEAVSKALGTGIAKGLTWHSIEVLNDETGKPCVSVYAPSFSGRVSISISHDRYSAVAMALFEPR | 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): 12611
Sequence Length: 117
Subcellular Location: Cytoplasm
EC: 2.7.8.7
|
Q1D4A0 | MGIRGLGLDICSISRIQRILDGPRAEPFLNRVYTEAERALCGRRSDAASAYAARFAAKEALVKALGAPPGIRWKDMEVRRQGGAPYFALSGVALEVMEARGLEAFLALTHDADVAAATVVLQSKGD | 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): 13474
Sequence Length: 126
Subcellular Location: Cytoplasm
EC: 2.7.8.7
|
B2A4X6 | MIIGLGVDIIEIARIKKVYNKFPWKFVNKLFSDREQKKLMTLHNPNEYISGRFAAKEAVAKAFGTGIGQVRWKDIEILTADEGYPVVNLHGEALNKAEELGVTKVYLSISHSKTSAVANAILWSD | 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): 13976
Sequence Length: 125
Subcellular Location: Cytoplasm
EC: 2.7.8.7
|
B9L9S0 | MIGIDIVSISRIDEMINKFGEKALKRFLNESEILLTKSSQNAAGFWAAKEAFSKALGTGIGSECSFLDIEISKDQKGKPFFTTKTLNKFNIKQADLSISHDGGFAIAAVILLK | 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): 12329
Sequence Length: 113
Subcellular Location: Cytoplasm
EC: 2.7.8.7
|
Q9RQW2 | MIYGIGTDIVSLKRIVRLSKKFGQAFAERILTPEELLEFPQAGKPVNYLAKRFAAKEAFAKAVGTGIRGAVSFRNIGIGHDALGKPEFFYAPALSKWLEEQGISRVSLSMSDEEDTVLAFAVAEK | 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): 13694
Sequence Length: 125
Subcellular Location: Cytoplasm
EC: 2.7.8.7
|
Q0AF73 | MIYGIGTDLVDPARIAGSLERYGERFARRVLADSEWSEYVRQTRPEVFLAKRFAAKEAFSKAVGTGLRTPVMFGNIAVQHDTQGKPYFEFHQELIDWIGQRGIVSHHLSISDELTLASAFVVLEK | 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): 14114
Sequence Length: 125
Subcellular Location: Cytoplasm
EC: 2.7.8.7
|
Q820I1 | MIYGIGTDLVDPARIASSLERYGEQFARRVLADSEWPDYLEHIKPALFLAKRFAAKEAFSKATGTGLRAPVMFGNMAVQHDSQGKPYFEFQQELAEWIGQRGITRHHLSISDELTMVSAFVVLEK | 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): 14104
Sequence Length: 125
Subcellular Location: Cytoplasm
EC: 2.7.8.7
|
Q2Y864 | MIYGIGTDLVETSRITRLLEKYGERFARRLLTDEEWPEYAKSMQPAMFLAKRFAAKEALAKAFGTGIRHPVSLSHIGVTHDTLGKPYFKFHPELHTLVQNEGITRHHLSISDELNLACAFVILEK | 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): 14238
Sequence Length: 125
Subcellular Location: Cytoplasm
EC: 2.7.8.7
|
Q3JCY7 | MIVGIGTDIVQVSRMTALLGRYGERFPRRILTGDEFKKFSVSKQPAYFLAKRFAAKEAAAKALGTGFGSGLRPCHIGVGHTERGQPFLEWQGRANELVRILGVSRGLLSLADEKEYALAFVTLLAEREGAKPGLSLERALNSLKLSGNGNGVTD | 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): 16634
Sequence Length: 154
Subcellular Location: Cytoplasm
EC: 2.7.8.7
|
A6Q3W1 | MIGIDIVQIERIEQLIEKYGQKGLERFLLPQEMEVAKKPQTVAGFWAAKEAVAKALKTGIGKELGFHDIFIYKTEKGAPEFKLLNGKEQMFRIQQTALSISHDAGVAVAVAVIIRC | 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): 12899
