ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q13956 | MSDNTTLPAPASNQGPTTPRKGPPKFKQRQTRQFKSKPPKKGVKGFGDDIPGMEGLGTDITVICPWEAFSHLELHELAQFGII | Function: Participates in processes of transmission and amplification of the visual signal. cGMP-PDEs are the effector molecules in G-protein-mediated phototransduction in vertebrate rods and cones.
Catalytic Activity: 3',5'-cyclic GMP + H2O = GMP + H(+)
Sequence Mass (Da): 9074
Sequence Length: 83
Domain: The C-termin... |
P61249 | MSDSPSLSPPAPSQGPTTPRKGPPKFKQRQTRQFKSKPPKKGVKGFGDDIPGMEGLGTDITVICPWEAFSHLELHELAQFGII | Function: Participates in processes of transmission and amplification of the visual signal. cGMP-PDEs are the effector molecules in G-protein-mediated phototransduction in vertebrate rods and cones.
Catalytic Activity: 3',5'-cyclic GMP + H2O = GMP + H(+)
Sequence Mass (Da): 9028
Sequence Length: 83
Domain: The C-termin... |
Q15003 | MGPPGPALPATMNNSSSETRGHPHSASSPSERVFPMPLPRKAPLNIPGTPVLEDFPQNDDEKERLQRRRSRVFDLQFSTDSPRLLASPSSRSIDISATIPKFTNTQITEHYSTCIKLSTENKITTKNAFGLHLIDFMSEILKQKDTEPTNFKVAAGTLDASTKIYAVRVDAVHADVYRVLGGLGKDAPSLEEVEGHVADGSATEMGTTKKAVKPKKKHLHRTIEQNINNLNVSEADRKCEIDPMFQKTAASFDECSTAGVFLSTLHCQDYRSELLFPSDVQTLSTGEPLELPELGCVEMTDLKAPLQQCAEDRQICPSLA... | Function: Regulatory subunit of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted f... |
Q9GYL2 | MIIKVFLRLLLLCAHIVCIDGKLEIRPVVSGVRIESDVDASGFLGYGDAGELLVEANTEVDLVIFGHGLENVEMVTFTDSVCVTSEFNVSESTFYIHKDMKIVFKYAFVAWPQPWRICLKSECHGLIQIDDDRTWIQAVQSTHETFMPVWAQCAILCLLFSISALCSGLTLGLMALTPQELSILMKSGSQREKKHAAAIYPIRCHGNRLLCTVIIMNVIVNTGITLLFDDLAEGLIAFVASTVGIVVFGEILPQSICVKYGLAVGANTIFITKFFMFLLFPITWPLGKILDKYAGVDIDVVNRSRMVEMLKMNMENDACD... | Function: Probable metal transporter. Probably acts redundantly with the other metal transport proteins cnnm-1, cnnm-3, cnnm-4 and cnnm-5 to regulate Mg(2+) homeostasis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 85012
Sequence Length: 760
Subcellular Location: Cell membrane
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Q3TWN3 | MIGCGACEPEVKMAGGQAAAALPTWKMAARRSLSARGRGVLQAAAGRLLPLLLLSCCWGAGGCTAAGENEETVIIGLRLEDTNDVSFMEGGALRVSERTRVKLRVYGQNINNETWSRIAFTEHERRRHTPSERGLGGPAPPEPDSGPQRCGIRTSDIIILPHIILNRRTSGIIEIEIKPLRKMEKSKSYYLCTSLSTPALGAGGSGSASGTVGGKGGAGVAGLPPPPWAETTWIYHDGEDTKMIVGEEKKFLLPFWLQVIFISLLLCLSGMFSGLNLGLMALDPMELRIVQNCGTEKEKNYAKRIEPVRRQGNYLLCSLL... | Function: Divalent metal cation transporter. Mediates transport of divalent metal cations in an order of Mg(2+) > Co(2+) > Mn(2+) > Sr(2+) > Ba(2+) > Cu(2+) > Fe(2+).
PTM: The N-terminus is cleaved within the endoplasmic reticulum. The signal peptidase complex seems to be involved in the processing, but the exact cleav... |
A0A131MCZ8 | MSKTPWALGLLIFLLTFTSPLSSSPVRSTDNSTSSKGLLNVNSSVILEPSILPSSASKPESLHLSKVRVSGLRLEAHASSTENIVLGHNKKHNVVVVPNKNVRVVLFGQNFQDIGALTFTADGSCKDLAHFFEADFSSMTPIRVVVEMSFPKTTESKDSFKLCVSEKFYANPQFVIVEDPFTMVTTEIPPVDEYMPKWLSWICLLILLCFSGLFSGLNLGLMTLSPYELQLYIASGTEQEKRDAGRILPIRKKGNQLLCTLLIGNVVVNVGVSLLMDQLVGSGFAVLVAATSCIVVFGEIIPQALCVKLGLPIGARTIPI... | Function: Probable metal transporter. Probably acts redundantly with the other metal transport proteins cnnm-1, cnnm-2, cnnm-4 and cnnm-5 to regulate Mg(2+) homeostasis. Promotes postembryonic gonad development by regulating Mg(2+) levels, probably via AMPK signaling.
Location Topology: Multi-pass membrane protein
Sequ... |
Q8NE01 | MAAAVAAAGRLGWLFAALCLGNAAGEAAPGPRVLGFCLEEDGAAGAGWVRGGAARDTPDATFLLRLFGPGFANSSWSWVAPEGAGCREEAASPAGEWRALLRLRLRAEAVRPHSALLAVRVEPGGGAAEEAAPPWALGLGAAGLLALAALARGLQLSALALAPAEVQVLRESGSEAERAAARRLEPARRWAGCALGALLLLASLAQAALAVLLYRAAGQRAVPAVLGSAGLVFLVGEVVPAAVSGRWTLALAPRALGLSRLAVLLTLPVALPVGQLLELAARPGRLRERVLELARGGGDPYSDLSKGVLRCRTVEDVLTP... | Function: Probable metal transporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 76119
Sequence Length: 707
Subcellular Location: Cell membrane
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Q32NY4 | MAAAAAAVVGWLGWVLAAFCLGSTAGEAAPAPGAGLLNFCTEEDSAPGAGSLRGRAAPEATLCLRLFCSGLANSSWTWVAAEGAGCPEGGRATEPEEAAAPTGEWRALLRLRAEAGHPRSALLAVRVEPGGGAAEEAAPPWALGLGAAGLLALAAVARGLQLSALALAPAEVQVLRESGSEAERAAARRLEPARRWAGCALGALLLLASLAQAALAVLLYGAAGQRAVPAVLGCAGLVFLVGEVLPAAVSGRWALALAPRALGLSRLAVLLTLPVALPVGQLLELAARPGRLRERVLELARGGGDPYSDLSKGVLRSRTV... | Function: Probable metal transporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 76279
Sequence Length: 713
Subcellular Location: Cell membrane
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Q17586 | MELYAAGRYDSEPFKMNEHDIIQLYGEDVQYVKNAFLSSDSTCNNNVYSLEEHELDDDKKNLSGVLVEYKIKISLLQSSDGVKHLFFCTNPKSVDIARMLEIPEGKDKTRVYFMMPLLVLCLGLSATFSGLNLAIMSFSINDLKLIQESDSDKLMKQRAMDVMRLRRNSNFVLVTIIFGNCFCNISITLLMNYFAEFYGFGGFIFVELISTALLLIFTEILPSLIFTKNALAIASRLQYFVIFTMCITSPISYPLAMLLNIILGKENADDSAPLDLDALQIDELEDEEAADGNNFHEMMSVVKKTIKLREKLASDVMTEI... | Function: Probable metal transporter. Probably acts redundantly with the other metal transport proteins cnnm-1, cnnm-2, cnnm-3 and cnnm-5 to regulate Mg(2+) homeostasis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 53072
Sequence Length: 467
Subcellular Location: Cell membrane
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Q6P4Q7 | MAPVGGGGRPVGGPARGRLLLAAPVLLVLLWALGARGQGSPQQGTIVGMRLASCNKSCGTNPDGIIFVSEGSTVNLRLYGYSLGNISSNLISFTEVDDAETLHKSTSCLELTKDLVVQQLVNVSRGNTSGVLVVLTKFLRRSESMKLYALCTRAQPDGPWLKWTDKDSLLFMVEEPGRFLPLWLHILLITVLLVLSGIFSGLNLGLMALDPMELRIVQNCGTEKERRYARKIEPIRRKGNYLLCSLLLGNVLVNTSLTILLDNLIGSGLMAVASSTIGIVIFGEILPQALCSRHGLAVGANTILLTKFFMLLTFPLSFPI... | Function: Probable metal transporter. The interaction with the metal ion chaperone COX11 suggests that it may play a role in sensory neuron functions (By similarity). May play a role in biomineralization and retinal function.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 86607
Sequence Length: 775
... |
Q69ZF7 | MAPGGGGGRRDGWPARGRLLLAALLLLWTRAASGQSSPQQSVILGMRLASCNKSCGMNPDGIIFVSEGSTVNLRLYGHSLGDISSNLISFTEVDDAEAVHNSTNCLELTKDLVVQRLVNVSRGNTSGMLVVITKFLRRSENMKLYALCTRPRADGPWTRWTDKDSLLFMVEEHGRFLPLWLHILLVMVLLVLSGIFSGLNLGLMALDPMELRIVQNCGTEKERKYARKIEPIRRKGNYLLCSLLLGNVLVNTSLTILLDNLIGSGIMAVASSTIGIVIFGEILPQALCSRHGLAVGANTIVLTKVFMLLTFPLSFPISKL... | Function: Probable metal transporter. The interaction with the metal ion chaperone COX11 suggests that it may play a role in sensory neuron functions (By similarity). May play a role in biomineralization and retinal function.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 86626
