ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
B8I492 | MTTYREAGVDVEAGYEAVKLMKNHVKRTFRPEVMTELGGFGGLFSLDKEKYEQPILVSGTDGVGTKLKIAFLTDKHDTVGIDCVAMCVNDIICSGAEPLFFLDYIAVGKNYPEKVAAIVKGVAEGCVMSGCSLIGGETAEMPGFYPVDEYDLAGFTVGIVDKKKIINGKTIKAGDKLIGLPSSGIHSNGYSLVRKLINPTENNLKEYVEKLGCTLGEELLKPTKIYVKTIMDIIGKYEIKGISHITGGGFIENIPRMIPDGLRAQIQKGSWPVLPIFDLLRDLGNMADKDIFNTFNMGIGMIMAVDAQKADEIISYLDSK... | Catalytic Activity: 2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ATP = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + ADP + H(+) + phosphate
Sequence Mass (Da): 36861
Sequence Length: 340
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-... |
Q9UX29 | MVSEEYKKAGVDLEKLRNYHNMISQIISSTYKNTIIGAGHYSGVIKIGSLNIAMHTDGVGTKTFLALQTRIIKPVGIDCVAMNVNDLICVGAKPVALVDYIALERPMDNVVNEIIDGIVQGAKEADVEVIGGETAIMPDVIRGFDLSCTAIGVVDKLKTGAEIRPGDYVLGLESSGIHANGYSLVRKLIEEGKLSLDEYKNELLKPTKIYVKPILEVMNMIKGAAHVTGGAFSKLKRLTSYKIVLNMPDPPQIFKTIEKAGVAHEEMYKVFNMGIGIVLFVSEELMKEVKTKLEGYGTVYELGRVYNGNGITIKTYKNEI... | Catalytic Activity: 2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ATP = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + ADP + H(+) + phosphate
Sequence Mass (Da): 35400
Sequence Length: 323
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-... |
A9VRE8 | MQKLELLYEGKAKRIYRTEAADMVWVEYKDSATAFNGEKKATITGKGRLNNEITTLLFRKLQEVGIKTHFVEKLSDTEQLVKKVSIIPLEVVTRNVIAGSLSKRLGMEEGTALTTPIVEFYYKDDDLGDPLVTEDHIRLLNVATPEQVSVLRDAALQINQVMIEHFASCRVRLVDFKLEFGVTEEGEIILADEISPDTCRLWDETSNEKFDKDVFRRDLGNLTEAYEEILKRLGGASHV | Catalytic Activity: 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + ATP + L-aspartate = (2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamido]succinate + ADP + 2 H(+) + phosphate
Sequence Mass (Da): 27124
Sequence Length: 239
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-ami... |
P12046 | MNIVKNELLYEGKAKKIYKTDDENTLYVVYKDSATAFNGEKKAEISGKGRLNNEISSLIFKHLHAKGINNHFIERISETEQLIKKVTIVPLEVVVRNVVAGSMSKRLGIPEGTELEQPIIEFYYKDDALGDPLITEDHIWLLKAATPEQVETIKSITTIVNEELQSIFDDCHVRLIDFKLEFGLDAEGQVLLADEISPDTCRLWDKETNEKLDKDLFRRNLGSLTDAYEEIFNRLGGIHHV | Catalytic Activity: 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + ATP + L-aspartate = (2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamido]succinate + ADP + 2 H(+) + phosphate
Sequence Mass (Da): 27460
Sequence Length: 241
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-ami... |
Q8A004 | MKALTKTDFNFPGQKSVYHGKVRDVYNINGEKLVMVATDRISAFDVVLPEGIPYKGQMLNQIAAKFLDATTDICPNWKMATPDPMVTVGVLCEGFPVEMIVRGYLCGSAWRTYKSGVREICGVKLPDGMRENEKFPEPIVTPTTKAEMGLHDEDISKEEILKQGLATPEEYETLEKYTLALFKRGTEIAAERGLILVDTKYEFGKHNGTIYLMDEIHTPDSSRYFYSDGYQERFEKGEPQKQLSKEFVREWLMENGFQGKDGQKVPEMTPAIVQSISDRYIELFENITGEKFVKEDTSNIAERIEKNVMNFLSK | Catalytic Activity: 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + ATP + L-aspartate = (2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamido]succinate + ADP + 2 H(+) + phosphate
Sequence Mass (Da): 35766
Sequence Length: 314
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-ami... |
C6BVA6 | MSKHVVETDIKELKLLSRGKVRDIYEVDDDKLLLVTTDRISAYDVIMPNPIDDKGKILNQITLFWMDMFKDIIPNHLIASKVDDYPEVLHKYRDQLEGRSVLVKKAKPLPIECIVRGYITGSGWKDYQKTGEVCGHKLPEGLKESEMLEQPLFTPSTKAELGEHDENISVEKATEMLGKELFDKVQEATLSIYKRGRDYAREKGIIIADTKFEFGIYDGELIIIDEVLTPDSSRFWPVEGYEAGKSQPSFDKQFLRDWLTEINFNKQPPAPEVPEEIATKTRDKYMEAFTLLTESELDA | Catalytic Activity: 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + ATP + L-aspartate = (2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamido]succinate + ADP + 2 H(+) + phosphate
Sequence Mass (Da): 34325
Sequence Length: 299
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-ami... |
Q8TIS9 | MKREQLYSGKAKTIYATDNPDTLIAEFRNSLTAFNGEKKGEMEKKGYYNAQISKKIFEMLEASGIKTHFVSMLSDIEMLVKKVEIIKIEVIVRNIAAGSITKKYPMKEGTIFESPVLVFDFKSDEYGDPMLNDDIAVALGIATREELATLRKLALRINELLVPYLDEKGILLPDFKLEFGRRDGEIILSDEISCDTCRFWDKKTGQSMDKDVFRFDKGDISKAYEEVARRIVPEIFE | Catalytic Activity: 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + ATP + L-aspartate = (2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamido]succinate + ADP + 2 H(+) + phosphate
Sequence Mass (Da): 27092
Sequence Length: 237
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-ami... |
A7IAF5 | MKQKKLLYTGKAKSVYHTDEKGTLIVEFRDDITAFDGGKKDTLKNKGSYNAGVSAFFFSYLEKNGVKTHFLEMQDESRMAVRELSMIPLEVIVRNYAAGSIVRNYPFKEGTPLKPPVIVIDYKDDSRHDPMLNDELIVALKLATPAELKKIKAIALKINTLLSGLLAKQGITLVDFKLEFGRQGTTIYLGDEISMDSMRLWDKKTGESLDKDVYRFNKGDVMATYNRVAARITKPQKPAAAKKKAPVSKKTVKRTR | Catalytic Activity: 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + ATP + L-aspartate = (2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamido]succinate + ADP + 2 H(+) + phosphate
Sequence Mass (Da): 28830
Sequence Length: 256
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-ami... |
Q58987 | MEIKLEEILKKQPLYSGKAKSIYEIDDDKVLIEFRDDITAGNGAKHDVKQGKGYLNALISSKLFEALEENGVKTHYIKYIEPRYMIAKKVEIIPIEVIVRNIAAGSLCRRYPFEEGKELPFPIVQFDYKNDEYGDPMLNEDIAVALGLATREELNKIKEIALKVNEVLKKLFDEKGIILVDFKIEIGKDREGNLLVADEISPDTMRLWDKETRDVLDKDVFRKDLGDVIAKYRIVAERLGLL | Catalytic Activity: 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + ATP + L-aspartate = (2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamido]succinate + ADP + 2 H(+) + phosphate
Sequence Mass (Da): 27761
Sequence Length: 242
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-ami... |
Q8TX83 | MERGRLVYEGKAKSLYEHPEDENLLVMEFRDDITAFNMEKMDTVEGKGVYNCLISARLFEVLEDAGIPTHYVELADERRMVVERLDMFNLEVICRNMATGSLVERLPFEEGEKLDPPIVEFDYKSDEYGDPMVNMDHIRALGLATEEEVERMRELTLQVNEVLSEFLKDCDIILVDFKLEFGVNPDGEVVVGDEISPDTCRFWDAETEESLDKDIFRKDEGDVLAGYREAAERILRGDEEKLAMLPG | Catalytic Activity: 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + ATP + L-aspartate = (2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamido]succinate + ADP + 2 H(+) + phosphate
Sequence Mass (Da): 28405
Sequence Length: 247
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-ami... |
B1MHW4 | MRPSLSDYQHVASGKVRELYRVDDEHLLFVATDRISAFDFVLDTPIPDKGRILTAMSVFFFGLLTVPNHLAGPPDDPRIPEEVLGRALLVRRLDMLPVECVARGYLTGSGLLDYQRTGAVCGHVLPQGLGEASRLDPPLFTPATKADIGEHDMNVDFAAVVGLVGAVRANQLRDETIKIYTRAAAHALHKGIILADTKFEFGVDIEGNLVLADEVFTPDSSRYWDAAHYQPGVVQDSFDKQFVRNWLTGPESGWDRASDTPPPPLPDEVAVATRERYIEAYERISGLSFSDWIGPSA | Catalytic Activity: 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + ATP + L-aspartate = (2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamido]succinate + ADP + 2 H(+) + phosphate
Sequence Mass (Da): 32730
Sequence Length: 297
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-ami... |
A8H5E7 | MNLADKVLVVNDNLPIRTDKPVHSGKVRSVYWLTEEDSARLIKDKGYDVPADAPLAIMVISDRISAFDCVWQGENGLNGVPGKGTALNAISNHWFKLFKDKGLADSHILDIPHPLVWIVQKARPVMIEAIARQYITGSMWRSYTKGEREFCGITIPEGLEKDQKLPELLITPSTKGVLTGLEGVPEADDVNVSRSDIERHVKGFNFSNESDIDLYEKLLKEGFDVISDALAEHDQIFVDTKFEFGYVNDAAGNEKLIYMDEVGTPDSSRIWDGSSHRDGKIIEQSKEGFRQWLLNHFPDPDILLNKNRMVERFALASDNK... | Catalytic Activity: 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + ATP + L-aspartate = (2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamido]succinate + ADP + 2 H(+) + phosphate
Sequence Mass (Da): 41365
Sequence Length: 367