Sequence Length: 116
Subcellular Location: Cytoplasm
EC: 2.7.8.7
|
Q9KPB6 | MIVGLGTDIAEIERVEKALARSGENFARRILTDSELEQFHASKQQGRFLAKRFAAKEAASKALGTGIAQGVTFHDFTISHDKLGKPLLILSGQAAELASQLQVENIHLSISDERHYAMATVILERR | 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): 13857
Sequence Length: 126
Subcellular Location: Cytoplasm
EC: 2.7.8.7
|
Q8D303 | MAIIGIGIDIVNLERINKIILCYGNKFVKKILSFNEKKKYYELKNKKKNISVNFLAKRLAAKEAASKAFGLGMKKGLYFSQFEVLNNNLGKPYFKFNNTAKNLIKALNITNIHLSLTDERKYACATVIFEDNRTNIILS | 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): 15871
Sequence Length: 139
Subcellular Location: Cytoplasm
EC: 2.7.8.7
|
A7IM60 | MIIGIGSDFSDARRIARSIERFGDRFLDRVFTPGERRKADQRKLRAETYAKRFAAKEACSKALGTGLSHGVFWRDMEVVNLPSGQPTLMLTGGAARRLAALVPDGYEPHIHLSLTDEGPLTAAYVIISAVPKTGV | 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): 14756
Sequence Length: 135
Subcellular Location: Cytoplasm
EC: 2.7.8.7
|
Q8KAN9 | MSAAEIKDKVYDIIVSKMGVNKDQIKPESKFADDLGADSLDTVELIMELENEFGVQIPDEDAEKIGTVQQAIDYIVNKKVS | 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... |
P80918 | MSDIEARVKKIIAEQLGVEESQVTNEKAFVADLGADSLDTVELVMALEDEFGIEIPDEDAEKITTVQNAIDYANTHQA | 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... |
B5Y7W4 | MEREKIFQELKNILKDTVTVEEEEITMESDLVNDLNLDSLDLVDLALSVEQVFGFEFSDEQLQQIKTVKDVVDIIESNLYTK | 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... |
Q1LKM2 | MDNIEQRVKKIVAEQLGVAEADIKNESSFVNDLGADSLDTVELVMALEDEFGMEIPDEEAEKITTVQQAIDYATAHVKA | 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... |
P80922 | MSTIEERVKKIVSEQLGVKEEEITNASSFVDDLGADSLDTVELVMALEEEFETEIPDEEAEKITTVQEAIDYVVSHQ | 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... |
Q6MAF8 | MSIEQEVIDIVVEQLGVDRDDVNSEKSFVEDLNADSLDLTELIMTFEERFECEISQEDAEKLKTVNDVISYLEKRKS | 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... |
A7FH28 | MSTIEERVKKIIVEQLGVKEDEVKNSASFVEDLGADSLDTVELVMALEEEFDTEIPDEEAEKITTVQAAIDFINANQQ | 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... |
Q6F7B8 | MNKKLEALFRENVKGKVALITGASSGIGLTIAKRIAAAGAHVLLVARTQETLEEVKAAIEQQGGQASIFPCDLTDMNAIDQLSQQIMASVDHVDFLINNAGRSIRRAVHESFDRFHDFERTMQLNYFGAVRLVLNLLPHMIKRKNGQIINISSIGVLANATRFSAYVASKAALDAFSRCLSAEVLKHKISITSIYMPLVRTPMIAPTKIYKYVPTLSPEEAADLIVYAIVKRPKRIATHLGRLASITYAIAPDINNILMSIGFNLFPSSTAALGEQEKLNLLQRAYARLFPGEHW | Function: Catalyzes the NADPH-dependent reduction of long chain acyl-CoA (with chain lengths of 14 to 22 carbons) to the corresponding aldehyde.