Sequence Length: 771
... |
A0JPA0 | MAASAGCYYGVLGCALSLLLLPPLSRCAARTDSPLPEELPLILGFRLERSDRHAALSPDGELEVVEGSRLELRVYGLHLREDSGHILAFTEYSPGSQDNRSCLEDSRDLVLTRLNVSDDGFGAAGAAIVRLDVLPLRKSQSSRVYVLCTSRGPGLPWKLHTGPDGRLRVLEEEKPLLPIWLQACIIAVLLTLSGIFSGLNLGLMALDPMELRVVQRCGTEKEKRYASKIEPVRRKGNYLLCSLLLGNVLVNTTLTALLDELIGSGLAAVLASTTGIVVLGEIVPQALCSRHGLAVGANTLWLTRIFMLLTFPVAYPVSRL... | Function: Probable metal transporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 85402
Sequence Length: 769
Subcellular Location: Cell membrane
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G5ED05 | MSLFLFAIFQLALGSPGAPNGPNVPLQLTGVRRGLDHVQKLPSEAFSFKLFGKNLAEDGYYFTTATRCEDSHLSTVSTVRATVKESYCSYAILSVPEGLPFNVSTSVYHLCHKNATIYTQKFLVVHEKKAAAAKYMGDEIVFCFFCILMSAYASGMTLGYMKFSMIDLNTMLKIAEGDAAKKRVRRIMHFRRRSTQLVVTFSLFSSVFTVLFTTTCEKMLHGVSNEDVLKMAVPALICLIFAEMIPQAVCNSKFGFNLAASLWFVTVIIFFVTLPIAYPASLVLGRFLKRDVREVMTPEEKTCLLRSMAQNEREKTILEN... | Function: Probable metal transporter. Probably acts redundantly with the other metal transport proteins cnnm-1, cnnm-2, cnnm-3 and cnnm-4 to regulate Mg(2+) homeostasis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 81104
Sequence Length: 722
Subcellular Location: Cell membrane
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Q39054 | MEGQGCCGGGGGKTEMIPTEEALRIVFGVSKRLPPVIVSLYEALGKVLAEDIRAPDPLPPYPASVKDGYAVVASDGPGEYPVITESRAGNDGLGVTVTPGTVAYVTTGGPIPDGADAVVQVEDTKVIGDVSTESKRVKILIQTKKGTDIRRVGCDIEKDATVLTTGERIGASEIGLLATAGVTMVKVYPMPIVAILSTGDELVEPTAGTLGRGQIRDSNRAMLVAAVMQQQCKVVDLGIVRDDRKELEKVLDEAVSSGVDIILTSGGVSMGDRDFVKPLLEEKGKVYFSKVLMKPGKPLTFAEIRAKPTESMLGKTVLAF... | Function: Catalyzes two steps in the biosynthesis of the molybdenum cofactor. In the first step, molybdopterin is adenylated. Subsequently, molybdate is inserted into adenylated molybdopterin and AMP is released.
Catalytic Activity: adenylyl-molybdopterin + H(+) + molybdate = AMP + H2O + Mo-molybdopterin
Sequence Mass ... |
Q39055 | MRRCFSKITDCHLGFKNSNFLLVGSEVGSGSVTRTITTTTSERLFSSSYAAHQVDQIKDNPVSDMLIDKFGRLHTYLRISLTERCNLRCQYCMPSEGVELTPKPQLLSQSEIVRLAGLFVSAGVNKIRLTGGEPTVRKDIEEICLQLSSLKGLKNLAITTNGITLAKKLPRLKECGLDSLNISLDTLVPAKFEFLTRRKGHDRVMKSIDTAIELGYNPVKVNCVIMRGLNDDEICDFVELTRDKPINVRFIEFMPFDGNVWNVKKLVPYAEVMDKVVKRFPSIKRMQDHPTETAKNFTIDGHCGSVSFITSMTEHFCAGC... | Cofactor: Binds 2 [4Fe-4S] clusters. Binds 1 [4Fe-4S] cluster coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine and 1 [4Fe-4S] cluster coordinated with 3 cysteines and the GTP-derived substrate.
Function: Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate.
Ca... |
Q39056 | MISTLRRAVFLRRFPAVVSPIKRAFSSRIDDEFDPQIMNINELNQEMQSIFGQEPSPDGPGTMDFSELKSSKIEPLRSKNIDFRQQIEYHKSTHSSKNDSQAIEQYAKVASDMSKLTHVGIAGEAQMVDVSSKDNSKRTALACCKVILGKRVFDLVLANQMGKGDVLGVAKIAGINGAKQTSSLIPLCHNIALTHVRVDLRLNPEDFSVDIEGEASCTGKTGVEMEAMTAVSVAGLTVYDMCKAASKDISITDVRLERKTGGKSGSWSRL | Function: Catalyzes the conversion of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP).
Catalytic Activity: (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate = cyclic pyranopterin phosphate + diphosphate
Sequence Mass (Da): 29513
Sequence Length: 270
Pathway: Cofactor ... |
P20785 | MGLHDSFLALLLLLGGAWAQQAEINARVLRAQDCPVDLFFVLDTSESVALRVKPFGDLVAQVKDFTNRFIDKLTERYFRCDRFLAWNAGALHYSDSVVIIKDLTAMPSGRAELKNSVSAINYIGKGTHTDCAIKQGIERLLLGGSHLKENKYLIVVTDGHPLEGYKEPCGGLDDAANEAKHLGIKVFSVAISPHHLDQRLNIIATDHAYRRNFTATSLKPTRDLDVEETINNIIEMIKDNMEQSCCSFECHPPRGPPGPPGDPGHEGERGKPGLPGQKGDAGDPGRPGDMGPVGYQGMKGDKGSRGEKGSRGAKGAKGEK... | Function: Collagen VI acts as a cell-binding protein.
PTM: Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.
Sequence Mass (Da): 107984
Sequence Length: 1019
Subcellular Location: Secreted
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P15988 | MSRRTAEMFQQAFLSTLLCVALVPLHAQFDDEPVTSCTEKTDCPISVYFVIDTSESIALQTVPIQSLVDQIKQFIPRFIEKLENEVYQNQVSITWMFGGLHYSDVVEIYSPLTRSKDTYLTKLRAIRYLGRGTFTDCAISNMTQQFQSQTARDVKFAVVITDGHVTGSPCGGMKMQAERARDMGIKLFAVAPSEDVYEQGLREIASPPHDLYRSNYTITPKDALHIDENTIERIIKAMKHEAYAECYKMTCLEIAGPAGPKGYRGQKGAKGNMGEPGSPGLKGRQGDPGIEGPIGYPGPKGVPGLKGEKGEIGSDGRRGA... | Function: Collagen VI acts as a cell-binding protein.
PTM: Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.
Sequence Mass (Da): 109177
Sequence Length: 1022
Subcellular Location: Secreted
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P12110 | MLQGTCSVLLLWGILGAIQAQQQEVISPDTTERNNNCPEKTDCPIHVYFVLDTSESVTMQSPTDILLFHMKQFVPQFISQLQNEFYLDQVALSWRYGGLHFSDQVEVFSPPGSDRASFIKNLQGISSFRRGTFTDCALANMTEQIRQDRSKGTVHFAVVITDGHVTGSPCGGIKLQAERAREEGIRLFAVAPNQNLKEQGLRDIASTPHELYRNDYATMLPDSTEIDQDTINRIIKVMKHEAYGECYKVSCLEIPGPSGPKGYRGQKGAKGNMGEPGEPGQKGRQGDPGIEGPIGFPGPKGVPGFKGEKGEFGADGRKGA... | Function: Collagen VI acts as a cell-binding protein.
PTM: Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 108579
Sequence Length: 1019
Subcellular Location: Secreted
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Q7MGQ9 | MSPFLSFSRATWSELRNSVPMTLSEEDLKALQGINENLTMQEAVEVYLPLSRLLNLYVQARQSRNSVLHQFLNNDEHAPPFVIGIAGSVAVGKSTTARVLCALLSRWENHPKVELVTTDGFLYPKKMLNQRGIMHKKGFPESYDMKKLVQFVSDVKAGKPELEVPVYSHITYDITEEVKRVDRPDVLIIEGLNVLQSGMDYPHDPHRVFVSDFLDFSIYVDAESNTIEQWYVERFLKFRKGAFTQPGSYFSHYTQLSEQQAIEKAQQIWRDINGINLTENILPTKERAQLILRKGQNHLVEEILLRK | Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
Sequence Mass (Da): 35338
Sequence Length: 307
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.33
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Q5E8M6 | MASLAGKRILLGISGGIAAYKCAELTRRLIERGAEVRVVMTKAAKEFITPLTMQAVSGHPVADSLLDPAAEASMGHIELAKWADIVLLAPATADLIARMAAGMGNDLLSTLVLATDSPVAVSPAMNQQMYSNIATQENIATLARRGMHIWGPAAGQQACGDVGMGRMLEPMELVHLCEDFFQANSCEQAEADEKPLKGQSLLITAGPTREAIDPVRYISNHSSGKMGFAIAEAAAQLGANVTLVSGPVNLATPENVKRIDIESAEQMHGAVMKNAQSHSIFIACAAVADFKLSQVATQKLKKTADEDGMTLHMVKNPDIV... | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes two sequential steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4'-phosphopantothenate to form 4-phosphopantothenoylcysteine. In the second step the latter compound is decarboxylated to form 4'-phosphopantotheine.