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-ami... |
A3DEU9 | MIKRALISVSDKTGIVEMARELQSMGVDIISTGGTAKTLSDAGIKVINISDVTGFPECLDGRVKTLHPKVHAGILAIRSNEEHMRQLKELNIETIDMVIINLYPFKQTILKENVDLSEAIENIDIGGPTMIRAAAKNYQDVVVIVDPSDYAAVLEELKTTKDVSLKTKFKLAYKVFEHTSHYDTLIAKYLREQIGEDEFPQTLSLTFEKVQDMRYGENPHQKAVFYKEVGANVGCITAAKQLHGKELSYNNINDANGAIEIIKEFDEPTVVAVKHANPCGVASASNIYDAYIKAYEADPVSIFGGIIAANREIDEKTAEE... | Catalytic Activity: (6S)-10-formyltetrahydrofolate + 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide = (6S)-5,6,7,8-tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Sequence Mass (Da): 56342
Sequence Length: 514
Domain: The IMP cyclohydrolase activity resides in the N-terminal r... |
A5FUH4 | MNDRVNIRRALISVSDKAGLVELGRALAAAGVEILSTGGSARALREAGIAVVEVADYTGVPEMLDGRVKTLVPKIHGGLLGRRDLPEHLAQMQRHDIPPIDLLAVNLYPFEETVAKGSDFETCVENIDIGGPALIRAAAKNHDSVAVLTSPAQYDDLIAALAAGGTTLEQRRRLAAAAYARTAAYDAAISAWFAQQTGEMFPAHLALAGARQQMLRYGENPHQSAAFYRTGNRPGVATARQLQGKELSYNNINDTDAAFECVAEFDRPAVVIVKHANPCGVALGADLAEAWDRALDCDPVSAFGGIIAVNRPLDVAAAEK... | Catalytic Activity: (6S)-10-formyltetrahydrofolate + 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide = (6S)-5,6,7,8-tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Sequence Mass (Da): 53979
Sequence Length: 513
Domain: The IMP cyclohydrolase activity resides in the N-terminal r... |
B7J5P7 | MGFMGEITRALISVSDKRGVVEFARRLQDFGVEILSTGGTAKALMADGVAVQEVGDYTGFPELLEGRLKTLHPKIHGGLLAKRDDSSHTRQMAEYGIPAIDLLCVNLYPFAETIASADCTLEEAMENIDIGGPTMLRAAAKNWEGVTVLVDPDDYAAVLQEMEQSYGGVGASTRFRLATKVFAHTARYDGAIANYLSSLGPDGNRTTFPQTLSLQFKKAQDLRYGENPHQAAAFYRDGSGGGLADAHQLQGKELSYNNIGDGDAAVALVMEFAEPACCVVKHGNPCGVAVGPDLLGAYQRAWAGDPISAFGGIVACNRPL... | Catalytic Activity: (6S)-10-formyltetrahydrofolate + 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide = (6S)-5,6,7,8-tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Sequence Mass (Da): 56281
Sequence Length: 524
Domain: The IMP cyclohydrolase activity resides in the N-terminal r... |
Q8UBM8 | MAVVSKKIPAPDKVKIRTALLSVSDKTDIIELATVLSKLGVKLLSTGGTAKAIAEAGLAVTDVSDVTNFPEIMDGRVKTLHPNVHGGLLAIRDDAEHVEAMKAHGIEAIDLSVINLYPFEEVRAKGGDYPTTVENIDIGGPAMIRASAKNHAYVTVVTDPSDYPALVEALQADDGQTSYALRQRFAAKAYARTAAYDAVISNWFAEALAIETPHYRAIGGVLKEKMRYGENPHQSAGFYLTGEKRPGVATATLLQGKQLSYNNINDTDAAYELVAEFLPENAPAVAIVKHANPCGVATGPTLAEAYRRALACDSVSAFGG... | Catalytic Activity: (6S)-10-formyltetrahydrofolate + 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide = (6S)-5,6,7,8-tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Sequence Mass (Da): 56891
Sequence Length: 538
Domain: The IMP cyclohydrolase activity resides in the N-terminal r... |
Q5WJ82 | MTKRALVSVSNKTGLIPFVKGLAEAGVEILSTGGGTKRALEEAGIAVVNVSDVTGFPEILDGRVKTLHPNIHGGLLAMRTNDEHIKQIEELGIEPIDYVVVNLYPFAETIANPDASFADAIENIDIGGPSMLRSAAKNHADVTVVVDPADYDAVLASLDASKEEQLALRQKLAAKVFRHTAAYDAMIGSYLTDAVGEENPESLTVTYTHKQTLRYGENPHQKAAFYESRTSSPSSIAQAKQLHGKELSYNNINDANAALEIVKEFSEPAAVAVKHMNPCGVGTGATVGEAYTRAYEADPKSIFGGIVALNREVDRATAEK... | Catalytic Activity: (6S)-10-formyltetrahydrofolate + 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide = (6S)-5,6,7,8-tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Sequence Mass (Da): 54665
Sequence Length: 511
Domain: The IMP cyclohydrolase activity resides in the N-terminal r... |
B4S133 | MQTPKPIKRALLSVSDKTGILDFATALHNAGVELLSTGGTAKLLAEAGLPVKEVSDHTGHPEIMAGRVKTLHPKIHGGILARRGVDEAVMEENNIAPIDLVVVNLYPFAATVANEDCTLEDAIENIDIGGPTMVRAAAKNHKDVTIVVNAADYSRVLAEMNDNNGSLTYSTRFDLAIKAFEHTAEYDGMIANYFGARLDSTGCEADCDHQHSEFPRTYNIQLTKKQDLRYGENSHQEAAFYVENNIQEASVATATQLQGKELSFNNIADTDAALECVKEFEEPACVIVKHANPCGVAIGNDILTAYDRAFKTDPTSAFGG... | Catalytic Activity: (6S)-10-formyltetrahydrofolate + 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide = (6S)-5,6,7,8-tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Sequence Mass (Da): 57731
Sequence Length: 532
Domain: The IMP cyclohydrolase activity resides in the N-terminal r... |
Q2IKQ7 | MTRRALVSVSDKTGLVPFARRLAALGVELLSTGGTQKALAEAGVPVTGVGDYTQAPEILGGRVKTLHPRVHGGILYRRGLASDEADVKARDIPPIDLVVVNLYPFREAVAAGKPFETCVEEIDIGGPTMVRSAAKNSAHVGVVVDPADYDKVAAELEATRALSDATRFYLMKKAFAHTAAYDAAISEYLTARETPEAAPAHFPATLAAVYTKAYDLRYGENPHQAGAFYRAAREPEEPSVAFAQVLQGKELSYNNLLDLQAALAGVMEFDETACVVIKHNTPCGVSTGRTAGEAFARARECDPVSAFGGIVALNRPVDEA... | Catalytic Activity: (6S)-10-formyltetrahydrofolate + 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide = (6S)-5,6,7,8-tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Sequence Mass (Da): 55984
Sequence Length: 524
Domain: The IMP cyclohydrolase activity resides in the N-terminal r... |
Q8REV6 | MRKRALISVYDKTGILDFAKFLVSKGIEIISTGGTYKYLKENNIEVIEVSKITNFEEMLDGRVKTLHPNIHGGILALRDNEEHMRTLKERNIDTIDYVIVNLYPFFEKVKEDLSFEEKIEFIDIGGPTMLRSAAKSFKNVVVISDVKDYESIKEEINKSDDVSYEARKKLAGKVFNLTSAYDAAISQFLLDEDFSEYLNISYKKFMEMRYGENSHQKAAYYTDNMTDGAMKDFKQLNGKELSYNNIRDMDLAWKVVSEFDEICCCAVKHSTPCGVALGDNVEGAYKKAYETDPVSIFGGIVAFNREVDEATAKLLNEIFL... | Catalytic Activity: (6S)-10-formyltetrahydrofolate + 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide = (6S)-5,6,7,8-tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Sequence Mass (Da): 56927
Sequence Length: 504
Domain: The IMP cyclohydrolase activity resides in the N-terminal r... |
Q9KF53 | MKRRALVSVSNKEGIVPFAKALVEHEVEIVSTGGTKRALQEAGIPVTGISDVTGFPEILDGRVKTLHPNIHGGLLAMRERDEHLAQLNEHHIRPIDFVVVNLYPFQQTIAKPEATFADAIENIDIGGPSMLRAAAKNHQHVTVVVDPVDYETVLKELADQGNVATETKRRLAAKVFRHTAAYDAMIAEYLTDAVGEESPESLTVTFEKKQDLRYGENPHQKATFYQKPLGAKASIAHAKQLHGKELSYNNINDADAALSIVKEFKEPAAVAVKHMNPCGVGTGETIKEAFDKAYEADPVSIFGGIIALNREVDVETAKTL... | Catalytic Activity: (6S)-10-formyltetrahydrofolate + 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide = (6S)-5,6,7,8-tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Sequence Mass (Da): 55578
Sequence Length: 511
Domain: The IMP cyclohydrolase activity resides in the N-terminal r... |
P31939 | MAPGQLALFSVSDKTGLVEFARNLTALGLNLVASGGTAKALRDAGLAVRDVSELTGFPEMLGGRVKTLHPAVHAGILARNIPEDNADMARLDFNLIRVVACNLYPFVKTVASPGVTVEEAVEQIDIGGVTLLRAAAKNHARVTVVCEPEDYVVVSTEMQSSESKDTSLETRRQLALKAFTHTAQYDEAISDYFRKQYSKGVSQMPLRYGMNPHQTPAQLYTLQPKLPITVLNGAPGFINLCDALNAWQLVKELKEALGIPAAASFKHVSPAGAAVGIPLSEDEAKVCMVYDLYKTLTPISAAYARARGADRMSSFGDFVA... | Function: Bifunctional enzyme that catalyzes the last two steps of purine biosynthesis . Acts as a transformylase that incorporates a formyl group to the AMP analog AICAR (5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide) to produce the intermediate formyl-AICAR (FAICAR) . Can use both 10-formyldihydrofolate... |
Q3A2D6 | MAVIKRALISVSDKTGIVEFARELAGYGVEILSTGGTAALLRQEGLAVKDVSEYTGFPEMLDGRVKTLHPKVHGGLLGMRENPAHVAKMKEHGIEPIDMVVVNLYPFEATVAKPDCTLEDAIENIDIGGPTMLRSAAKNNRDVTVVVDHVDYDQVLAEMKGSGGAVSRGTNFKLAVKVYQHTAAYDGAISNWLGQRMGDELADFSDTLTVQFKKVQDMRYGENPHQKAAFYVERDVQEASISTSRQLQGKELSYNNIADTDAALECVKQFNEGPACVIVKHANPCGVALGSNLLEAYNRAFSTDSESAFGGIIAFNRELD... | Catalytic Activity: (6S)-10-formyltetrahydrofolate + 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide = (6S)-5,6,7,8-tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Sequence Mass (Da): 56353
Sequence Length: 521
Domain: The IMP cyclohydrolase activity resides in the N-terminal r... |