Catalytic Activity: CoA + hexadecanal + NADP(+) = H(+) + hexadecanoyl-CoA + NADPH
Sequence Mass (Da): 32529
Sequence Length: 295
EC: 1.2.1.n2
|
Q3C258 | MNQVMTIFLVLGVIVYSVESSSTPDGTWVKCRHDCFTKYKSCQMSDSCHDEQSCHQCHVKHTDCVNTGCP | Function: Toxin that is lethal to crab . It interacts with divalent metal ions (zinc and nickel) suggesting it may function as a metal ion chelator to regulate metal ion levels or as a metal ion transporter, or that its function is modulated by metal ions. Is not active against any of the voltage-gated potassium and so... |
P0DQJ2 | MSLILIFFAFTVLKSSKWICANRSVCPI | Function: Probable toxin expected to be employed in prey capture and/or defense against predators (based on its abundance in tentacles). Has only a weak affinity for lipid membranes . Shows moderate cytotoxic activity against breast cancer cell lines (MCF-7 and MDA-MB-231) .
PTM: May be N-glycosylated at Asn-22. Activi... |
Q336V5 | MCRFLISTPFSRRRGERKAEAGRMARSVSYVSAAKLLAMARSNPRVAIIDVRDEERSYQAHIGGSHHFSSRSFAARLPELARATGDKDTVVFHCALSKVRGPSCAKMFSDYLSETKEESGTKNIMVLERGFNGWELSGQPVCRCTDAPCKGTCSPEEPEL | Function: Possesses arsenate reductase activity in vitro. Catalyzes the reduction of arsenate [As(V)] to arsenite [As(III)]. May play a role in arsenic retention in roots.
Catalytic Activity: [glutaredoxin]-dithiol + arsenate + glutathione + H(+) = arsenite + glutathionyl-S-S-[glutaredoxin] + H2O
Sequence Mass (Da): 17... |
P27095 | MLKLAGKEDKKLKTTVFQDETRIFNPPKELVEKSIVMQWMKKKGFKTEKEMRAWCSSDEHYLEFWDEMAKTYVDWHKPYTKVMDDSEMPYFHWFTGGEINITYNAVDRHAKGAKKDKVAYIWIPEPTDQPVQKITYGDLYKEVNKFANGLKSLGLKKGDRVSIYMPMIPQLPIAMLACAKLGVSHIVVFSGFSSKGLMDRAAHCGSRAIITVDGFYRRGKPVPLKPNADEAAGGAPSVEKIIVYKRAGVDVSMKEGRDVWWHDLVKGQSEECEPVWVDPEHRLYILYTSGTTGKPKGIEHATGGNAVGPAQTLHWVFDLK... | 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, ... |
A0R5G1 | MCCAIWSASRAPACSASQLSSSHAVRPSVVPDANPRAAPRYSPDLRIQCTSGTPRPCGSSPLAIVTSRETARATTPSAVPNGASVSNSPCATAASTGAGALDPPVRSSISNSRRGPTSGSVRGRPRCSSSVRSAAASACSRASACIGARCHTVTNEVAPPSSASATRIAPAVTGSGSPSADSCTAPPSSTADARAPRSADSAAVCGQPRRLTLCRCARPSASRASSQAAATPGSSNSGARGSGRSVITSHASRPLIASSPTVQRNQTTVHQQTCEGPTCVQRSVTRLTAMSNPSHAEVPSAYPPPADFAANANATGELYA... | 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, ... |