Catalytic Activ... |
Q8KDS9 | MSKKAIYPGTFDPFTNGHLDVLERALNIFEHVDVVLAENSQKQTLFSVEERFDMVREVVRDLPNVSVDVLREGLLADYARQAGASAIVRGVRQVKDFEYEFQMSLLNRHLYPEVTTVFLMPNVKYTYVASTIIREVSMLGGDVSKFVHPYVLDQLSRKRAERRAH | Function: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
Catalytic Activity: (R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA + diphosphate
Sequence Mass (Da): 18964
Sequence Length: 165
Pathway: Cofactor biosynthesis; coenzyme A bios... |
Q1QTC8 | MNIVVYPGTFDPVTNGHYDLIERASRMFDKVVVAVAASPRKQPTLSLETRVALIEEVTADLDNVTVTGFSCLLTQLLAQQNARIILRGLRAVSDFEYELQLANMNRAQAPDVESLFLTPEVENSYISSTIVREIARLGGDVSKLVHPCVVDALSRHFAQDPSSPKTQ | Function: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
Catalytic Activity: (R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA + diphosphate
Sequence Mass (Da): 18414
Sequence Length: 167
Pathway: Cofactor biosynthesis; coenzyme A bios... |
A5CQP6 | MQRIAVVPGSFDPVTLGHLDVIRRAARLYDELVVLVVHNPGKTPMLPLGERVALIERVIRDAGLPDTVRVDSWGAGLLVDYCRQVGATVLVKGVRSQLDVTYETPMALVNRDLADVETVLLLPDPAHAHVSSSLVRQVEALGGDVTPYVPAAVADALAVRRAG | Function: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
Catalytic Activity: (R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA + diphosphate
Sequence Mass (Da): 17472
Sequence Length: 163
Pathway: Cofactor biosynthesis; coenzyme A bios... |
Q97IB2 | MKVAVYPGSFDPITNGHLDIISRASKVFDKVIVGVLINPEKKGMFSVDERVDLIKRVIKPFNNVSVQSFSGLLVNFMENNDSNVMIRGLRSVGDFEYELQTSLMNKKLNPNVETVFMMTSLEFSFLSSTAIKQVAVFGGCIKELVPDEIIDDVLRKAKEFN | Function: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
Catalytic Activity: (R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA + diphosphate
Sequence Mass (Da): 18056
Sequence Length: 161
Pathway: Cofactor biosynthesis; coenzyme A bios... |
O27918 | MKRKYSLVAVGGTFDRFHKGHRRLLDEAFRVGETVMIGVTSDEFAAAKGEGIEPCSVRMKNLEEYLRDKDADYHVMRLDDPYGTTVTDEAFEAIVVSRETEPVAREINAIRRNRGFRELDIITIDMVNADDGIPISSTRIRRGEIDPMGHIIKRIRGALRRRRE | Function: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
Catalytic Activity: (R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA + diphosphate
Sequence Mass (Da): 18791
Sequence Length: 164
Pathway: Cofactor biosynthesis; coenzyme A bios... |
C5CAE0 | MRRAVCPGSFDPLHKGHVEVIARAANLFEEVVVAVSANPAKTYRFSVDERIAMIEATVSSLAGVAVRPMGPGLLAEFCRQIGADAIVKGLRGGADLEFEAPMAAMNRHLTGVETVYLPADARYTHVSSSLIKEVHGLGGDVAEFVPAAVLRGLDGGA | Function: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
Catalytic Activity: (R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA + diphosphate
Sequence Mass (Da): 16497
Sequence Length: 157
Pathway: Cofactor biosynthesis; coenzyme A bios... |
B1MDL6 | MTGAVCPGSFDPVTLGHLDVFERAAAQFDEVIVAVLINPNKAGMFTVDERIEMIRESTADLPNLRVESGQGLLVDFVRERGLNAIVKGLRTGTDFEYELQMAQMNKHIAGVDTFFVATAPAYSFVSSSLAKEVATYGGDVSALLPASVHQRLLGKLRGQAQ | Function: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
Catalytic Activity: (R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA + diphosphate
Sequence Mass (Da): 17373
Sequence Length: 161
Pathway: Cofactor biosynthesis; coenzyme A bios... |
O69466 | MSSVVCPGSFDPVTLGHIDVFERAAAQFDEVVVAILINPVKKGMFDLDERIAMINESTMHLPNLRVEAGEGLVVALVRSRGMTAIVKGLRTGVDFEYELQMAQMNKHIAGVDTFFVATAPRYSFVSSSLVKEVAMLGGDVSELLPESVNRRFREKMSGTS | Function: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
Catalytic Activity: (R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA + diphosphate
Sequence Mass (Da): 17496
Sequence Length: 160
Pathway: Cofactor biosynthesis; coenzyme A bios... |
Q6MTX3 | MKTAIYPGSFNPFHNGHLNILKKAILLFDKVYVVVSKNINKSLDPDLQSRVKNIKNLIRDFNNVEIIINENKLTTTIAKELNASFIIRGLRSQTDFEYEIKYYDGFKSLYPNIEVIYFISDYDKRSLSSTILREIEFYKK | Function: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
Catalytic Activity: (R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA + diphosphate
Sequence Mass (Da): 16437
Sequence Length: 140
Pathway: Cofactor biosynthesis; coenzyme A bios... |
Q98RB3 | MSMNKKIAIFPGSFDPFHNGHKHILNKALALFDLVYLVITINPDKITKTSFDQRKTLLENEILDFDKSRVQVLVNKDSLTAEIAKKLGAKFIIRSARNDIDYQYELVLAAGNKKINNEVETILIFPDYDKIEINSTLIRHQKFIENLKK | Function: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
Catalytic Activity: (R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA + diphosphate
Sequence Mass (Da): 17190
Sequence Length: 149
Pathway: Cofactor biosynthesis; coenzyme A bios... |
Q9ZBR1 | MRRAVCPGSFDPITNGHLDIIARASSLYDEVYVAVMINQAKKGLFEIEERIDLIRRVTAEYGNVRVESFHGLLVDFCKQREIPAIVKGLRAVSDFDYELQMAQMNNGLSGVETLFIPTNPTYSFLSSSLVKEVATWGGDVAHLVPPLVLEALTERLRNR | Function: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
Catalytic Activity: (R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA + diphosphate
Sequence Mass (Da): 17813
Sequence Length: 159
Pathway: Cofactor biosynthesis; coenzyme A bios... |
B1VYY6 | MRRAVCPGSFDPITNGHLDIIGRASKLYDVVHVAVMINQSKKGLFTVDERIELIREVTADFGNVEVESFHGLLVDFCKQREIPAIVKGLRAVSDFDYELQMAQMNNGLSGVETLFVPTNPTYSFLSSSLVKEVATWGGDVSHLLPPTVHEALVKRLGER | Function: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
Catalytic Activity: (R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA + diphosphate
Sequence Mass (Da): 17614
Sequence Length: 159
Pathway: Cofactor biosynthesis; coenzyme A bios... |
Q8DVH2 | MSDRIGLFAGSFDPVTNGHVDIIRRASGLFDKLYVGLFYNKDKTGLFEPARRQIMLKEALGDLKNVEVVAARDSLAVDIARQHQVTHLVRGLRNAQDLEYEANLAFFNSQLAKEIETVFLLTALDYRYFSSSRIRELIHFGADISPYVPQGVVKEVGKKCENKQKI | Function: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
Catalytic Activity: (R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA + diphosphate
Sequence Mass (Da): 18777
Sequence Length: 166
Pathway: Cofactor biosynthesis; coenzyme A bios... |
P63821 | MLTKIGLYTGSFDPVTNGHLDIVKRASGLFDQIYVGIFDNPTKKSYFKLEVRKAMLTQALADFTNVIVVTSHERLAIDVAKELRVTHLIRGLRNATDFEYEENLEYFNHLLAPNIETVYLISRNKWQALSSSRVRELIHFQSSLEGLVPQSVIAQVEKMNEKT | Function: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
Catalytic Activity: (R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA + diphosphate
Sequence Mass (Da): 18629
Sequence Length: 163
Pathway: Cofactor biosynthesis; coenzyme A bios... |
Q8KD46 | MKARLPLLVGVTGGIGSGKSTVCAMLAEMGCELFEADRIAKELQVEDPEVIRGIEKLFGPDVYSRDASGKLLIDRKAIAAIVFSEPEKLAALNRLIHPKVREAFVNEVKRCAREGKRILCKEAAILFEAGADRDLDRIIVVAANDGLRLARAVARGLACEEARKRMQAQWPQEKLVERAHYVIFNDGTLDELRSQVEQVYQSLLTVVE | Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
Sequence Mass (Da): 23057
Sequence Length: 208
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Subcellul... |
Q97K22 | MLKIGLTGGIGSGKSTISRIFKERQILVVDADEVSKEVLKEHPEILTAVRNKFGDNFFDENGEFTRREFGNFIFNSEPHRKEYENIIMPYIKKDIVRTMKLYESLNENVCVLDAPTLIENDIYKDMDINILVWVDKATQIKRVQKRDGMSEDEVIMRINSQMSLEEKKKYVDFIIDNSGEFENTIKQIDRIMQSVSIMKGK | Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
Sequence Mass (Da): 23395
Sequence Length: 201
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Subcellul... |
Q8XIX0 | MIKVGLTGGICSGKSTISSMIKEAGIPVIDADIIAREVLEKYPDILLRVRATFGGHFFDWRGDFRRREFGNHIFRFPKERIKYEEIIMPYIKEEIEIKLKEYEKINTKLVVVDGATLIENDMHKDMDMVVLVWVDKSSQIERMGFRDKLSKGEAINRINSQLSLERKKDYANIIIDNSGNLIKTKEQIDDLLEFFTLYQ | Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
Sequence Mass (Da): 23152
Sequence Length: 199
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Subcellul... |
Q892J5 | MKEKIGMMLSDVDLEWLKKKYCIKNKGKFLKIGLTGGIGSGKSTISKMFKNMGIDVIDADKIAREVLEKYPPILEYIEENFGEQYIDEFGNLNRREFGNHIFSISKKEREKYENIIIPYIKLEIENQFKLYEKIGKKVCLLDAPLLIEQDMQKDLDFTVLSWVNKETQIKRVGIRDNLSEDEILNRIEAQISLDKKRELVDFIIDNSNTIEETRVQVEKLFQFINCL | Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