P74741 | MARLALLSVSDKSGIVELAQRLVNEFQFDLISSGGTAKTLKEAGVPVTKVSDYTGAPEILGGRVKTLHPRIHGGILARRDLPSDQADLEANDIRPLDLVVVNLYPFEQTIAKPGVTVAEAVEQIDIGGPAMIRATAKNFAHTTVLTNPNQYEAYLQALQEQGEIPLALRQQFAGEAFALTNAYDQAIANYFSGLSGDSANQFGLSGTLRQPLRYGENPHQSAGWYQTGREATGWAKAEKLQGKELSYNNLVDLEAARRIINEFDVREPAAVILKHTNPCGVALAPTLVEAYQKAFNADATSAFGGIVALNQPLDGPTAAA... | Catalytic Activity: (6S)-10-formyltetrahydrofolate + 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide = (6S)-5,6,7,8-tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Sequence Mass (Da): 54565
Sequence Length: 511
Domain: The IMP cyclohydrolase activity resides in the N-terminal r... |
Q9X0X6 | MKRILVSLYEKEKYLDILRELHEKGWEIWASSGTAKFLKSNGIEANDVSTITGFENLLGGLVKTLHPEIFAGILGPEPRWDVVFVDLYPPPDIDIGGVALLRAAAKNWKKVKPAFDMETLKLAIEIDDEETRKYLAGMTFAFTSVYDSIRANQFVEGISLAFKREDLQLRYGENPHEKAFVYGKPAFEILHEGKTISFNNILDAENAWFMAKNLPRMGAVVVKHQSPCGAAIGEDKVEIVKKAIEADDESSFGGILAVNFEMDEEVAKSLKKYLEVIVAPSFTQEAIEVLSKKKVRLLKPGDYASWAGKMAFGSLVLSER... | Catalytic Activity: (6S)-10-formyltetrahydrofolate + 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide = (6S)-5,6,7,8-tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Sequence Mass (Da): 49867
Sequence Length: 452
Domain: The IMP cyclohydrolase activity resides in the N-terminal r... |
Q8DIN5 | MGRMALLSTSNKQGLVELARALVQEFGFTLLSSGGTAKALQTAGIPVTTVSEYTGAPEILGGRVKTLHPKIHGGILARRDRPQDEADLQAQAIHPIDLVVVNLYPFAETIAQPNVTLAEAIEQIDIGGPTLIRAAAKNHAHVTVLVDPSQYETYLQELRLYGDAQPAFRLACAQQAFALTAHYDQAIAEYLQKVTAAGTEPEILPPVFHLTGRQKQVLRYGENPHQRASWYVCGAHPRGWAAAHLLQGKELSYNNLLDLEAARGVISEFLGDSPPAAVIIKHTNPCGVAEGKTLVEAYERAFAADRVSAFGGIVALNRPL... | Catalytic Activity: (6S)-10-formyltetrahydrofolate + 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide = (6S)-5,6,7,8-tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Sequence Mass (Da): 55271
Sequence Length: 518
Domain: The IMP cyclohydrolase activity resides in the N-terminal r... |
B5YLE5 | MIKRALISVSDKRGLVDFAKELDKLGVEILSTGGTAKTLRDSGIKVIDVSQYTGFPEIMDGRVKTLHPLIHGGILARRDNKEDIEAMERLGIKPIDMVVVNLYPFESVAKKHLSQILQPSDLNLQAFLEEAIENIDIGGPTLLRASAKNYKDVIVIVDPDDYSSIIEDIKKGSVSIEKKFELAKKVFSHTARYDALIADYFEKISPSGFKKDWTLPLKMTRTLRYGENPHQKAALYALNESPSLIDADVLQGKEMSFNNYLDTHSAVLLATEFSEPVCVIVKHNNPCGVAIGENIHTAYKKAFECDPVSAFGGIIAFNRV... | Catalytic Activity: (6S)-10-formyltetrahydrofolate + 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide = (6S)-5,6,7,8-tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Sequence Mass (Da): 58100
Sequence Length: 522
Domain: The IMP cyclohydrolase activity resides in the N-terminal r... |
Q116T4 | MKRLALLSTSDKTGLIDLAKSLVTEFDYEIISSGGTAKTLKDAGIYVTKVSDYTGFPEILGGRVKTLHPRIHGGILARKDLPQDVEELNANNIRPIDLVVVNLYPFEETISKPEVTLAEAIEKIDIGGPAMLRASAKNFAHLTVLCNHFQYNSYLEELRKNAGEVSLEFRQKCALAGFKHTATYDQAIATYLQEQQTTSESEKSEKEIFFLSGKKIKTLRYGENPHQYATWYQRGINASGWGASKIIQGKELSYNNLVDLEAARRIIIEFSDAPTVAILKHTNPCGVAVDETILAAYERAFAGDSVSAFGGIVALNKSID... | Catalytic Activity: (6S)-10-formyltetrahydrofolate + 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide = (6S)-5,6,7,8-tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Sequence Mass (Da): 56371
Sequence Length: 517
Domain: The IMP cyclohydrolase activity resides in the N-terminal r... |
Q9PMG4 | MSKADIIVGIQWGDEGKGKVVDKLCENYDFVCRSAGGHNAGHTIWVNGVRYALHLMPSGVLHPRCINIIGNGVVVSPEVLIAEMAQFENLKGRLYISDRAHLNLKHHSLIDIAKEKLKGKNAIGTTGKGIGPSYADKINRTGHRVGELLEPQRLCEALIKDFEANKTFFEMLEIEIPSAEELLADLKRFNEILTPYITDTTRMLWKALDEDKRVLLEGAQGSMLDIDHGTYPYVTSSSTISAGTLTGLGLNPKEAGNIIGIVKAYATRVGNGAFPTEDKGEDGEKIAQIGKEIGVSTGRKRRCGWFDAVAVRYTARLNGL... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
Catalytic Activity: GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate
Sequence Ma... |
P0CH96 | MCDVVLGSQWGDEGKGKLVDLLCDDIDVCARCQGGNNAGHTIVVGKVKYDFHMLPSGLVNPKCQNLVGSGVVIHVPSFFAELENLEAKGLDCRDRLFVSSRAHLVFDFHQRTDKLKEAELSTNKKSIGTTGKGIGPTYSTKASRSGIRVHHLVNPDPEAWEEFKTRYLRLVESRQKRYGEFEYDPKEELARFEKYRETLRPFVVDSVNFMHEAIAANKKILVEGANALMLDIDFGTYPYVTSSSTGIGGVLTGLGIPPRTIRNVYGVVKAYTTRVGEGPFPTEQLNKVGETLQDVGAEYGVTTGRKRRCGWLDLVVLKYS... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Plays an important role in the de novo pathway and in the salvage pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP (By similarity).
Catalytic Activity: GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-... |
Q6FMU9 | MVNVVLGSQWGDEGKGKLVDILVSHYDVVARCAGGNNAGHTIVVDGVKYDFHMLPSGLVNPNCKNLLGNGVVIHIPSFFKELETLESKGLNDARGRLFISSRAHLVFDFHQRTDKLRELELAGRSKDGKNIGTTGKGIGPTYSTKASRSGLRVHHLVNDNPGAWELFESRYRRLLETRKQRYGDFDYDAEEELNRFKQYKESLKPFVVDSVDFLHKSIANNEKILVEGANALMLDIDFGTYPYVTSSNTGIGGVITGLGIPPQKIQEVYGVVKAYTTRVGEGPFPTEQLNEQGEKLQSIGAEFGVTTGRKRRCGWLDLVL... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Plays an important role in the de novo pathway and in the salvage pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP (By similarity).
Catalytic Activity: GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-... |
Q9A3U9 | MANVTVVGAQWGDEGKGKIVDWLSNRADVVVRFQGGHNAGHTLVVDGKVYKLALLPSGVVQGKLSVIGNGVVVDPWHLLSEIDKIADQGVAITPDLLILADNACLILPLHRDLDQAREAASTQKIGTTGRGIGPAYEDKVGRRAIRVADLADPEALKPKIERLLAHHGALRRGLGLPEANAQELFDALMELAPRILSYAQPAWRVLDQAYKAGRRILFEGAQGSLLDVDHGTYPFVTSSNTAAGQASAGSGMGPSATGFVLGIVKAYTTRVGEGPFPAELFDEVGKHLSTVGREVGVNTGRARRCGWFDSVLVRQSVAIN... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
Catalytic Activity: GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate
Sequence Ma... |
Q88SV6 | MASVVVVGSQWGDEGKGKITDFLSQEADVVSRYQGGDNAGHTIVFNGQTFKLRLIPSGIFFHDKLAVIGNGVVLNPKSLVEELQYLRDKGVNPDNLRISNRAHVILPYHITLDGAQEKAKAGGKIGTTNKGIGPAYMDKAERIGIRVADLLDKDTFAALLKRNLAEKNQIITKLYDLEPLKFEDIFDDYYAYGQTLKPFVTDTSVVINDALDNGQRVLFEGAQGVMLDIDQGTYPYVTSSNPVAGGVTIGSGVGPSKIDNCVGVLKAYTSRVGDGPFPTELFDEVGDFIRETAHEYGTVTKRPRRIGWFDSVVLRHAKRV... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
Catalytic Activity: GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate
Sequence Ma... |
Q72PA7 | MPASLVVGTQWGDEGKAKVIDFLSKDTDIIVRYQGGANAGHTVVVHGKKYVFHLVPSGVIYDQTICVIGNGVVLDPLFFIEECDRLQKEGFPVFDKLLLSDACHLLFPYHSQIDSARETTLSQEHKIGTTKKGIGICYADKMMRTGLRVGDLLDTSYQTRLKHLVDEKNRELDKLYGMPPVSYNDINEGLKFFLSKVKKNIINTAYYLDTELKKGKRVLLEGAQGTGLDVDFGTYPYVTSSNPTTGGALIGTGIPFQHLKHVIGITKAYTTRVGEGPFPTELLGEAGEKLRQKGGEFGATTGRPRRCGWFDVEMLKHSVR... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
Catalytic Activity: GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate
Sequence Ma... |
Q2S1J1 | MPVSIVIGSQWGDEGKGKIVDLLSPDVDIVARYQGGANAGHTIVWDEEGETEEFVLHLVPSGIFHEGVTCVIGNGVVLDPKAILEEIEKIESLGIDVEGRLKISHNAHLIMPYHKAIEAAQEEDRASASDDDEIGTTGRGIGPAYTDKFARTGIRVVDLLDEDVLRRKLRRSIEEKNAILRDVYDAEALDVDRIVEEYVEFDQKIDDYVTDTSAYLSRALDDGARVLAEGAQGSLLDVDFGSYPYVTSSHPTAGGCCTGLGVSPTEIDRVLGIAKAYCTRVGNGPFPTELDGEVGQALREKGGEFGATTGRPRRCGWLDL... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
Catalytic Activity: GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate
Sequence Ma... |
O67239 | MKPLVGVIMGSISDWEYMKKAVEVLKEFGVPHEVKVVSAHRTPELMYEYAKTARERGIEVIIAGAGGSAHLPGMTASMTTLPVIGVPIPTKNLGGVDSLYSIVQMPAGIPVATVAIGNATNAGLLAVRILSIKYPEYAKKLDEYTEKLKEKVAKMNEELQKEVENGI | Function: Catalyzes the conversion of N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole ribonucleotide (CAIR).