P9WQD0 | MSESTPEVSSSYPPPAHFAEHANARAELYREAEEDRLAFWAKQANRLSWTTPFTEVLDWSGAPFAKWFVGGELNVAYNCVDRHVEAGHGDRVAIHWEGEPVGDRRTLTYSDLLAEVSKAANALTDLGLVAGDRVAIYLPLIPEAVIAMLACARLGIMHSVVFGGFTAAALQARIVDAQAKLLITADGQFRRGKPSPLKAAADEALAAIPDCSVEHVLVVRRTGIEMAWSEGRDLWWHHVVGSASPAHTPEPFDSEHPLFLLYTSGTTGKPKGIMHTSGGYLTQCCYTMRTIFDVKPDSDVFWCTADIGWVTGHTYGVYGP... | 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, ... |
Q82SI5 | MATIESILHENRIFPPASEFVRNANLSGREAYETLRQEAEHDYTGFWAKLAQQYIAWHKPFTRVLNDANPPFYKWFDDGELNISWNCLDRHLATQADKTAIIFESDAGEVNHCSYRELHRQVCHFANGLKSLGIRQGDRVVIYMPMRIEAVVAMQACARIGAIHSVVFGGFSAKSVYERIIDAGASAVITADEQIRGGRYHPLKATVDEALAMGDTATVHSVIVFRHTGTGITWQPERDHWWHDLIAGQPDECEPAWINAEHPLFTLYTSGSTGKPKGVQHSSAGYLLGAVTSMQWVFDYHADDVFWCTADVGWVTGHSY... | 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, ... |
Q93LL2 | TSGKVSIKWFEDGVLNVTESCLDRHLATRGDQVAIIWEGDDPNADSKVTYRELHARVCQLANAMRGMGVQKGDRVCIYLPMIEEAAVAMLACARIGAVHSIVFGGFSPDSLSSRIQDSDCVLLITADEGRRGGRKVPLKVNADEALKTCPSIRHVIVAKNTGGNVAMQEGRDHWWADACDNQPKTSTPEPMGAEDPLFILYTSGSTGKPKGVLHTTGGYLVWASFTHQNVFDYRDGEIYWCTADVGWVTGHTYIVYGPLANGATTLMFEGVPNYPTVSRFWEVIDKHQVNIFYTAPTAIRALMRDGEAPVKKTSRKSLRI... | 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, ... |
B2JD61 | MSAIESVLQERRVFQPSAEVAAQATVSGMDAYKALVAEAERDYEGFWGRLARETLSWNKPFTKVLDESNAPFYKWYDDGELNASYNSIDRHVEAGNGERVAIIFEADDGTITNVTYNDLLQRVSRFANALKQRGIKKGDRVVIYMPMSVEGIVAMQACARIGATHSVVFGGFSSKSLNERLVDVGAVALVTSDEQMRGGKALPLKNIADEALAMGGCEAVKSVIVYQRTGGKIGWDDKRDLWMHEITASESDHCPPEWVGAEHPLFILYTSGSTGKPKGVQHSTGGYLLWAAQTMKWTFDWKPTDVFWCTADIGWVTGHS... | 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, ... |
Q96WT2 | MVPISTRSEVQDGLIAQARSLITRIVHNSDDVYGFGTLSCTVYDTAWVALVTKHVNGIKHWLFPESFHYILASQCDDGTWCEDKTAQFDGVLNTIAGLLVLKRYRRDPLQLKVDNRDLDSRIKLATSALHSLLEEWDVSTTNNVGFEIIVPTMLDLLVQEDPSLSFELKGREALTEIREAKMNRFQPELLYQGKLMTLTHSLEALLGRIDYDNVARYTVKGSMFASPSSTAAYLMSASTWDDEAETYLRYTITASTGKGSGGVPGVFPTTYFEYTWILSTLFRAGFQSSELDSPELTAMTDTLLKAFKAFSGAIGLDSGI... | Cofactor: Binds 3 Mg(2+) ions per subunit.
Function: Aphidicolan-16-beta-ol synthase; part of the gene cluster that mediates the biosynthesis of aphidicolin, a specific inhibitor of eukaryotic DNA synthesis and DNA polymerase alpha . The geranylgeranyl pyrophosphate synthase GGS is required for supplying a sufficient a... |
P30170 | AGFAGDDAPRAVFPSIVGRPRHTGVMVGMGQKDAYVGDEAQSKRGILTLKYPIEHGIVSNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDHLMKILTERGYSFTTTAEREIVRDVK | 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... |
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