Sequence Mass (Da): 26611
Sequence Length: 227
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Subcellul... |
Q47VS4 | MSKLVIGLTGGIGSGKTTITNYFLALGVEIIDADIIAREVVAINSPALKAIAKHFGDDYIQADGQLNRPLLRNRIFSNKADKLWLNKLLHPLIRVNIVTQTKEAKSPYCILVAPLLIENNLLELVDRVLIVDVNESTQITRTLVRDSSSEQEIKAIIASQTSRAARVNVADDIINNDDSPLSEIKEAVLSLDKKYLTLTKMV | Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
Sequence Mass (Da): 22260
Sequence Length: 202
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Subcellul... |
P58101 | MKIIGLIGGIGSGKTTVAQLFVDEGFPLVD | Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
Sequence Mass (Da): 3077
Sequence Length: 30
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Subcellular... |
Q8FPN2 | MLRIGLTGGIGSGKSTVADLLSAEGFLIIDADAIARDIVEPGQPALAELVEAFGEDILNPDGTLNRPGLAAKAFVSSEQTALLNSITHPRIAEETARRFAEAEAAGTKAAVYDMPLLVDKGLDRTMDLVVVVDVEEDERVRRLVAKRGLEEDDVRRRIASQVPDEIRLKAADIVIDNNGPVENLRAQADRLIAEILTRIK | Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
Sequence Mass (Da): 21602
Sequence Length: 200
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Subcellul... |
P58897 | MLRIGLTGGIGSGKSTVADLLSSEGFLIVDADQVARDIVEPGQPALAELAEAFGQDILKPDGTLDRAGLAAKAFVSEEQTALLNAITHPRIAEESARRFNEAEDQGAKVAVYDMPLLVEKGLDRKMDLVVVVDVDVEERVRRLVEKRGLTEDDVRRRIASQVPDDVRLKAADIVVDNNGTLEDLHAEASKLIAEILSRVN | Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
Sequence Mass (Da): 21663
Sequence Length: 200
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Subcellul... |
Q83F01 | MLRIGLTGGIGSGKSTVANYFAELGAPVIDADQIAHEITKPDQAAFKQIINHFGNAVLTKGKFLNRTKLRELIFENPDDRQWLENLLHPLIIAKMKTQLKKIKAPYCILAIPLLAEASQSVDFIDRILVVDAPETLQIQRTKSRDQLSDQQIQLILQSQSPREKRLAIADDVIVNDQTIPILRKAVFQLHCKYLQIAQT | Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
Sequence Mass (Da): 22388
Sequence Length: 199
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Subcellul... |
Q46X10 | MLEIGLTGGIGSGKTRVADMFAARGAAIIDTDLLAHEITAPGGQAIPALVEAFGPQCLRPDGAMDRDAMRAVVFADPAAKARLEGITHPLIRELTTSRAAEIAHAGEHPYLIYVVPLLVESGAWLNRVGRVLVVDCSEDTQIARVMSRNGFSREQVLAIMAKQATRAQRLAVAHDVIDNDGPVEALTAQVDQLDRTYRALSAAGVTQA | Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
Sequence Mass (Da): 22088
Sequence Length: 208
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Subcellul... |
Q6A9M5 | MRRTVIGDETTARDVARADWVAGAGGVVRVGLTGGIASGKSTVSQMLGERGAVIIDYDRLSRDVVAVGTQGLAQVVEAFGREVLVADGSLNRSALGSIVFADLQARRRLEAIIHPLVEEAAHRVDEEARAADGLVVVVHDIPLLVETGRADEFDVVMVTDVDPAEQVRRVVERDGCSQADAWARIHAQASREEHLAVADVIIDTSVPLEDLPEQIDRVWSRIAGALRFDRR | Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
Sequence Mass (Da): 24972
Sequence Length: 231
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Subcellul... |
Q3Z6W5 | MKIVGITGGIGSGKTTVCRYLKELGVNIIDADEIGHRVLQNKGIRTRITDVFGNEVMNPDGSINRKILGELVFGYPERLEHLNKITHPLIEQAIASLLEEYRQKGIKAVAIEAPLLVEAGWLKLVNEVWLITAPKESIFKRLRNRMGLSREQVMARIQSQATDNERLKYASIVINNNCRFEDLKSCVQLLAKERLELA | Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
Sequence Mass (Da): 22320
Sequence Length: 198
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Subcellul... |
Q9RT73 | MTRSPAPSSPTHPRRLGLTGSIGAGKSTVARLLRERGLTVLDADAEARWVTEQPEVLTELNEAFPGVVTGGTLDRAGLAARVFSDPAQVARLNAITHPRVRARMEALEAAATARGEHWVVQDIPLLFEGGLERGMDAVLVVDAPLELRLERALARGGLTREDILARDARQLSSEEKRRRATIVLDNSGPLEALEGQLDAALRQLEIT | Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
Sequence Mass (Da): 22374
Sequence Length: 207
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Subcellul... |
Q30NW0 | MAFKYAIALSGGIATGKSTVASLLSLNGMRVIDADAISHDILDASSLWVRENFGDEFVDGVSVNRSKLGTLIFSDNIAKKKLESFLHPKIRAEIEQRSIKQDSFMFPYLIDIPLFFESGAYDIKESVVVYVPKELQLERFIKRNGFSREESLRRIESQMDIEEKKKRATWVIDNSGDLKHLQRECEEFVEKIKAKYLEKK | Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
Sequence Mass (Da): 22929
Sequence Length: 200
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Subcellul... |
Q67R57 | MRIIGLTGSIASGKSTVSAMLREPGAAVIDADAIVHHLQLPGTPVFESIVREFGPGVVRPDGSLDRQALGRIVFADPGRRRALEAIVHPAVRAEIWRQVEQYRREGRPAVVLDVPLLYESGWDRQVDEVWVVWVDAETQKARLIARSGLSPEEAEARIAAQMSLDEKARRADRIIDNRGSLDRTRAQVEAAWRAACGGEGGEPAAGSSAHHGAGSVDPGAGPCDGPGAAPEAERRGGDR | Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
Sequence Mass (Da): 25541
Sequence Length: 239
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Subcellul... |
Q2LUP6 | MPEGVPCGRRGAMLNVGLTGSISCGKSTVARMLEGKGAFIIDFDRLAHDVEEPDKPAWRGIVDTFGPDVLREDRTIDRARLGTLVFADRRKLEKLNEIVHPAVFEAWRRSVEEIRGVRPDAIVVSDFPLLIELGKQNDYDVILLVYIPPQEQIRRLILRNGYSPEEAIQRVNSQMSIEDKIDFADIIVNNAGPREQTQAQIDKIWTQLLKKERLQRKSAASSFQTGTIHKEREVG | Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
Sequence Mass (Da): 26585
Sequence Length: 235
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Subcellul... |
Q3A6J1 | MLVLGLTGGIGSGKSIVAEMFRTLGAKVVSADDLARMIVQPGSPTLARIARRFGAEVLCEGGALNRAWLAKKIFSDPQARLDLDRITHPAIAELARRRFAALAQASATLVVYDAPLLFEAGADTQVDAVVVVSVAEEVQLQRLMLRDGLDEQAARSRMDSQMPLDEKLARADYVIDNNGSLEQTRDQVVALMARLVPGMKGPDPHASGSAG | Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
Sequence Mass (Da): 22519
Sequence Length: 211
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Subcellul... |
Q31RL4 | MGAPNHVNFVRRRIGLTGGIATGKSTVADYLRDRYQLPILDADRYAREVVAVGSPVLQVIRDRYGASILLADGQLDRQKLGSIIFADPAERQWLEQQTHPAIRACFERDLAQLESDPIVVLVIPLLFEAGLQDWVEQIWVVACPLEQQRDRLIHRDRLTPAAAEQRLAAQWPIAQKCEHADIVIDNSRDRTFTFQQVDQAIEKVVVAEN | Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
Sequence Mass (Da): 23628
Sequence Length: 209
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Subcellul... |
Q2JLX1 | MRIIGLTGGVGTGKSTVARILEQHGIPVADADQMARQALAVGSPIRERVLERYGKVIQTPSGDLDRRRLGQIVFADAAERAWLEAQIHPFVRAQLQDFLSALAEQSSKVHGVPLEEEPASQKRSGVGFSSGQGSQTVCLMIPLLFEAHMENWASEIWVVTCTPEQQRQRLARRDPLTPEEIEARIASQWPLAEKVRRADVVLDNSGSLAELEAQVKQALASAGQRPFASPPRAGYSDG | Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
Sequence Mass (Da): 25967
Sequence Length: 238
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Subcellul... |
Q3AVV9 | MTFGDWPPQRRIGLTGGIASGKSSVAALLEKRGCPVLDADVYAREALATDTSASKAVVARYGKRVQKDGTSDIDRAELAAIVFNDPNERSWLEQLVHPIVQRRFDDALRSLPDAPIVILMIPLLFEAGLEKWCSEIWVVRCTALQQRERLMARNNCTEAEATQRIAAQWPIDIKVQRADSVINNSGRIDDLHDQLDALL | Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
Sequence Mass (Da): 22148
Sequence Length: 199
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Subcellul... |
Q55515 | MDTKPPRQRLIGLTGGIATGKSTVTDYLQQKYSVPILDADLYARQAVEPGSEILVAIARRYGPEILDQQGQLKRQALGEIVFNNAEEKQWLESQIHPFVGRCFRSALAQLKQEQTVLLSIPLLFEAQLTDWVTEIWVVTCGPQQQVERLIKRNGLTEAEALARITSQMPLAEKVALADVVLDNSGQIADLEPQIIKAWHHR | Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
Sequence Mass (Da): 22520
Sequence Length: 201
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Subcellul... |
Q47QN9 | MLKVGLTGGIGSGKSSVARRLAAHGALVIDADAIAREVVEPGTPALAEIVAEFGDQVLTPEGRLDRARLGEIVFADETKLARLNAIVHPRVGERTQELMAQAKEGTIVVYDVPLLVENNLADQYDVVIVVDVPVHTQVERVTANRGMPEEQVRARINAQASREQRRAVADIIIDNSGTEEELDARVAEVWEELQRRLHSR | Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
Sequence Mass (Da): 21881
Sequence Length: 200
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Subcellul... |
Q47UY4 | MILLIDIGNSRTKYVQLISGELSATTQLNNSEFSAEYFTKYFNQASQLIVANVAKSALTDELATWCAREKISYKQVHSEQKKNTLISAYQEPTTLGIDRWLALLGTIHLYPQENVLIIDAGTATTVDLLTSNGQHQGGWILAGINALFTSILSHSTLVHAKSKTMPSLAFGANTSDNVNNACWAATLGMIERAIEQAQQLGDINRIILTGGDGKALTRLLLAQTTENILAVENIQFIDNLIFFGLQEYA | Cofactor: A monovalent cation. Ammonium or potassium.