Catalytic Activity: 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole + H(+) = 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
Sequence Mass (Da): 18037
Sequence Length: 167
... |
O28997 | MSQFLSLRNCLRLTIRLLRQFRRGEGMKAVIIMGSKSDLDYSKKIASKLADFGIDAVMRIASAHKTPEKVLEIIKEYEKEDVVFVTVAGRSNALSGFVDANTSKPVIASPPYSDKFGGADIFSSIRMPSGVAPMLVLEAENAALAVAKIFALKDEGVREKVVQFQENKRREIYKADEELR | Function: Catalyzes the reversible conversion of 5-aminoimidazole ribonucleotide (AIR) and CO(2) to 4-carboxy-5-aminoimidazole ribonucleotide (CAIR).
Catalytic Activity: 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + H(+) = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + CO2
Sequence Mass (Da): 20015
Sequence... |
P12044 | MQPLVGIIMGSTSDWETMKHACDILDELNVPYEKKVVSAHRTPDFMFEYAETARERGIKVIIAGAGGAAHLPGMTAAKTTLPVIGVPVQSKALNGMDSLLSIVQMPGGVPVATTSIGKAGAVNAGLLAAQILSAFDEDLARKLDERRENTKQTVLESSDQLV | Function: Catalyzes the conversion of N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole ribonucleotide (CAIR).
Catalytic Activity: 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole + H(+) = 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
Sequence Mass (Da): 17174
Sequence Length: 162
... |
P52558 | MSVDVAIIMGSQSDWETMHHAADTLEALGISFDARIVSAHRTPDRLVAFAKGAKAEGFKVIIAGAGGAAHLPGMAAAMTPLPVFGVPVQSKALSGQDSLLSIVQMPAGIPVGTLAIGRAGAVNAALLAAAVLALYDEALAARLDEWRKAQTESVAERPSNEA | Function: Catalyzes the conversion of N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole ribonucleotide (CAIR).
Catalytic Activity: 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole + H(+) = 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
Sequence Mass (Da): 16596
Sequence Length: 162
... |
P0AG19 | MSSRNNPARVAIVMGSKSDWATMQFAAEIFEILNVPHHVEVVSAHRTPDKLFSFAESAEENGYQVIIAGAGGAAHLPGMIAAKTLVPVLGVPVQSAALSGVDSLYSIVQMPRGIPVGTLAIGKAGAANAALLAAQILATHDKELHQRLNDWRKAQTDEVLENPDPRGAA | Function: Catalyzes the conversion of N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole ribonucleotide (CAIR).
Catalytic Activity: 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole + H(+) = 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
Sequence Mass (Da): 17780
Sequence Length: 169
... |
P43849 | MSKTAQIAVVMGSKSDWATMQEATQILDELNVPYHVEVVSAHRTPDKLFEFAENAQKNGYKVIIAGAGGAAHLPGMIAAKTLVPVLGVPVKSSMLSGVDSLYSIVQMPKGIPVGTLAIGPAGAANAGLLAAQILAGWDDALFTRLQAFRENQTNMVLDNPDPRT | Function: Catalyzes the conversion of N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole ribonucleotide (CAIR).
Catalytic Activity: 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole + H(+) = 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
Sequence Mass (Da): 17269
Sequence Length: 164
... |
Q58033 | MICIIMGSESDLKIAEKAVNILKEFGVEFEVRVASAHRTPELVEEIVKNSKADVFIAIAGLAAHLPGVVASLTTKPVIAVPVDAKLDGLDALLSSVQMPPGIPVATVGIDRGENAAILALEILALKDENIAKKLIEYREKMKKKVYASDEKVKEMFK | Function: Catalyzes the conversion of N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole ribonucleotide (CAIR).
Catalytic Activity: 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole + H(+) = 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
Sequence Mass (Da): 16951
Sequence Length: 157
... |
P41654 | MKPRVMILLGSASDFRIAEKAMEIFEELRIPYDLRVASAHRTHEKVKAIVSEAVKAGVEVFIGIAGLSAHLPGMISANTHRPVIGVPVDVKLGGLDALFACSQMPFPAPVATVGVDRGENAAILAAQIIGIGDPGVRERVADLRRGFYERVRRDECQVLNSIEGSYYAPLEVEMPPIGDKVPSDSQDDPMVSVIPGSYSDMKIAKKTTMFLERMGISYDLNVISPIRYPERFERYLEKMENVKLFIAISGLSAHVTGAVVALSDRPVIGVPCPLKMNGWDSLLSMINMPPGVPVGTVGVGNGGNAAILAAEMLGIYDEKI... | Function: Catalyzes the conversion of N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole ribonucleotide (CAIR).
Catalytic Activity: 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole + H(+) = 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
Sequence Mass (Da): 36245
Sequence Length: 334
... |
P46702 | MTRQPRVGVIMGSDSDWSVMQDAAHALAEFDIPIEVRVVSAHRTPAEMFDYARNAVDRSIAVIIAGAGGAAHLPGMVASATPLPVIGVPVPLARLDGLDSLLSIVQMPAGVPVATVSIGGARNAGLLAVRILGSSDLQLRAQLVAFQDRLADTVRAKDADLQRFRGKLIGD | Function: Catalyzes the conversion of N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole ribonucleotide (CAIR).
Catalytic Activity: 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole + H(+) = 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
Sequence Mass (Da): 17912
Sequence Length: 171
... |
Q9UY68 | MVKVGMPKVGIIMGSDSDLPVMKEAAKVLEDFEVDYEMKVISAHRTPERLHEYARTAEERGIEVIIAGAGGAAHLPGVLAALTMIPVIGVPIKSKALNGLDSLLSIVQMPPGIPVATVGIDGAKNAALLALEILSIKYPEIKEKLKKYREDMKRKVEEKSKKLEELGWRKYLEG | Function: Catalyzes the conversion of N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole ribonucleotide (CAIR).
Catalytic Activity: 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole + H(+) = 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
Sequence Mass (Da): 19000
Sequence Length: 174
... |
O06456 | MPKVAVIMGSKNDWEYMREAVEILKQFGIDYEARVVSAHRTPEFMMQYAKEAEKRGIEVIIAGAGGAAHLPGMVASLTSLPVIGVPIPSKNLNGLDSLLSIVQMPYGVPVATVAIGGAKNAALLAIRILGIKYKELADKIKKFSEDMRNDVLSTRLEA | Function: Catalyzes the conversion of N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole ribonucleotide (CAIR).
Catalytic Activity: 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole + H(+) = 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
Sequence Mass (Da): 17096
Sequence Length: 158
... |
O27427 | MVLTDSEMEFIRKELGRDPNPLEYGMLDVMFSEHCSYKSSRPVLGLFPTEGEDVIIGPGDDAGVVEITDELALVIGIESHNHPSAIEPYGGAGTGIGGILRDIISMGAMPVALLDSLRFGYLEDQKSRYLFEHVVRGISDYGNRVGVPTVAGEVEFDENFQLNPLVNVMCAGLVPKNDIKRGIAPRPGDVFLLMGGRTGRDGIHGVTFASEELTSSSELEDRPAVQVGDPFTKKMVMEASFEIMDEIEVSGVKDLGGGGLTCCISELVAKCDNGARVSLEAIPLREEGMTPYEIMLSESQERMIFVMAPDDVEAAMEICR... | Function: Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed o... |
A0B5C7 | MKVIGLADSELESSLRKAGIGMSASEARSIASILGRDPTLAELFCYDAMWSEHCSYKSSRAVLREFLPTEGPNVVLGPVEDAGIVSIDDEWCVVISHESHNHPSQILPNEGAATGIGGIVRDVNCMGARVVATADPLRFGDPYGRESSRVRWVAEGVVDGIWQYGNALGVPVIAGDVVFSRCFDYNCLVNVVAIGVVRRDEIIRSRAPPGSGEKGYDVILIGKPTDSSGLGGVIFASDTLREEEEEANRGAVQIPDPFLKNVLFKANEDLFRLVREKGVEIGFKDLGGGGLTCASSEMGAAGGYGMEIDLDRLHVAGEFP... | Function: Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed o... |
Q743F0 | MTVSPTSAPTQAIDTVERAATTPDEPQPFGELGLKDDEYQRIREILGRRPTDTELAMYSVMWSEHCSYKSSKVHLRYFGETTTDEMRAGMLAGIGENAGVVDIGDGWAVTFKVESHNHPSYVEPYQGAATGVGGIVRDIMAMGARPVAVMDQLRFGAADAPDTRRVLDGVVRGIGGYGNSLGLPNIGGETVFDACYAGNPLVNAMCVGVLRQEDLHMAFASGTGNKIILFGARTGLDGIGGVSVLASDTFDAENSRKKLPSVQVGDPFMEKVLIECCLELYAGGLVVGIQDLGGAGLACATSELASAGDGGMEVRLEAVP... | Function: Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed o... |
Q3IQL3 | MSLSPSDRELVTEELGREPTPAEEALFENLWSEHCAYRSSQPLLSAFESEGDRVVVGPGDDAAVVALPDPETGENSDTYITMGIESHNHPSYVDPFDGAATGVGGIVRDTMSMGAYPIALADSLYFGDFDREHSKYLFEGVVEGISHYGNCIGVPTVTGSVAFHDDYEGNPLVNVACVGLTDDERLVTAEAQTPGNKLVLFGNATGRDGLGGASFASEDLDEDAETEDRPAVQVGDPYAEKRLIEANEELVDDSLVRAARDLGAAGLGGASSELVAKGGLGAHIELDRVHQREPNMNALEILLAESQERMCYEVRPEDVD... | Function: Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed o... |
B1L3X7 | MIPRERILSVLSKYDESDVKIGTICSHSSLQIFNGARREGLRSVGIVLRENKPYYESFPRASPDIFIEVDSYGDLLSEETQEELISENVIMIPHGSFVEYVGSENILERFRVPMFGNRLTLYWEGDRRRQRKWLEDAGVPTPRIYRSPEDIDRPVIVKLHGAKGGKGYFKASSPEEFYEKFSELKERGLVGSLEDVVIEEFIVGVRFYPHFFFSPIEGENIADLEGGRLELLGIDRRLEVIDEIHRGLPDLMEDFMDYTVTGNIPVIVREKYLVDLLRDAVKIISSSRRLFYPGLIGPFCMEMIYNPSRGFITFEVSARI... | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Function: Catalyzes the ATP- and formate-dependent formylation of 5-aminoimidazole-4-carboxamide-1-beta-d-ribofuranosyl 5'-monophosphate (AICAR) to 5-formaminoimidazole-4-carboxamide-1-beta-d-ribofuranosyl 5'-monophosphate (FAICAR) in the absence of folates.
Catalytic... |
Q8TU67 | MITKQQVLEFLKNYDLENITIATVCSHSSLQIFDGARKEGFRTLGICVGKPPKFYEAFPKAKPDEYLIVDSYSDIMNKVEELRKKNVIIIPHGSFVAYLGTENFAELTVPTFGNRAVLEWESDRDKEREWLLGAGIHMPGKIDDPRDINGPVMVKYDGAKGGKGFFVAKTYEEFDELVDRTQKYTIQEFITGTRYYLHYFYSPIRNEGYTLSEGSLELLSMDRRVESNADEIFRLGSPRELIEAGIRPTYVVTGNVPLVARESLLPLIFSLGERVVEESLGLFGGMIGAFCLETVFTDSLEIKVFEISARIVAGTNLYIS... | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Function: Catalyzes the ATP- and formate-dependent formylation of 5-aminoimidazole-4-carboxamide-1-beta-d-ribofuranosyl 5'-monophosphate (AICAR) to 5-formaminoimidazole-4-carboxamide-1-beta-d-ribofuranosyl 5'-monophosphate (FAICAR) in the absence of folates.
Catalytic... |
Q57600 | MISKDEILEIFDKYNKDEITIATLGSHTSLHILKGAKLEGFSTVCITMKGRDVPYKRFKVADKFIYVDNFSDIKNEEIQEKLRELNSIVVPHGSFIAYCGLDNVENSFLVPMFGNRRILRWESERSLEGKLLREAGLRVPKKYESPEDIDGTVIVKFPGARGGRGYFIASSTEEFYKKAEDLKKRGILTDEDIANAHIEEYVVGTNFCIHYFYSPLKDEVELLGMDKRYESNIDGLVRIPAKDQLEMNINPSYVITGNIPVVIRESLLPQVFEMGDKLVAKAKELVPPGMIGPFCLQSLCNENLELVVFEMSARVDGGTN... | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Function: Catalyzes the ATP- and formate-dependent formylation of 5-aminoimidazole-4-carboxamide-1-beta-d-ribofuranosyl 5'-monophosphate (AICAR) to 5-formaminoimidazole-4-carboxamide-1-beta-d-ribofuranosyl 5'-monophosphate (FAICAR) in the absence of folates.
Catalytic... |
A9A1D3 | MASIATLGSHCSLQVLKGAKDEGLKTILVCEKKREKLYRRFPFIDELIIVDKFREVLDEKVQSTLEQNDAVLIPHGTLIAQMSSDEIESIKTPIFGNKWILRWESDREMKEKLMREATLPMPKPVTNPSEIEKLSIVKRQGAAGGKGYFMAANEDDYNTKRNQLISEGVISEDETLYIQEYAAGVLAYLTFFYSPLKEELEFYGVDQRHESDIEGLGRIPAEQQMKSNKVPSFNVIGNSPLVLRESLLDEVYTMGENFVEASKRIVAPGMNGPFCIEGVYDENAQFTSFEFSARIVAGSNIYMDGSPYYNLLFNETMSMG... | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Function: Catalyzes the ATP- and formate-dependent formylation of 5-aminoimidazole-4-carboxamide-1-beta-d-ribofuranosyl 5'-monophosphate (AICAR) to 5-formaminoimidazole-4-carboxamide-1-beta-d-ribofuranosyl 5'-monophosphate (FAICAR) in the absence of folates.
Catalytic... |
Q9X0X2 | MKPRACVVVYPGSNCDRDAYHALEINGFEPSYVGLDDKLDDYELIILPGGFSYGDYLRPGAVAAREKIAFEIAKAAERGKLIMGICNGFQILIEMGLLKGALLQNSSGKFICKWVDLIVENNDTPFTNAFEKGEKIRIPIAHGFGRYVKIDDVNVVLRYVKDVNGSDERIAGVLNESGNVFGLMPHPERAVEELIGGEDGKKVFQSILNYLKR | Function: Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed o... |
Q5SI57 | MRWAIVRFPGANCDEDARFALEKAGIRAEFVWHTERDLRGFDGVFLPGGFSYGDYLRAGALAAKSPVMEAVRRFAEEGRYVVGVCNGFQILTEAGLLPGALLANLNLHFTCKEVGVRVERNDLPFTRLYPRGQVLRLPIAHGEGRYYADPETLARLEGEGLVVFRYAPLKDEADYNPNGSLHDIAGIVSEKGNVLGMMPHPERAVDEVLGNTDGLPFFLGLVKEVAR | Function: Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed o... |
Q97C36 | MKQSPKIGILLMEGTNNETEVYYSVKRSGGSPDFIHINDLSAGRKRVSDYDGLIIPGGFSAGDYIRAGVIFAARLGAVAGKEIREFVDDGKPLIGICNGFQVLMEMGLIYDRSKITLTNNESNRFECRYTYMKMTSRNRIFQSGFYGKGVFQVPVAHAEGRIAVSERSVLKKLYENDQVVFKYSNENDVTDEYPWNPNGSIDSVASLSNEAGNVIGLMPHPERIYYRYQAMYLETEKDEVAGKIFYDSLVNYARDRNG | Function: Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed o... |
Q73MV2 | MKPRALVLHATGTNRDGDAARALELAGAEPEIVHINKLKAKEKNWKDYEILVIPGGFSYADALGAGKLFALDLSNYFFDEVSEFVAAGKPVIGICNGFQVLVKSGILPGKEKDGKVILDKDGYKNRQATLTYNKQGRFECRFTTMIPQKSNCIWTKDLKGNIHCPIAHGEGRFLTDSQKTLDDLFEKGQIALVYGGKDAEKSIPANGEYPFNPNGSLADIAGICNTKGNVLGLMPHPENNVVIRERDSEEEKERTKLCLDMWKAGVNYVL | Function: Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed o... |
Q7M9X7 | MSIAVLRFPGTNCEFDMLHSFKLLGVESHLVWHQEKELPKGTHLVVIPGGFSYGDYLRSGAIARFSPIMQAVIRYAKEGGKVLGICNGFQILVESGLLPGALRRNENLHFVSKFQKLAVVSNNNPFLREYAVSETLNIPIAHADGNYFIDAKGLEELKENDQILLTYQGENPNGSIESIAGVCNKEKSVFGLMPHPERAMEPLLGSVDGARMLRGLAC | Function: Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed o... |
P46927 | MTTIGTPLRTNATKVMMLGSGELGKEVVIELQPLGVEVIAVDRYDNAPAQQVAHRAYTISMLDGNALRDLVEKEKPDFIVPEVEAIATATLVELEQEGYNVIPTAKATQLTMNREGIRRLAAEELGLKTSPYRFVDNFEQFQQAIQEIGIPCVVKPIMSSSGHGQSVIKSEADIQQAWDYSQQGGRAGGGRVIVEGFIKFDYEITQLTVRHIHGIVFSSHRHIQVDGDYRESWQPQQMSDIALKKAQETAEKITSALGGRGIFGVELFVCGDEIIFNEVSPRPHDTGIVTMASQELSQFALHARAILGLPIPEIYRISPA... | Function: Involved in the de novo purine biosynthesis. Catalyzes the transfer of formate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR). Formate is provided by PurU via hydrolysis of 10-formyl-tetrahydrofolate.
Catalytic Activity: ATP + formate + N(1)-(5-phospho-beta-D-ri... |
P31115 | MSNFIRRLVGKMKAISTGTNAIVSKKDSIYANWSKEQLIRRITELENANKPHSEKFQHIEDNKKRKISQEEVTRSKAKKAPKKFDFSKHNTRFIALRFAYLGWNYNGLAVQKEYTPLPTVEGTILEAMNKCKLVPSMVLQDYKFSRCGRTDKGVSAMNQVISLEVRSNLTDEEQRDPTNDSREIPYVHVLNQLLPDDIRISAVCLRPPPNFDARFSCVHRHYKYIFNGKNLNIEKMSKAASYFVGERDFRNFCKLDGSKQITNFKRTIISSKILPLSETFYCFDLVGSAFLWHQVRCMMAILFLVGQSLEVPEIVLRLTD... | Function: Formation of pseudouridines at positions 38 and 39 in the anticodon stem and loop of transfer RNAs.
Catalytic Activity: uridine(38/39) in tRNA = pseudouridine(38/39) in tRNA
Sequence Mass (Da): 50889
Sequence Length: 442
Subcellular Location: Nucleus
EC: 5.4.99.45
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Q9LT72 | MAKWRLATATLRRQLQSSSPTISTFKNPTKALSAAAHQSTRSYSTTQTDDSRGKWLTLPPFSPTIDGTAVGKDLLSDGDSVKSSTDNSKTTALRWILRCRPDLPRTLVQKLFRLRQVRREMSMSVDGDELQRSQLKRVAAKESLNVGDRIYLPLSVDNDTPQTPPAKKESFQCSDEERKFVCSLVLYKDPAIIVLNKPHGLAVQGGSGIKTSIDELAASCLKFDKSESPRLVHRLDRDCSGLLVLARTQTAATVLHSIFREKTTGASAYGVKKNVKSLKRKYMALVIGCPPRQRGQISAPLRKVVVDDGKSERITVNDNG... | Catalytic Activity: a uridine in RNA = a pseudouridine in RNA
Sequence Mass (Da): 52965
Sequence Length: 477
Subcellular Location: Mitochondrion
EC: 5.4.99.-
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Q69K07 | MAALLYLRRRAAAAALAGVAPKPQWLATAARRGALVSGDDGGETGERGKSPWLQLPPFAPLDAAAAARAISRGGGEGGDGEQGATAIKWVRRCCPDLPTSLVQKLFRLRKVKKNVVTAEISSADASAEQHRLRRVSAKDQLMPGDILFLPVNLKESSVAEKTKKFDNRNEINFLRGLEIYKDEAIIVVNKPPGMPVQGGVGIKNSIDVLASMFEENSSEAPRLVHRLDRDCSGILVLGRNQLSTSMLHAIFREKTADALADGTQHVLQRKYVALVIGTPRHPKGLLSAPLAKILLQDGKSERLTIRASSNAASVQDALTE... | Catalytic Activity: a uridine in RNA = a pseudouridine in RNA
Sequence Mass (Da): 49035
Sequence Length: 448
Subcellular Location: Mitochondrion
EC: 5.4.99.-
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O59721 | MTVTNTYNPTLFFTRVVFQRITKFTAKANEENEILFYALFVADLCLDMKGGLIAINKPSGRTSAQCLNELKKIISNSELAQYFRPAPPHPNDRNRRRRKSNRLPDIKIGHGGTLDPLASGVLVVGLGTGTKQLSSLLSCMKTYRATALFGCSTDTYDSAGKIIKIAVHIPTKEEILSGLDAFRGDISQLPPLYSALHIQGKRLYEYAREGIPLPESIKARSMHCEELILKDFIPKEEHTYTDPDEFASKEAIESEELLRPIEGGAERHDLLAKTEQDINPQDGDEKINAKSPTTNSVTDVAKDQTVTNPKKRKFEVTDLA... | Function: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs. Also catalyzes pseudouridylation of mRNAs with the consensus sequence 5'-GGUUCRA-3'.