Function: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
Sequence Mass (Da): 27265
Sequence Length: 249
Pathway: Cofactor biosynthesis; coe... |
B2AG52 | MNAPRLLVDIGNTRLKWAWCEAGAPLPASTGTTVLPTPWQHAGAVAHAADGALRTLAAELRALRAGGPMPSVWISNVAGPVIAAAVDAALADAFGGCAPVQWVRSAAAHGDLVNGYREPTQLGVDRWVGAVGAHRWLPRDTLLVVTAGTATTLDIVTVAAEGGARFEGGLILPGLALMLGTLARNTAQLPALDVGEAGSVAGAQRRWADNTHDAIAAGCLAAQAGAIERTWRALGERGDAARPPRCLLSGGARGALAGALAVPFEMHDNLVLLGLHAMAMADA | Cofactor: A monovalent cation. Ammonium or potassium.
Function: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
Sequence Mass (Da): 28843
Sequence Length: 283
Pathway: Cofactor biosynthesis; coe... |
Q11Q02 | MNIVIDVGNNYIKIGAFSGGKLQWTKTYSRLHDVLQAVQAEKPVHVFISSVRNQTDFSALETVTQVHFLNKHTRLPIDIDYETPHTLGTDRIAAAVGAATLFPGCNNLFFDLGTCLTHGFINTKAVFEGGSISPGVEMRFKALAHFTEKLPLVKAEKEPPLTGKSTSGSIMSGVLNGIQFEIEGFIEAYQNKYTPINVLLTGGNASLFEKRLKEPIFVIAELNLIGLNRILNYNV | Cofactor: A monovalent cation. Ammonium or potassium.
Function: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
Sequence Mass (Da): 25840
Sequence Length: 235
Pathway: Cofactor biosynthesis; coe... |
Q479J6 | MIVCLDSGNTRIKWGVHDGVKWLAQGAVAHAEVGALSRLVAEWPLPEKVMLANVAGVEAGSRIREQLAAWAPVFHEVRPELRRCGVTNLYKSPERLGVDRWCALLGARSLVDSATVVVMAGTATTIDTLDADGNFLGGVIMPGIGLMLRSLAHGTAALPFADGEYATYPRCTDDAIVTGVIDAQAGAIERIFSRLDDPAASCLLSGGYAEQIAVHLVVRHRLADNLPLEGLRHLALKS | Cofactor: A monovalent cation. Ammonium or potassium.
Function: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
Sequence Mass (Da): 25367
Sequence Length: 238
Pathway: Cofactor biosynthesis; coe... |
Q3Z9C7 | MSEKLVAVDIGNTSVNIGIFEGEKLLANWHLGSVAQRMADEYASLLLGLLQHAGIHPEELNRVIMCSVVPPLTTTFEEVFKSYFKAAPLVVGAGIKSGVKVRMDNPREVGADRIVNAAAARVLYPGACIIVDMGTATTFDTLSEGGAYIGGAIAPGIATSAQAIAEKTSKLPKIEIIRPAKVIGSNTVSAMQSGIYFGYIGLVEELVRRIQTELGQKTRVVATGGYAALIAEGSRIFDIVRPDLTLQGLRIIYQMNQA | Cofactor: A monovalent cation. Ammonium or potassium.
Function: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
Sequence Mass (Da): 27490
Sequence Length: 258
Pathway: Cofactor biosynthesis; coe... |
Q9RX54 | MPAFPLLAVDIGNTTTVLGLADASGALTHTWRIRTNREMLPDDLALQLHGLFTLAGAPIPRAAVLSSVAPPVGENYALALKRHFMIDAFAVSAENLPDVTVELDTPGSVGADRLCNLFGAEKYLGGLDYAVVVDFGTSTNFDVVGRGRRFLGGILATGAQVSADALFARAAKLPRITLQAPETAIGKNTVHALQSGLVFGYAEMVDGLLRRIRAELPGEAVAVATGGFSRTVQGICQEIDYYDETLTLRGLVELWASRSEVR | Cofactor: A monovalent cation. Ammonium or potassium.
Function: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
Sequence Mass (Da): 27839
Sequence Length: 262
Pathway: Cofactor biosynthesis; coe... |
B8J468 | MQPELLLFDIGNTSIKIGLAHERQVVTSYTLRTDAGQTADDLGLKLATLLGHAGVTPQSLRACVASSVVPGFDPLLREAVARYVDCPLYRVGADLSVPLENRYERPAEVGADRLVGAYAARRLYPEFPGLLVVDFGTAVTIDCVNGNAYMGGLIFPGPRTALSALSREAAKLPRVNLDVRADEPTPGRSTATSIQHGLVFGFACMVEGLAQRLKRQLPGPARVLGTGGFAASIARVSPVFDHVLPALLLEGLRRLYYEERTAF | Cofactor: A monovalent cation. Ammonium or potassium.
Function: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
Sequence Mass (Da): 28245
Sequence Length: 263
Pathway: Cofactor biosynthesis; coe... |
A8ZZH7 | MLLVIDIGNTNTVFGIFEDQKLVRDWRIRTKRNTTEDELNVLLTGLFTGSSVALADISRAVIASVVPPVERIYSAFCKKYLRCTPQWVSPANCAGITIRYANPQEVGADRIVNAVGAHAKYQTDLIVVDFGTATTFDLVSADGAYEGGVIAPGIGISADALFSHASKLPRVDLMTVPETVVGKDTAGSIKSGIIFGYAGLVDGIVSRMITERGRPHKVIATGGLAPLIAGVSATIEAVEPNLTLEGLRIIGSSAE | Cofactor: A monovalent cation. Ammonium or potassium.
Function: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
Sequence Mass (Da): 26973
Sequence Length: 255
Pathway: Cofactor biosynthesis; coe... |
Q6AKW8 | MILVIDVGNSHTVTGLYDHGKLIGHWRLKTDRDRTSDELAIRYHGLFIMEGIDPRQITDIVLASVVPTLSSAWIRCCERHFGKHLNQPVMDLSVTKLAPLVRVETDNPHEVGIDRLVNAYGAWHTRKTDLIVIDFGTAITFDCVTSDCVYIGGVILPGIAISLDALATRTAKLPMVDVRDVPSSLIGKNTVHAMQSGILYGYGAMVDGIVEGIQKEMLGGKRRAEVIATGGMANLIEPFTTTIEHIDKLLTLDAMELILHALKKKQ | Cofactor: A monovalent cation. Ammonium or potassium.
Function: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
Sequence Mass (Da): 29231
Sequence Length: 266
Pathway: Cofactor biosynthesis; coe... |
Q72F93 | MARHLLLFDIGNTNVKVGIATEGTVLTSYALPTDGTQTGDGFGLALLDIMRHAGLGADDIDACVGSSVVPSLDPLLRHACERFLWRPLQLAHVDLPVPLENRYERPTEVGADRLVAAFAARRLYPDARALVSVDFGTATTFDCVDGDAYLGGLICPGVLSSAGALSSRTAKLPRVSLEVSEDMPVVGRSTTTSLNHGFIFGFAALAEGVTARLRKVLPEPLEVVATGGFARAVARVSDCFDHVRPDLLLEGLRLLYLESEQR | Cofactor: A monovalent cation. Ammonium or potassium.