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Mass (Da): 45166
Sequence Length: 407
Subcellular Loc... |
P48567 | MNGIFAIEKPSGITSNQFMLKLQHALTKSQVFSKEIQRATAERKQQYEKQTGKKASKRKLRKVSKVKMGHGGTLDPLASGVLVIGIGAGTKKLANYLSGTVKVYESEALFGVSTTSGDVEGEILSQNSVKHLNFDDLKTVEEKFVGQLKQTPPIYAALKMDGKPLHEYAREGKPLPRAIEPRQVTIYDLKVFSDSLKRDHDYPLLRPTTEEAVDTVKNLNANMLNDVLYFSKEYTEKHGLDSEVAKVEEPFPLSEQEEQEIQKEGDSYRAPKLHFKANVSSGTYIRSLVSDIGKSMRSSCYMVKLIRLQQQDWSLEKNNV... | Function: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs . Also catalyzes pseudouridylation of mRNAs with the consensus sequence 5'-GGUUCRA-3' .
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Mass (Da): 45273
Sequence Length: 403
Subcellular L... |
Q750S3 | MNRWAVPILHEHKHYYIVNKVHGIVCQPPDLRTWYKYHDYEPPVLLDLLRKQHPNFGGEVWRTVHRLDEPVTGGVLVSRNKRAAAMFSRSLALGGNRGFPLTRRYVALLAREAKGLPSEGRITMGDMITDYKRLENDLVLLQLQTGRKHQIRKQMAQVFGQPVVNDKMYGGDSVDGIVDNLIGLHSAFIGAQCGLQARTYLIPIPRTQDAFKLWDKYIDEQGGFIPSVQKELRDFSLPSKLENTITLLSGGQGGIQISYK | Function: Pseudouridylate synthase responsible for the pseudouridine-2819 formation in mitochondrial 21S rRNA. May modulate the efficiency or the fidelity of the mitochondrial translation machinery.
Catalytic Activity: uridine(2819) in 21S rRNA = pseudouridine(2819) in 21S rRNA
Sequence Mass (Da): 29476
Sequence Length... |
Q5A0Y2 | MKLDLVKRTFNYAVVNKPSGMVCDASHTNNIITALTNEFTKILPSVNSSQFRLVQRLDRFVTGGLVVARNKKWADKVRKSFFQEGTLRLTRRYVGLIALDQIPESTQGTIDFPIQALEKDYRGKNKSRELFTYSAVTHYKLIPSARRTIKGVFPVFQQGPILPIILELETGRKNQIRDHIIQKFGVPLLNDDNFSDFKLNSEIPKDVNSKLYKSNQIALHSGLVIMENNGISQQFLFPVNNAYDRELW | Function: Pseudouridylate synthase responsible for the pseudouridine-2819 formation in mitochondrial 21S rRNA. May modulate the efficiency or the fidelity of the mitochondrial translation machinery.
Catalytic Activity: uridine(2819) in 21S rRNA = pseudouridine(2819) in 21S rRNA
Sequence Mass (Da): 28391
Sequence Length... |
Q6FS81 | MSARLKVVYDGMHYMIVYKSAGVLSQPGLASDSRPVLMSELRGLLSETLDLYSVQRLDACVTGGTVVAKNKRAAMMFSRYLKQGGGSGYGLTRRYLARINAQPVCDEGTIESPGMVTYYRRVRDDCVVVELKTGKKHQIRKHLALNLNCPIVNDTYYGGSVVKGVNGQIALHSAFVRTRIGKNMQDHLVGIEPQEQTLWKSILTENGMLPDDIVRTLTRDKLF | Function: Pseudouridylate synthase responsible for the pseudouridine-2819 formation in mitochondrial 21S rRNA. May modulate the efficiency or the fidelity of the mitochondrial translation machinery.
Catalytic Activity: uridine(2819) in 21S rRNA = pseudouridine(2819) in 21S rRNA
Sequence Mass (Da): 24814
Sequence Length... |
Q6BNX8 | MKPTFLKCLQGIDKNHAYRQINIIDIHSRYLIINKPSGIQCNGTKSHSNYLLPQLYKQLKAHFSANNPNYKLNPDQYKVVHRLDKYVSGGLIIARGKNANAFRKSFSNQNTNLSVKRKYIGLVPIPNTVSFKQHLHEFGDLKVQHENEVRYLNRPESVTDKKGLIFKDDSLTEGIINFDIVALPKDDRRNKNTGELVTYSALTKFKILHSMSQVPTNEQISRFPKLYKNKTIYPIIIELETGRKNQIRDHILQAFKVSLLNDDKFIDFKMVQKSNTANINSEVYNSNQIGLHSAYISISKSSFANEYVIPIPEGDEYLWK... | Function: Pseudouridylate synthase responsible for the pseudouridine-2819 formation in mitochondrial 21S rRNA. May modulate the efficiency or the fidelity of the mitochondrial translation machinery.
Catalytic Activity: uridine(2819) in 21S rRNA = pseudouridine(2819) in 21S rRNA
Sequence Mass (Da): 39114
Sequence Length... |
Q6CQC4 | MLRRGFIKQPPFVKIFKIVSPESTNAKATHCEVEFPLKVQELWRDKHHVIFNKPPLALSQLPDKRTWYNTHDYDPPVLLDIVQSSSGSILKDGTYEPSYYPIHRIDTPVSGGIVYAVNKQSAQQFSRNLRYGGNKGFSLTRKYVAKVGKSKTANECKEGLIKWNGAITYFQRVDNEHLILQLVTGKKHQIRKLTQQVLDSPIYNDLKYGGKKVFDSDFQIALHSAYIRTKIGFNIHEQIIPVPDGFRMIWGESVDQNGNFNEDITRVLKEDWAGTIKECLKKLKIQETKLADNQLIFVS | Function: Pseudouridylate synthase responsible for the pseudouridine-2819 formation in mitochondrial 21S rRNA. May modulate the efficiency or the fidelity of the mitochondrial translation machinery.
Catalytic Activity: uridine(2819) in 21S rRNA = pseudouridine(2819) in 21S rRNA
Sequence Mass (Da): 34308
Sequence Length... |
Q06244 | MSLKKQIPIIFENTHYFIVNKPPGIPSQPPDCRTWGRTHPNLDPTPLLERFKAIYYSHREVELCRTVHRLDHCVTGGMLIAKTKDGSVKFSRFLQKGGNNGYKLQRKYVAIVESSGRFNKPNNYEIKYGPKYNFLISHGGREITKFKEVDENCIVLQLVTGKKHQIRNHVSQILNQPILNDKRHGSTVNFPELFNDQIALHSACIITKIGLQTKTHLIPMEHNNTGQLWSRKYVNEEGEFTLPIKEVLLENWDQ | Function: Pseudouridylate synthase responsible for the pseudouridine-2819 formation in mitochondrial 21S rRNA. May modulate the efficiency or the fidelity of the mitochondrial translation machinery.
Catalytic Activity: uridine(2819) in 21S rRNA = pseudouridine(2819) in 21S rRNA
Sequence Mass (Da): 29359
Sequence Length... |
Q9SVS0 | MASPALTGGYRNLTAPVSLLRTLASTRVTTPLFRSNKHSPRFISSPKRFTCLSLLKTDSQNQTTLSSSSNSGYHEYNRLMPCPAYNLPPRIEHMVVLEDDVLVSEFISKQLDLPPLYVADLIRFGAVHYALVCPKPPPTATPEEIILFEEVTSPSVLKKRSSIKGKTVREAQKTFRVTHTNQYAEAGTYLRVHVHPKRSPRCYEIDWKSRIVAVTDSYVILDKPAGTTVGGTTDNIEESCATFASRALDLPEPLKTTHQIDNCTEGCVVFARTKEYCSVFHTKIRNKEVKKLYRALAAAPLPIGIISHYMRPKNMAPRLV... | Catalytic Activity: a uridine in RNA = a pseudouridine in RNA
Sequence Mass (Da): 52938
Sequence Length: 472
Subcellular Location: Plastid
EC: 5.4.99.-
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A3BN26 | MPKAAASLASLLPQLWHRPVQPPPFLHRALSSSSPLLRRHRAALHSPAAPLSAAAVSTSAATVEAPATAAYPVYGRLLPCPLQDDPPRIEHLVAREDEVAVDFISRSLTLPPLYVADLIKFGAVYYALVAPQPPPHAAPEHVRIFREVTEPSVLCRRKSIKGKTVREAQKTFRVTDPNQRLEAGTYLRVHVHPKRFPRCYEIDWKSRVIAVTDNYVVLDKPAATSVGGATDNIEESCVVFTSRALGLETPLMTTHQIDNCSEGCVVLSKTKEFCSVFHGMIREKQVNKRYLALTTAPVSTGIITHYMRPINRAPRLVSED... | Catalytic Activity: a uridine in RNA = a pseudouridine in RNA
Sequence Mass (Da): 52881
Sequence Length: 477
Subcellular Location: Plastid
EC: 5.4.99.-
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P53294 | MSTIKVIEVYTQNGLRKVRPYYNRRSAFVKGRWLGKLLIDVLVSEFKLRPRAYYLDQIRKGTYRLIRDGVPLVPDHLMTTIIKNHDVLETTTHKHEPPVKQWCSQEVEAEDLPGRIAGFNIVFEDESILVIDKPSGIPVHPTGQFYQNTITELLKLHGVDALPCYRLDKITSGLLILAKNSQSAGEIQKSIRSRDMIKIYLARVKGRFPHSELILDNENAAETTFEDTSKVTVEMTPIYSIDPKRQFPVGLSTSKDAITKFYPIRYFSHADETVVACKPITGRTHQIRIHLARLGHPIVNDSVYCSHITKYPERLKFITQ... | Function: Catalyzes the formation of pseudouridine at position 31 in the psi GC loop of tRNAS.
Catalytic Activity: uridine(31) in tRNA = pseudouridine(31) in tRNA
Sequence Mass (Da): 46816
Sequence Length: 404
Subcellular Location: Cytoplasm
EC: 5.4.99.42
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Q1L8I0 | MERNTLSCFISDHEGFNGTIKNSPQDFVVIEIDTNGQFVNSVNTEEEERPCQTTKRIGKLKPSKPDDTDSLIQDCFDLNLILGLSVNRELEHFTNKLKVKPCSDDQEKVELSLGTFPDKHMRAVVHKAVRFNFPFLQTLTNQSEIRVREDPDFQELAGLASEGEAEDFFRFIDAKTPGSVFTFLPDDSKEHRTSVHHFVSRRFGKLVETKSFVDQQKTCITVRLRERGKQAKKRTMADCQMQEESLYTAFTLRKENLETLEAISYMAAVLGVLPSDFTYAGIKDKRAITYQAMVVKKISPERLLEKGSEFERRGMEISRV... | Function: Pseudouridine synthase that catalyzes pseudouridylation of mRNAs.
Catalytic Activity: a uridine in mRNA = a pseudouridine in mRNA
Sequence Mass (Da): 73112
Sequence Length: 643
EC: 5.4.99.-
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Q9H0K6 | MEEDTDYRIRFSSLCFFNDHVGFHGTIKSSPSDFIVIEIDEQGQLVNKTIDEPIFKISEIQLEPNNFPKKPKLDLQNLSLEDGRNQEVHTLIKYTDGDQNHQSGSEKEDTIVDGTSKCEEKADVLSSFLDEKTHELLNNFACDVREKWLSKTELIGLPPEFSIGRILDKNQRASLHSAIRQKFPFLVTVGKNSEIVVKPNLEYKELCHLVSEEEAFDFFKYLDAKKENSKFTFKPDTNKDHRKAVHHFVNKKFGNLVETKSFSKMNCSAGNPNVVVTVRFREKAHKRGKRPLSECQEGKVIYTAFTLRKENLEMFEAIGF... | Function: Pseudouridine synthase that catalyzes pseudouridylation of mRNAs.
Catalytic Activity: a uridine in mRNA = a pseudouridine in mRNA
Sequence Mass (Da): 80700
Sequence Length: 701
EC: 5.4.99.-
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A2XFQ8 | MAAAAAAAGSSDSRKPAAHPPPRDFLVHVEAYLSRRDGVDKLLKISRYAARLALAAGPLPPAASARLKSFESSVGLSRKAFRLGKFVQNVNALRAHPHPPPAVALLAYGGEGVYYFLEQFVWLAKAGLLPAHLLPRLQRLSAWAELLGYVGSITIKLEEIGKLESSVKMRLKEGCREESDVVRTLRVKLLLKRMSVVQDVADAVMALGDVTDGKGLLGSSTLMASAGLLSALISAHKNWNSC | Function: Involved in peroxisomal proliferation.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 25931
Sequence Length: 242
Subcellular Location: Peroxisome membrane
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Q01IH3 | MSAGDTLDKLVVFLAKRDGIDKLVKTFQYVSKLAHWAAESSSPGLAGRAKNWETSAGLSRKAFRTGRFLTGLNGLRRAPGEFGALAVLANAGEMVYFFFDHFTWLSRVGVLDAWLARRMSFISAFGESVGYVFFIAMDLIMIRRGLRQERKLLREGGKDKDKEVKKIRMDRVMRLMATAANVADLVIGIADIEPNPFCNHAVTLGISGLVSAWAGWYRNWPS | Function: Involved in peroxisomal proliferation.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 24711
Sequence Length: 222
Subcellular Location: Peroxisome membrane
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Q5VRJ8 | MSSLESARADLALLILYLNKAEARDKICRAIQYGSKFVSNGQPGPAQNVDKSTSLARKVFRLFKFVNDLHALISPPAKGTPLPLILLGKSKNALLSTFLFLDQIVWAGRTGIYKNKERAEFLSKIAFYCFLGSNTCTSIIEVAELQRLSKSMKKLEKELKHQELLKNEQYQMKLQKCNERRLALIKSSLDIVVAIGLLQLAPKKVTPRVTGAFGFASSLIACYQLLPAPAKSK | Function: Involved in peroxisomal proliferation.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 25889
Sequence Length: 233
Subcellular Location: Peroxisome membrane
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Q9FZF1 | MATKAPEKITKPKDRDFLNHLETYLSKRDGVDKLLKISRYATKIILASSLIPETRSIIPRLKSFESSVGVSRKAFRLGKFVQDINALRSSRWDSNHELVLLIIAYGGEGLYYFVEQFIWLTKSGLIDAKHSKWLQKISAWAELVGYVGSVSIKIRDLRKLNDEESCVASTIEISVSRGLACDGEDEKMKMIKEKKTLKVLSILQDLADGLMTIADIRDGKGVLSAPNVISSAGLFSAIVSTHKNWISC | Function: Involved in peroxisomal proliferation. Promotes peroxisomal duplication, aggregation or elongation without fission.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 27677
Sequence Length: 248
Subcellular Location: Peroxisome membrane
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O75192 | MDAFTRFTNQTQGRDRLFRATQYTCMLLRYLLEPKAGKEKVVMKLKKLESSVSTGRKWFRLGNVVHAIQATEQSIHATDLVPRLCLTLANLNRVIYFICDTILWVRSVGLTSGINKEKWRTRAAHHYYYSLLLSLVRDLYEISLQMKRVTCDRAKKEKSASQDPLWFSVAEEETEWLQSFLLLLFRSLKQHPPLLLDTVKNLCDILNPLDQLGIYKSNPGIIGLGGLVSSIAGMITVAYPQMKLKTR | Function: May be involved in peroxisomal proliferation and may regulate peroxisomes division . May mediate binding of coatomer proteins to the peroxisomal membrane (By similarity). Promotes membrane protrusion and elongation on the peroxisomal surface .
PTM: Seems not to be N-glycosylated.
Location Topology: Multi-pass... |
O70597 | MDAFIRVANQSQGRDRLFRATQHACMLLRYLLESKAGKEAVVTKLKNLETSVSTGRKWFRLGNVLHAIQATEQSIQATDLVPRLCLTLANLNRVVYYICDTVLWAKSVGLTSGINREKWQMRAARHYYYFLLLSLVRDLYEVLLHMGQVARDRAKREKSSGDPPKYSVANEESEWLQSFLLLLFQSLKRNPPLFLDTVKNFCDILIPLNQLGIYKSNLGVVGFGGLVSSVAGLITVVYPQLKLKAR | Function: May be involved in peroxisomal proliferation and may regulate peroxisomes division. May mediate binding of coatomer proteins to the peroxisomal membrane . Promotes membrane protrusion and elongation on the peroxisomal surface.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 27923
Sequence L... |
Q9STY0 | MSLDTVDKLVVFLAKRDGIDKLVKTFQYVAKLACWHVEATRPEAADRFKKWEVASGLSRKAFRTGRSLTGFNALRRNPGATPMIRFLAVLANSGEMVYFFFDHFLWLSRIGSIDAKLAKKMSFISAFGESFGYTFFIIIDCIFIKQRLKSLKKLQHSTDEPKEEIGAKISEIRGDIVMRLMGISANVADLLIALAEIHPNPFCNHTITLGISGLVSAWAGWYRNWPS | Function: Involved in peroxisomal proliferation. Promotes peroxisomal duplication, aggregation or elongation without fission.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 25598
Sequence Length: 227
Subcellular Location: Peroxisome membrane
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Q00317 | MVYGELIYHPVVTKLLKFLDSSASREKLLRLLQYLCRFLTFYTFKRNFNIETIQLIKKIQSSIGISRKPLRFLKNLPHLKNLNKIYSNELLDSTLKIGDLIKNFGYALYFQFDTLQWLKLLGLLTSKNSGSLYFKIDKLAANFWLIGLTGSIITDLRNLKISYDSNKALLNEINSQNNNSNNDTLDEKLIEQNNDLILKNNEKINLNKRDLFKNILDSLIALKGSQLIDLNDGVLGFAGIITSIIGIEDIWNATKA | Function: Involved in peroxisomal proliferation. Could participate in peroxisomal elongation or fission. May be involved in parceling of peroxisomes into regular quanta.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 29339
Sequence Length: 256
Subcellular Location: Peroxisome membrane
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O96011 | MDAWVRFSAQSQARERLCRAAQYACSLLGHALQRHGASPELQKQIRQLESHLSLGRKLLRLGNSADALESAKRAVHLSDVVLRFCITVSHLNRALYFACDNVLWAGKSGLAPRVDQEKWAQRSFRYYLFSLIMNLSRDAYEIRLLMEQESSACSRRLKGSGGGVPGGSETGGLGGPGTPGGGLPQLALKLRLQVLLLARVLRGHPPLLLDVVRNACDLFIPLDKLGLWRCGPGIVGLCGLVSSILSILTLIYPWLRLKP | Function: Involved in peroxisomal proliferation . May regulate peroxisome division by recruiting the dynamin-related GTPase DNM1L to the peroxisomal membrane . Promotes membrane protrusion and elongation on the peroxisomal surface .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 28431
Sequence Leng... |
Q96HA9 | MASLSGLASALESYRGRDRLIRVLGYCCQLVGGVLVEQCPARSEVGTRLLVVSTQLSHCRTILRLFDDLAMFVYTKQYGLGAQEEDAFVRCVSVLGNLADQLYYPCEHVAWAADARVLHVDSSRWWTLSTTLWALSLLLGVARSLWMLLKLRQRLRSPTAPFTSPLPRGKRRAMEAQMQSEALSLLSNLADLANAVHWLPRGVLWAGRFPPWLVGLMGTISSILSMYQAARAGGQAEATTP | Function: Promotes membrane protrusion and elongation on the peroxisomal surface.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26636
Sequence Length: 241
Subcellular Location: Peroxisome membrane
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Q8RG75 | MKFFVDLNSDIGEGYGAYKLGMDEEIMKCVTSVNCACGWHAGDPLIMDKTIKIAKENNVAVGAHPGYPDLLGFGRRKMVVTPDEARAYMLYQLGALNAFAKANETKLQHMKLHGAFYNMAAVEKDLADAVLDGIEQFDKDIIVMTLSGSYMAKEGKRRGLKVAEEVFADRGYNPDGTLVNRNLPGAFVKEPDEAIARVIKMIKTKKVTAVNGEEIDIAADSICVHGDNPKAIEFVDRIRKSLIADGIEVKSLYEFIK | Function: Catalyzes the cleavage of 5-oxoproline to form L-glutamate coupled to the hydrolysis of ATP to ADP and inorganic phosphate.
Catalytic Activity: 5-oxo-L-proline + ATP + 2 H2O = ADP + H(+) + L-glutamate + phosphate
Sequence Mass (Da): 28314
Sequence Length: 257
EC: 3.5.2.9
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Q5FUE6 | MTAKTIDLNADLGESFGHYTMGNDSAMLDIVTSANVACGFHGGDPEVMAETFRIAREKGVSVGSHPGFPDLWGFGRRVMPFTPAQIERIVAYQIGAAQALATYSGHRMTYMKTHGALGNLTERDPAVAEAIVNAVKAVDANLPIMAIALSHLERIGRERGLTVFSEIFADRAYTEDGHLVSRKEPGAVLHDADFAAARAVRMVQNGAIETISGKMLPTRIDTICVHGDNAESVEVARKVRAGFEAAGIAVRALT | Function: Catalyzes the cleavage of 5-oxoproline to form L-glutamate coupled to the hydrolysis of ATP to ADP and inorganic phosphate.
Catalytic Activity: 5-oxo-L-proline + ATP + 2 H2O = ADP + H(+) + L-glutamate + phosphate
Sequence Mass (Da): 27165
Sequence Length: 254
EC: 3.5.2.9
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P45347 | MKKIDLNADIAEGFPFDESLLQLLSSANVACGLHAGGAKEMQSAVKFAKENKVRIGAHPSFPDRENFGRTAMALSSQELIAHLRYQLGALKAICDGEGAVISYVKPHGALYNQAAKDEKIARLIAQTVYQFDPNLKLMGLAGSLMLRIAEEEKLQTISEVFADRHYMPDGSLVPRSQPNAMVESDKEAIQQVLQMVTKGQVNAIDGSLVPVKAESICLHGDNQHSLQFAKRIVEELEKNHIKITA | Function: Catalyzes the cleavage of 5-oxoproline to form L-glutamate coupled to the hydrolysis of ATP to ADP and inorganic phosphate.