Function: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
Sequence Mass (Da): 28014
Sequence Length: 262
Pathway: Cofactor biosynthesis; coe... |
Q4FUX4 | MLWLDLGNTRLKYWLTDDIGQIVSHDAKQHLQAPAELLMGLTDRFERYAPDFIGISSVLGDDLNIKVSETLSRLNIPFEFVHVDANYPLMKSAYNDEQLGCDRWLQMLGAVDKTKRQCLIGCGTAITIDLIDHATHLGGYIFPSIYLQRESLFSGTKQITISNGTFDSVSQGITTQDAVHRGILLSIVGAINEISTRHPNFEVIMTGGDAAIIAQHVNRPVRLRDDLLLNGLARYFDHSKQS | Cofactor: A monovalent cation. Ammonium or potassium.
Function: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
Sequence Mass (Da): 27013
Sequence Length: 242
Pathway: Cofactor biosynthesis; coe... |
Q7UVH5 | MVRVGIDVGNTAIKVVTQASTAVEAAQPARTRGPQLRSISLRDPEWITKCIEHLQTLAEKVAACESRECESVCYDVRVASVNRGSAEPLVFALDEAFFQCIRVRFVTHEDVSMPIDVNFPERVGIDRLLGAEAAFRRHAAPLIVVDAGTTVTVDFVSAEGVFRGGAILPGLEMQTAALAAGTDALPKLDWASHRCREMPEGPGRDTVAAMRLGVLASVAGAVERLLRIYGGAATLVVTGGDAGCLVDALPAECDAVEEPHLVAQALLDLMLHE | Cofactor: A monovalent cation. Ammonium or potassium.
Function: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
Sequence Mass (Da): 29051
Sequence Length: 273
Pathway: Cofactor biosynthesis; coe... |
B6ISW6 | MLLAIDAGNTNVVFAVFEGDVKRGQWRVSTDGRRTADEHAVWLVALMAMKGLTPKDIHAAILSSVVPAQTGPLTTLCEEHFGCTPMRVGDPGVRLGLEVRIDNPKEAGADRLVNAVAAVATYPPPLVVIDIGTGTTFDVVDANGDFAGGVIAPGPVLSLDALHRVAAQLPKVDILRPDRVIGKGTVAAMQSGMFWGYTGMIEGILTRIKAELSPTGDPPVTVIGTGGLVRLFAEGSSLVDAIDADLTLRGLRLIHQRNAAR | Cofactor: A monovalent cation. Ammonium or potassium.
Function: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
Sequence Mass (Da): 27443
Sequence Length: 261
Pathway: Cofactor biosynthesis; coe... |
Q2RU25 | MLLAIDSGNTNTVFAVYDGDAKRGEWRAATNANRTADEMGVWLLQLMTLEGLSQGDIDATIIASVVPATVFNLRMLCHRYFHSPPMVVGEPDVDLGIGILLERPDEVGADRLVNAVAAHETYRGPLIVIDFGTATTFDVVDEEGNYCGGAIAPGVNLSLEALHMASAQLPRVAIGRPRTVIGKATIPAMKSGIYLGYVGLIEGLVKRISEEFGAPMRVIATGGLAPLFAEATDAIQTIDDDLTLRGLLIIHRRNQPD | Cofactor: A monovalent cation. Ammonium or potassium.
Function: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
Sequence Mass (Da): 27523
Sequence Length: 257
Pathway: Cofactor biosynthesis; coe... |
A5UVB3 | MLLTIDIGNTNIKIGVYQDERLTAHWRVTTERHRLADEYLVLLHNLFDLGGIDPREIDGCAISCVVPPLTGEFRTLCRTYFRVEPLMVNATTPTGLRYNVDTPAELGADRIANSLAAFRRYGGPVIVLAFGTATTFDVITADGEYIGGAIAPGIGISADALFRLAAKLYQVELVRPPSVIGKNTIHHMQSGVILGYAGLVEGLVNRMQAELGTSCPVVATGGLAELIAAETEAITTVEPYLTLEGLRLIYEMNRS | Cofactor: A monovalent cation. Ammonium or potassium.
Function: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
Sequence Mass (Da): 27605
Sequence Length: 255
Pathway: Cofactor biosynthesis; coe... |
Q1AU02 | MLMAVDIGNTQTVLGYFEGERLRASWRMTTEPYRSPDEVGAACAALFALRGLSLEDADAMIVSSVVPDLTGTYRHLAADILQVPFYAVGPEMDLGMENRYDDPSAVGADRLVNAVAARRYYGAPAIIADSGTATTVCAVDAGGAYRGGAILPGLYVSMDALASRTAKLPRVDLEEEPPRAIATNTPDSIRSGFIYGYAGAIDALIRRFKEELAAEGETEGLRVVATGGLSPVISRYCREIEVLDPDLTLKGLQVLYALNASRAR | Cofactor: A monovalent cation. Ammonium or potassium.
Function: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
Sequence Mass (Da): 28214
Sequence Length: 264
Pathway: Cofactor biosynthesis; coe... |
Q21MA1 | MKLYVDAGNTRTKWRLADGREGVVASDDISGMERSFALLAGVVTGVFVCSVLGEAFNRRLEALCGQLFGVPPHFARVKQGVLDIVPAYERLDTLGVDRWLGLVFARSHAKSQCSVVVGAGSALTVDLLDAQACHLGGWIAPGCASVEAALGGKVQFARSEAYLKALQSDGALTPPQTSAFGSSTVACVQAGVDAMIRGFLQQVIACAGTEFGGREAVYFLAGGDSPRVEAMLRELDPNLELVLSPAIVLDALVLWSEWCA | Cofactor: A monovalent cation. Ammonium or potassium.
Function: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
Sequence Mass (Da): 27419
Sequence Length: 260
Pathway: Cofactor biosynthesis; coe... |
P9WGA9 | MIIVVGIGADGMTGLSEHSRSELRRATVIYGSKRQLALLDDTVTAERWEWPTPMLPAVQGLSPDGADLHVVASGDPLLHGIGSTLIRLFGHDNVTVLPHVSAVTLACARMGWNVYDTEVISLVTAQPHTAVRRGGRAIVLSGDRSTPQALAVLLTEHGRGDSKFSVLEQLGGPAERRRDGTARAWACDPPLDVDELNVIAVRYLLDERTSWAPDEAFAHDGQITKHPIRVLTLAALAPRPGQRLWDVGAGSGAIAVQWCRSWPGCTAVAFERDERRRRNIGFNAAAFGVSVDVRGDAPDAFDDAARPSVIFLGGGVTQPG... | Function: Catalyzes the methylation of both C-5 and C-15 in precorrin-6Y to form precorrin-8X.
Catalytic Activity: precorrin-6B + 2 S-adenosyl-L-methionine = CO2 + 3 H(+) + precorrin-8X + 2 S-adenosyl-L-homocysteine
Sequence Mass (Da): 41854
Sequence Length: 390
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynt... |
Q9HZU0 | MSSADSTPPWLTLVGIGEDGYPGLGKQARRALLQASRIVGAARQLELLPPCIGAARETWPTPFSLEPLLARRGQPTCVLASGDPMLFGVGASLARQLPATELRVLPAPSSLSLAAARLGWALQEVACLSLVARPLAALQAQVHDGRRLLVLSNDGDSPAAIARLLNARGFGASRLSVLEHLGGPLERRLDGLAGDWSLPRAADLNLVAVECRAGAGAVRLPLTPGLADEAYRHDGQLTKRDVRAVTLARLAPCPGELLWDVGAGCGSIGIEWMRAHPSCRAIAIEANDERQEHIRHNRDALGVPTLHLVAGSAPEALLEL... | Function: Catalyzes the methylation of both C-5 and C-15 in precorrin-6Y to form precorrin-8X.
Catalytic Activity: precorrin-6B + 2 S-adenosyl-L-methionine = CO2 + 3 H(+) + precorrin-8X + 2 S-adenosyl-L-homocysteine
Sequence Mass (Da): 44128
Sequence Length: 415
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynt... |
P21921 | MADVSNSEPAIVSPWLTVIGIGEDGVAGLGDEAKRLIAEAPVVYGGHRHLELAASLITGEAHNWLSPLERSVVEIVARRGSPVVVLASGDPFFFGVGVTLARRIASAEIRTLPAPSSISLAASRLGWALQDATLVSVHGRPLDLVRPHLHPGARVLTLTSDGAGPRDLAELLVSSGFGQSRLTVLEALGGAGERVTTQIAARFMLGLVHPLNVCAIEVAADEGARILPLAAGRDDALFEHDGQITKREVRALTLSALAPRKGELLWDIGGGSGSIGIEWMLADPTMQAITIEVEPERAARIGRNATMFGVPGLTVVEGEA... | Function: Catalyzes the methylation of both C-5 and C-15 in precorrin-6Y to form precorrin-8X.
Catalytic Activity: precorrin-6B + 2 S-adenosyl-L-methionine = CO2 + 3 H(+) + precorrin-8X + 2 S-adenosyl-L-homocysteine
Sequence Mass (Da): 42938
Sequence Length: 413
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynt... |
P9WGB0 | MTVYFIGAGPGAADLITVRGQRLLQRCPVCLYAGSIMPDDLLAQCPPGATIVDTGPLTLEQIVRKLADADADGRDVARLHSGDPSLYSALAEQCRELDALGIGYEIVPGVPAFAAAAAALKRELTVPGVAQTVTLTRVATLSTPIPPGEDLAALARSRATLVLHLAAAQIDAIVPRLLDGGYRPETPVAVVAFASWPQQRTLRGTLADIAARMHDAKITRTAVIVVGDVLTAEGFTDSYLYSVARHGRYAQ | Function: Catalyzes the methylation of C-11 in precorrin-4 to form precorrin-5.
Catalytic Activity: precorrin-4 + S-adenosyl-L-methionine = precorrin-5 + S-adenosyl-L-homocysteine
Sequence Mass (Da): 26420
Sequence Length: 251
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide fr... |
Q9HZP9 | MTVYFIGAGPGDPDLITVKGQRLIRQCPVILYAGSLVPQALLEGHQAGQVVNTAELDLEQIVELLAQAHRRGLDVARVHSGDPSLYGAIGEQIRHLRELGIPYEIVPGVTATAACAALLGCELTLPEVSQTLILTRYAARTKMPEGESLGDLARHRATLAIHLGVAHLAKIVEELLPHYGADCPVAVIHRASWPDQEQVRGTLGDILPKVAARNFRRTALILVGEVLAAEGFADSSLYRAEHRHLYRPGE | Function: Catalyzes the methylation of C-11 in precorrin-4 to form precorrin-5.
Catalytic Activity: precorrin-4 + S-adenosyl-L-methionine = precorrin-5 + S-adenosyl-L-homocysteine
Sequence Mass (Da): 27040
Sequence Length: 250
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide fr... |
O68100 | MTVHFIGAGPGAADLITIRGRDLIASCPVCLYAGSLVPEALLAHCPPGAKIVNTAPMSLDAIIDTIAEAHAAGQDVARLHSGDLSIWSAMGEQLRRLRALNIPYDVTPGVPSFAAAAATLGAELTLPGVAQSVILTRTSGRASAMPAGETLENFARTGAVLAIHLSVHVLDEVVQKLVPHYGEDCPVAIVWRASWPDQRVVRATLATLQTSLGAELERTALILVGRSLATEDFDESRLYAGDYDRRYRPLGTHPRFPEGSE | Function: Catalyzes the methylation of C-11 in precorrin-4 to form precorrin-5.
Catalytic Activity: precorrin-4 + S-adenosyl-L-methionine = precorrin-5 + S-adenosyl-L-homocysteine
Sequence Mass (Da): 27704
Sequence Length: 261
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide fr... |
Q53138 | MTVYFIGAGPGAADLITVRAQRIIAASPVCLYAGSLVPQELLAECPEGARVIDTARLSLDEIVALLIEADAAGQDVARLHSGDPSIFSAVAEQVRRLESAGVAYQVVPGVPAFTAAAASLGRELTVPGVSQSIVLTRVSTLSTAMPEGEDLRSLGRSGATMVVHLGAHRIDQIAEELIEDYGRDCPAAVVAFASRPDEIVLRGTLATIADQVKAAGVTKTAVVIVGRVLAAEGFPDSYLYSATRERTTH | Function: Catalyzes the methylation of C-11 in precorrin-4 to form precorrin-5.
Catalytic Activity: precorrin-4 + S-adenosyl-L-methionine = precorrin-5 + S-adenosyl-L-homocysteine
Sequence Mass (Da): 25963
Sequence Length: 249
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide fr... |
P21922 | MTVHFIGAGPGAADLITVRGRDLIGRCPVCLYAGSIVSPELLRYCPPGARIVDTAPMSLDEIEAEYVKAEAEGLDVARLHSGDLSVWSAVAEQIRRLEKHGIAYTMTPGVPSFAAAASALGRELTIPAVAQSLVLTRVSGRASPMPNSETLSAFGATGSTLAIHLAIHALQQVVEELTPLYGADCPVAIVVKASWPDERVVRGTLGDIAAKVAEEPIERTALIFVGPGLEASDFRESSLYDPAYQRRFRGRGE | Function: Catalyzes the methylation of C-11 in precorrin-4 to form precorrin-5.
Catalytic Activity: precorrin-4 + S-adenosyl-L-methionine = precorrin-5 + S-adenosyl-L-homocysteine
Sequence Mass (Da): 26863
Sequence Length: 253
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide fr... |
P29930 | MSDETTVGGEAPAEKDDARHAMKMAKKKAAREKIMATKTDEKGLIIVNTGKGKGKSTAGFGMIFRHIAHGMPCAVVQFIKGAMATGERELIEKHFGDVCQFYTLGEGFTWETQDRARDVAMAEKAWEKAKELIRDERNSMVLLDEINIALRYDYIDVAEVVRFLKEEKPHMTHVVLTGRNAKEDLIEVADLVTEMELIKHPFRSGIKAQQGVEF | Function: Required for both de novo synthesis of the corrin ring for the assimilation of exogenous corrinoids. Participates in the adenosylation of a variety of incomplete and complete corrinoids (By similarity).
Catalytic Activity: 2 ATP + 2 cob(II)yrinate a,c diamide + reduced [electron-transfer flavoprotein] = 2 ade... |
Q9I466 | MRDLILGGARSGKSRLAERLAAESGLAVSYIATAQAGDGEMGRRIAEHRARRPAHWRTLEEPLALAATLRSEAEAGRCLLVDCLTLWLTNLLLCDDPQRLDGEREALLECLGELPGRIILVSNETGLGVVPLGELSRRYVDEAGWLHQAIAERCERVTFTVAGLPMPLKGEPL | Function: Catalyzes ATP-dependent phosphorylation of adenosylcobinamide and addition of GMP to adenosylcobinamide phosphate.
Catalytic Activity: adenosylcob(III)inamide + GTP = adenosylcob(III)inamide phosphate + GDP + H(+)
Sequence Mass (Da): 18862
Sequence Length: 173
Pathway: Cofactor biosynthesis; adenosylcobalamin... |
Q94KT8 | MESFFSRSTSIVSKLSFLALWIVFLISSSSFTSTEAYDALDPEGNITMKWDVMSWTPDGYVAVVTMFNFQKYRHIQSPGWTLGWKWAKKEVIWSMVGAQTTEQGDCSKYKGNIPHCCKKDPTVVDLLPGTPYNQQIANCCKGGVMNSWVQDPATAASSFQISVGAAGTTNKTVRVPRNFTLMGPGPGYTCGPAKIVRPTKFVTTDTRRTTQAMMTWNITCTYSQFLAQRTPTCCVSLSSFYNETIVGCPTCACGCQNNRTESGACLDPDTPHLASVVSPPTKKGTVLPPLVQCTRHMCPIRVHWHVKQNYKEYWRVKITI... | Function: Involved in determining the orientation of cell expansion, probably by playing an important role in cellulose deposition. May act by recruiting cellulose synthesizing complexes to discrete positions on the cell surface.
Location Topology: Lipid-anchor
Sequence Mass (Da): 51203
Sequence Length: 456
Subcellular... |
O30198 | MALDLLRSSLGFLTTLPVKGDVDVLRRNLWVFSFVGIFIGSVISIPAVLGFWFLCVLLYVAIEGVNHIDGLADFGDAFFAPEERKKVAIKDLNLGTGGAVFLCVYFLILFYSFQRVSAFYIIFSQVLAKFSMLLLLTTSKPAWQGMTGFMMEFARKRDVVIGSLPLLLVVLKPLAVFPLLFAITISLLVKRYAEEKFGGVSGDVVGASNCLVFAGSLLVCYFLAD | Function: Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate (By similarity).
Catalytic Activity: adenosylcob(III)inamide-GDP + alpha-ribazole = adenosylcob(III)alamin ... |
O27961 | MIKAIRSAISFLTTLPLGGDVEELRKNLWLFPYAAILIALIVSVPHFIRNFVDIRFLALVLYLGAEGINHVDGLADFGDALFAPKNRKREAIKDLNTGAGGVAVVVVYFLLLYTLLYRSDFWEIALSQVLAKYSMLLLMLLSRPSWDGMGSYFMEKISSKDVFIGAVPVVLLCYKVGIESLAALASGFAVVLLLKAYSEKHFGGVNGDVIGSANCLTFAASLSALTIAGQL | Function: Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate (By similarity).
Catalytic Activity: adenosylcob(III)inamide-GDP + alpha-ribazole = adenosylcob(III)alamin ... |
A3DK68 | MKYLKRILLMVGFLTRIPVPFKIDGTEEDYGKGLVFAPVVGLLIGGILTILFYILKRFFPPGVTGILLIAAYIMLTGGLHLDGLGDTFDGIFSNRSREKMLEIMRDSRIGTNAVLAVICVVILNYALLSSIPLSGLPKALLLFPVAGRIGSLVGAGSTVYAREGEGLGKSFINCCGIKEILQGGIIYFIVSLLVLNIKGLLLAAATMITSFATVKFFAGKVGGATGDILGAVCELNQTFFLILFYLFK | Function: Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.
Catalytic Activity: adenosylcob(III)inamide-GDP + alpha-ribazole = adenosylcob(III)alamin + GMP + H(+)
Loc... |
B2HZL6 | MAPFWIALQFLTILPIELKTIPTAQQNGRAILFYPLVGLIIGGILFLVTCIFVKLPALLLAAIVFALWIWLTGGLHLDGLADTADAWVGGFGDKLRTLQIMKDPSCGPIGVLSIVIVCLLKFALIYVLIEQHQSLFLICIPILGRVVPSILFLTTPYVREKGLGRSLTDHLPKTASWIITGFVLLLPLYWEWQGLIAIISFLISLVYLRHVFIKRIGGITGDTVGAAIEIGETVLIFTFVVSYFYLV | Function: Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.
Catalytic Activity: adenosylcob(III)inamide-GDP + alpha-ribazole = adenosylcob(III)alamin + GMP + H(+)
Loc... |
Q0A4T1 | MTTAVRGLLLALAFLTRLPVWWLGPPRREDHAASLPAYPVVGLILGILLLALYALLQWFFPDQFVVQAALLVAAWALVTGLLHLDGLGDSADAWLGGHGDRLRSLEIMKDPRSGPAAVAVITLALVVKVAALAALLRLDAALAALLIAPVLGRAAAALLIAGTPYARKQGLAGPLAEAPATRWIGLTALGALLFVTALAGWAGLAAVLGVVAVGVWAQHLMMRRLDGFTGDTAGALVEVAELAALLGLLAVLANSAG | Function: Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.