Catalytic Activity: 5-oxo-L-proline + ATP + 2 H2O = ADP + H(+) + L-glutamate + phosphate
Sequence Mass (Da): 26822
Sequence Length: 245
EC: 3.5.2.9
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B9DHG0 | MFESNMVLQTLSSSSPPIHRLYLHHSQILPSSGSPSKISLQIHGRTLAIRSFHDYVFAEISARGLPALNKASLKKLPIKGSTFLLGQSLLMVSAHPQLAAAAEIIKPEPIYEVGELFELSIQLSYLLLLLGLLGVGTFYVIRQVLVRRELDLSAKELQEQVRSGDASATELFELGAVMLRRKFYPAANKFLQQAIQKWDGDDQDLAQVYNALGVSYVREDKLDKGIAQFEMAVKLQPGYVTAWNNLGDAYEKKKELPLALNAFEEVLLFDPNNKVARPRRDALKDRVKLYKGVVAVKSKKR | Function: Nuclear genome-encoded factor required for the accumulation of photosystem I (PSI). Functions as PSI biogenesis factor . Cooperates with PSA3 to promote the stable assembly of PSI in the thylakoid membrane. May target primarily the PsaC subunit .
Location Topology: Multi-pass membrane protein
Sequence Mass (D... |
C0PEY7 | MARLLLFPSQACVDPGRHLLLHPPVSRPRAVRSGPPPAAPRRTGVVSLPGRCPPPLCWNHHPFLPCRSSKRGWVVFASENVQEISSHLPRKDERRSGNLLLRFSALPYCTMAWLSTAQLAQSSVGEKLNMVYEVGELFELGIQLSYLLILIGLLGAGTFFVIRQVLVRRELDLSAKELQEQVRSGDASATEYFELGAVMLRRKFYPAAIKYLQQAIDKWDRDEQDLAQVYNALGVSYKRENKLDKAIQQFQKAVELQPGYVTAWNNLGDAYEQQKDLKSALKAFEEVLLFDPNNKVARPRVDDLRPRVSMYKGVPVKSEK... | Function: Nuclear genome-encoded factor required for the accumulation of photosystem I (PSI). Functions as PSI biogenesis factor. Cooperates with PSA3 to promote the stable assembly of PSI in the thylakoid membrane. May target primarily the PsaC subunit.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da)... |
P11216 | MAKPLTDSEKRKQISVRGLAGLGDVAEVRKSFNRHLHFTLVKDRNVATPRDYFFALAHTVRDHLVGRWIRTQQHYYERDPKRIYYLSLEFYMGRTLQNTMVNLGLQNACDEAIYQLGLDLEELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYEFGIFNQKIVNGWQVEEADDWLRYGNPWEKARPEYMLPVHFYGRVEHTPDGVKWLDTQVVLAMPYDTPVPGYKNNTVNTMRLWSAKAPNDFKLQDFNVGDYIEAVLDRNLAENISRVLYPNDNFFEGKELRLKQEYFVVAATLQDIIRRFKSSKFGCR... | Function: Glycogen phosphorylase that regulates glycogen mobilization . Phosphorylase is an important allosteric enzyme in carbohydrate metabolism . Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates . However, all known phosphorylases share catalytic and structural pro... |
P06737 | MAKPLTDQEKRRQISIRGIVGVENVAELKKSFNRHLHFTLVKDRNVATTRDYYFALAHTVRDHLVGRWIRTQQHYYDKCPKRVYYLSLEFYMGRTLQNTMINLGLQNACDEAIYQLGLDIEELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYEYGIFNQKIRDGWQVEEADDWLRYGNPWEKSRPEFMLPVHFYGKVEHTNTGTKWIDTQVVLALPYDTPVPGYMNNTVNTMRLWSARAPNDFNLRDFNVGDYIQAVLDRNLAENISRVLYPNDNFFEGKELRLKQEYFVVAATLQDIIRRFKASKFGST... | Function: Allosteric enzyme that catalyzes the rate-limiting step in glycogen catabolism, the phosphorolytic cleavage of glycogen to produce glucose-1-phosphate, and plays a central role in maintaining cellular and organismal glucose homeostasis.
PTM: Acetylation, which is up-regulated by glucose and insulin and down-r... |
P11217 | MSRPLSDQEKRKQISVRGLAGVENVTELKKNFNRHLHFTLVKDRNVATPRDYYFALAHTVRDHLVGRWIRTQQHYYEKDPKRIYYLSLEFYMGRTLQNTMVNLALENACDEATYQLGLDMEELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYEFGIFNQKISGGWQMEEADDWLRYGNPWEKARPEFTLPVHFYGHVEHTSQGAKWVDTQVVLAMPYDTPVPGYRNNVVNTMRLWSAKAPNDFNLKDFNVGGYIQAVLDRNLAENISRVLYPNDNFFEGKELRLKQEYFVVAATLQDIIRRFKSSKFGCR... | Function: Allosteric enzyme that catalyzes the rate-limiting step in glycogen catabolism, the phosphorolytic cleavage of glycogen to produce glucose-1-phosphate, and plays a central role in maintaining cellular and organismal glucose homeostasis.
PTM: Phosphorylation of Ser-15 converts phosphorylase B (unphosphorylated... |
Q9WUB3 | MSRPLSDQDKRKQISVRGLAGVENVSELKKNFNRHLHFTLVKDRNVATPRDYYFALAHTVRDHLVGRWIRTQQHYYEKDPKRIYYLSLEFYMGRTLQNTMVNLALENACDEATYQLGLDMEELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYEFGIFNQKICGGWQMEEADDWLRYGNPWEKARPEFTLPVHFYGRVEHTSQGAKWVDTQVVLAMPYDTPVPGYRNNVVNTMRLWSAKAPNDFNLKDFNVGGYIQAVLDRNLAENISRVLYPNDNFFEGKELRLKQEYFVVAATLQDIIRRFKSSKFGSR... | Function: Allosteric enzyme that catalyzes the rate-limiting step in glycogen catabolism, the phosphorolytic cleavage of glycogen to produce glucose-1-phosphate, and plays a central role in maintaining cellular and organismal glucose homeostasis.
PTM: Phosphorylation of Ser-15 converts phosphorylase B (unphosphorylated... |
A4XKT1 | MKHLLGLRDLSKEDIIKILNLAKDMKTILKSETKKTPHLQGYSVVTLFYENSTRTRTSFELAAKFMSANTTSISVQTSSVQKGESLLDTVKTLEALKTDVLIVRHSVSGVPHFIAKNCSFSVINAGDGMNEHPTQALLDMFTIRERLGTIEKLKIAIIGDILHSRVARSNIWGLSKFDNQITVFGPQTLIPPYIENFAKVASSLEEAVSGKDIVIDLRIQLERQKRGFITSKQEYYKFYGLNEDIMKFISDSTLIMHPGPVNRGVEISSEVMQLKNSTIDEQVTNGIAVRMAVLYLCTRKEGIYR | Catalytic Activity: carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-aspartate + phosphate
Sequence Mass (Da): 34247
Sequence Length: 305
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3.
EC: 2.1.3.2
|
A0RQX6 | MSYVKKDLISTKDLSKDDIFSILSLAKDYKALNLEPVKKDPILKGVTVVNAFFENSTRTRTSFEIAAKRLGADAINFSSSTSSTNKGETLIDTIHNIEAMKTDIFIVRHYSSGAAKFVTKNTPSCVVNAGDGCNEHPTQALLDLLTIYEAKGSFSGLSVTIIGDIFHSRVARSNIYAMQTLGIKVKLFGPPMFMQNAEVFGCHICKDMDEAVMGSDAIIMLRIQLERSDGEVAFPSIREYSKYFGLTKTRMQKAKDDVIILHPGPINRGVEINSDVADDARFSSILDQVENGVAIRMAVLKTIYQNKFKA | Catalytic Activity: carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-aspartate + phosphate
Sequence Mass (Da): 34211
Sequence Length: 310
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3.
EC: 2.1.3.2
|
Q3AC00 | MVKRKHLLGLQELSKEEINTILDIARPMRDIIMRDIKKVPTLRGKTVATLFYEPSTRTRSSFELAAKFLSADTLSINVSSSSVQKGESLIDTIRTLEAMGVEIIAVRHQQSGVPKFISLNTKMSVINAGDGFHEHPTQALLDLFTIKQKLYKIEGLKVAIIGDIYHSRVARSNIWGLLKLGAEVTVCGPPSLIPVEIEKLGVRVEINLQRTLEWADVVNVLRIQKERQDAGYLTTLDEYRDWYGLTQEKLEKLKGKKLLILHPGPLNRGVEIDDYVADSPNAVVNEQVTNGVAVRMAVLYLLAGGNESGNVD | Catalytic Activity: carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-aspartate + phosphate
Sequence Mass (Da): 34737
Sequence Length: 312
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3.
EC: 2.1.3.2
|
B3PKF2 | MNFTGAHILSIQQFQREDINRIFDVADAMEPYALRRRVTRVLEGAILGNMFFEPSTRTRVSFGAAFNLLGGNVRETTGFESSSLTKGESLFDTARVLSGYSDVICMRHPAAGSVAEFAEGSRVPVINGGDGPNEHPTQALLDLYTIRKELRSKGRGIDDLRIAMIGDLKHGRTVHSLCKLLGLFNNVSITLVSPKELAMPDYIVEDLRQAGHKVTITDDLPTSITHIDIAYSTRIQEERFASKEEADSYRGRFRLNQAIYTQFCEPNTVIMHPLPRDSRAEANELDNDLNTNPNLAIFRQADNGVLVRMALFALVLDVAD... | Catalytic Activity: carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-aspartate + phosphate
Sequence Mass (Da): 37809
Sequence Length: 338
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3.
EC: 2.1.3.2
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Q043A9 | MEKLNLVSLPHFVSVENLSAEEVEALINRAEYFKNGGATPRLTQPVYISNMFFEDSSRTHTSFEMAERKLGLTVIPFDPAHSSVNKGETLYDTSLIMDAVGVNIEVIRHSQNEYYQDLIHPKKHQHLNIGVINAGDGSGQHPSQCLLDMMTIHEHFGHFKGLKVAIVGDITNSRVAKSNMELLTRLGAEVYFSGPEYWYSSEYDKYGKYEKLDKLIPEMDVMMLLRVQHERHSDDPNEKNFDAQAYHEEYGINHKRYQELKPDTIIMHPGPINHDVELSGDLVESDKCMFTRQMQNGVFMRMAMIEAVLRGRKLGGLN | Catalytic Activity: carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-aspartate + phosphate
Sequence Mass (Da): 36319
Sequence Length: 318
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3.
EC: 2.1.3.2
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