Catalytic Activity: adenosylcob(III)inamide-GDP + alpha-ribazole = adenosylcob(III)alamin + GMP + H(+)
Loc... |
A6TU75 | MNIDMNRFISILQFLTRIPIKRDVPMEEAFHKGIIYFPVVGGIIGALLMVAYRGASLYLAHSLSALLTVGFFVFLTGGLHLDGLGDTFDGLYSNRNKETILEIMKDSRLGTNGVLAMVFILLLKLYGIQGLGEHQIYWGIILMPVMGRQAIVYGCYRTIYGRSQGLGHLFIGKVSKKELLISSLLTFILAAMHLPSLIFALLLPIGSQLYKGHVMKKIDGMTGDTLGSLCELTEGCYLLFILLITGAGLF | Function: Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.
Catalytic Activity: adenosylcob(III)inamide-GDP + alpha-ribazole = adenosylcob(III)alamin + GMP + H(+)
Loc... |
A8MIW2 | MKSLLLMMTFFTRIPVTYPYDYDEKDFIKGVKFLPVIGLLIGILMYLPTLLAPYIHRPIIIVSIWALYFLITGGLHIDGLADTFDGIFSYRSKEEMLRIMKDSRIGAFGVLGILWLLILNLTLAYYTENMLLLLVPVVGRASAVFAASRTIYARSEGMGGAFIESCRTKEGVISIAFSLLLGSMVSIKGAIIPMGITFLGVAMLTKKISKILGGMTGDTIGATIEISQTLFMLSAYLLKSIII | Function: Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.
Catalytic Activity: adenosylcob(III)inamide-GDP + alpha-ribazole = adenosylcob(III)alamin + GMP + H(+)
Loc... |
B9JW08 | MTLTAFVDDLARSLGFLSRLPIASRFFQNHSGEMSRTPRAFPLAGAVITAPAGLLLALMLGLGASSMVAAFAAIGLQVLLTGALHEDGFADTADGLGGANRERALDIMKDSRVGTFGVLALVFGVGLRVAALASLVNSLSPINVALVMIGIAAVSRALMVWHWHALPPAKPDGVAASLGKPEDNTLYTALFLGLAVAVVTIAPVTSFHPLAVMLVASGAAAFASNRLVSHRLGGQTGDTIGATQQICEITALASIAMAL | Function: Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.
Catalytic Activity: adenosylcob(III)inamide-GDP + alpha-ribazole = adenosylcob(III)alamin + GMP + H(+)
Loc... |
Q5P2R7 | MTTMRYQLELFFTALGFFTRLPVPAWVPWSPERLNHAARFFPLVGWVVGAIGAASYLAFVQLLPPALAVLLSMAVTIRATGAFHEDGWADACDGLGGGWDRLQVLTIMKDSRIGSYGTAGLVLMLLAKAAALVELAAHGNLQVALALLAAHPLSRLASTSLIHTMQYVREDESAKSKPLARRLSATELVVAAVFGLAPLALLAPAEALAALTATAAATLWAARVFARRLGGYTGDCLGAAQQGSELACYLGILAAWNFI | Function: Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.
Catalytic Activity: adenosylcob(III)inamide-GDP + alpha-ribazole = adenosylcob(III)alamin + GMP + H(+)
Loc... |
Q8EI17 | MSERESWHKEIDLFFVAMGYFTRIPMPKWVEVDADKLNKASRYFGLVGLLVGLLSAIIFWLTQNWLPAGVSVLLSMLTGILLTGGFHEDGLADTFDGFGGGWTAEDKLRIMKDSRLGSYGALALIMVLLLKWQLLVELALYDPVVAGSAMIVAHTVSRVVAASLIFTETYVRDDETSKSKPLAQHQGINDLFILIASGVLVLLVLKGIAALSLLLVMIGLRRLIVVIFRRQIGGYTGDTLGAAQQICEIVCYFVLLVVGGIL | Function: Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.
Catalytic Activity: adenosylcob(III)inamide-GDP + alpha-ribazole = adenosylcob(III)alamin + GMP + H(+)
Loc... |
Q8EI18 | MSQSSLSFQIEPVSKAQDQVIQQKIDLKTKPPGALGMLESLALQIARIQGPQQLQIVKPTMLVFAGDHGIAAEGVSIAPSEVTHQMVQNFAEGGAAINVFCRQLGLTLEVIDCGILTPVEGVEGIIDQRLGAGTGAIHLEPAMSLDCVDKGFAMARELIERHHQAGCNLVAFGEMGIGNTSSAAAIMAAIMQLEVADCVGRGTGINSETLARKLTLVELALLSHQSAMTGPKQVLACLGGFEIVQMTGAMLAAAERKMLVVVDGFIATAAALVAVTINANVRDYLIFAHRSEEQGHQRMLEHLQAKPLLSLGLRLGEGTG... | Function: Catalyzes the synthesis of alpha-ribazole-5'-phosphate from nicotinate mononucleotide (NAMN) and 5,6-dimethylbenzimidazole (DMB).
Catalytic Activity: 5,6-dimethylbenzimidazole + nicotinate beta-D-ribonucleotide = alpha-ribazole 5'-phosphate + H(+) + nicotinate
Sequence Mass (Da): 36785
Sequence Length: 350
Pa... |
Q83R14 | MQIIADLLNTIPAINSAAMSRAQRHVDGLFKPVGSLGKLEALAIQLAGMPGVNGIPHVGKKAVLVMCADHGVWEEGVAISPKEVTAIQAENMTRGTTGVCVLAAQAGANVHVIDVGIDTAEPIPGLINMRVARGSGNIASAPAMSRRQAEKLLLDVICYTRELAKNGVTLFGVGELGMANTTPAAAIVSTITGRDPEEVVGIGANLPTDKLANKIDVVRRAITLNQPNPQDGVDVLAKVGGFDLVGIAGVMLGAASCGLPVLLDGFLSYAAALAACQMSPAIKPYLIPSHLSAEKGARIALSHLGLEPYLNMDMRLGEGS... | Function: Catalyzes the synthesis of alpha-ribazole-5'-phosphate from nicotinate mononucleotide (NAMN) and 5,6-dimethylbenzimidazole (DMB).
Catalytic Activity: 5,6-dimethylbenzimidazole + nicotinate beta-D-ribonucleotide = alpha-ribazole 5'-phosphate + H(+) + nicotinate
Sequence Mass (Da): 36880
Sequence Length: 359
Pa... |
C3MDH9 | MSASGLPFDDFRELLRNLPGPDAAALVAARERDAQLTKPPGALGRLEEIAFWLAAWTGRPPAVNRPLVAIFAGNHGVTRQGVTPFPSSVTAQMVENFAAGGAAINQICVTHDLGLKVFDLALDYPTGDITEEAALSERDCAATMAFGMEAIAGGTDLLCIGEMGIGNTTIAAAINLGLYGGTAEEWVGPGTGSEGEVLKRKIAAVERAVALHRDHLSDPLELMRRLGGREIAAMAGAILAARMQKVPVIIDGYVATAAAAILKAANPAALDHCLIGHVSGEPGHIRAIEKLGKTPLLALGMRLGEGTGAALAAGIVKAAA... | Function: Catalyzes the synthesis of alpha-ribazole-5'-phosphate from nicotinate mononucleotide (NAMN) and 5,6-dimethylbenzimidazole (DMB).
Catalytic Activity: 5,6-dimethylbenzimidazole + nicotinate beta-D-ribonucleotide = alpha-ribazole 5'-phosphate + H(+) + nicotinate
Sequence Mass (Da): 34692
Sequence Length: 338
Pa... |
P29934 | MSSNSKAKPTTRENAAEPFKRALSGCIRSIAGDAEVEVAFANERPGMTGERIRLPELSKRPTLQELAVTRGLGDSMALRKACTHARIQRTMSPQGADARAIFDAVEQARVEAIGSLRMAGVAKNLNVMLEEKYAKANFATIERQADAPLGEAVALLVREKLTGQKPPASAGKVLDLWREFIEGKAAGDIEHLSSTINNQQAFARVVRDMLTSMEVAEKYGDDDNEPDEQESETDEDQPRSQEQDENASDEEAGDDAAPADENQAAEEQMEEGEMDGAEISDDDLQDEGDEDSETPGEVKRPNQPFADFNEKVDYAVFTRE... | Function: Catalyzes cobalt insertion in the corrin ring.
Catalytic Activity: ATP + Co(2+) + H2O + hydrogenobyrinate a,c-diamide = ADP + cob(II)yrinate a,c diamide + 5 H(+) + phosphate
Sequence Mass (Da): 70367
Sequence Length: 631
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamid... |
P45695 | MASGVMVSDDVIKVFNEMKVRHQLSPEDAKKRKKAVVFCLSDDKKTIILEPGKEILQGDIGCNVEDPYKTFVKMLPRNDCRYALYDALYETKETKKEDLVFVFWAPEEASLKSKMIYASSKDAIKKRLPGIKHEWQINTYEDVNDPCNLADKLGGNTVVSLEGKSVRS | Function: May play a role in the regulation of cell morphology and cytoskeletal organization (By similarity). Binds to F-actin and exhibits pH-sensitive F-actin depolymerizing activity. Required for formation of the cleavage furrow during cytokinesis.
PTM: Inactive when phosphorylated. Phosphorylation levels vary durin... |
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