ids
stringlengths 6
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stringlengths 11
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stringlengths 108
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Q9I513 | MSSKQPSLSYKDAGVDIDAGEALVERIKGVAKRTARPEVMGGLGGFGALCEIPAGYKQPVLVSGTDGVGTKLRLALNLNKHDSIGQDLVAMCVNDLVVCGAEPLFFLDYYATGKLNVDVAATVVTGIGAGCELAGCSLVGGETAEMPGMYEGEDYDLAGFCVGVVEKAEIIDGSRVQAGDALIALPSSGPHSNGYSLIRKIIEVSGADIAQVQLDGKPLADLLMAPTRIYVKPLLQLIKQTGAVKAMAHITGGGLLDNIPRVLPDNAQAVIDVASWNRPAVFDWLQEQGNVDETEMHRVLNCGVGMVICVAQSDAEKALEVLRAAGEQPWQIGRIETCGADAERVVLNNLKNH | 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): 37123
Sequence Length: 353
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 2/2.
Subcellular Location: Cytoplasm
EC: 6.3.3.1
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Q89W81 | MTTMLSSDLPLPKIGRGKVRDIYAVDDDRLLLLTTDRISAFDVVMGETIPMKGAVLTQISAFWFGELEGVVPHHMISADTDEIIAAVPALKPHRAEILGRAMLSRRTTVFPIECVIRGYLSGSAWKEYATSGTLAGEKLKAGLVESEKLEPAIFSPATKAETGHDENITIARMREVVGDETAYTLESMTRAIYTLGEELAREQGIIIADTKFEFGRDKDGRIILIDEVMTPDSSRFWAVDAYKPGQPQASFDKQPLRDYLDVERRAGRWNGDAPPPPLPASVVEATSKRYLEAYRRVTGKELKI | 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): 33701
Sequence Length: 304
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate: step 1/2.
EC: 6.3.2.6
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Q98I23 | MRTLSDAFIPELPGYYKGKVRENYDLADGRRIIIATDRLSAFDIILTSIPFKGEILTQTARYWFEETADICPNHVLEYPDPNVVVGTRLDILPVEIVVRGYLAGTTSTSILTRYRRGEREMYGMRLPDGLRDNEKLAAPVITPTSKAADGGHDEPLSRAEILAQGLLTQAQWDTVSDYALKLFARGQARAAERGLILADTKYEFGTDKNGTIILADEIHTPDSSRYWIAASYEQALASGTRPDSFDKDFIRSWVAARCDPYKDPIPRIPDEIVEQASRIYAQAYEAITGKAFVPDLSGDTVLDRIRSNLVRFF | 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): 35091
Sequence Length: 313
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate: step 1/2.
EC: 6.3.2.6
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Q9HNU7 | MASVKDRRVESPATDTDLGRGVFEFSDRYSVFDWGEMPDHVPGKGASLCTMGAYTFEQLAAAGVPTHYQGVRTPDGETVRLADAPEAPTQMVIDLTQVPTLPFEDGSYDYDRYHDAGGSNYLVPLEVVFRNAVPVGSSLRTRCAPADVGIDADEWPQGPVELPETIVEFSTKYEEQDRYLSRSMADEIAGDADIAELDALARRVNETITDCAADAGFVHDDGKLECVYVDGEVRVADVAGTFDENRFRFDGREVSKEAVRQFYKRSDPEWVGAVKDAKRAADERGVADWKSLCEPSPDPLPPEILQAAADLYAAGANRYTAREWFDAPPLGDALDAFE | 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): 37124
Sequence Length: 338
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate: step 1/2.
EC: 6.3.2.6
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O68830 | MEKEKLLYEGKAKKLYFTDDSEVLWVEYCDQATALNGARKEQITGKGALNNQITSLIFEKLNAEGLETHFIEKLSKTEQLNRKVSIIPLEVVLRNVVAGSFAKRFGLEEGIVLQEPIVEFYYKDDALDDPFINDEHVRFLNIATYSEIEFLKSETRKINEILKKIWAEIGLTLVDFKLEFGRLADGRIILADEISPDTSRLWDANGQHMDKDVFRRNIGDLVETYTEVLNLLENAK | 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): 27136
Sequence Length: 236
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate: step 1/2.
EC: 6.3.2.6
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Q88U22 | MTAAIEKQALLYTGKAKAMYATNDPEILWVEYLDQATALNGKRKVPIDQKGRLNNRIASLIFKDLANHGIANHFIEQPSDYVQLVRRVTMIPLETVVRNAASGSFERKFAVPHLTKFAEPVLEFFYKSDQLDDPFINDSQIHALNVATPAIVAEIKRQALQVNQRLTAIFAAMGVQLVDFKIEFGLTTTGKVLLADEISPDSCRLVDLKTGASLDKDVFRKDLGDLTSVYQEVLTRLATVEEA | 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): 27081
Sequence Length: 243
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate: step 1/2.
EC: 6.3.2.6
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P12048 | MTIKRALISVSDKTNLVPFVKELTELGVEVISTGGTKKLLQENGVDVIGISEVTGFPEIMDGRLKTLHPNIHGGLLAVRGNEEHMAQINEHGIQPIDLVVVNLYPFKETISKEDVTYEEAIENIDIGGPGMLRAASKNHQDVTVIVDPADYSPVLNQIKEEGSVSLQKKRELAAKVFRHTAAYDALIADYLTNVVGEKEPEQFTVTFEKKQSLRYGENPHQEATFYQTALPVKGSIAQAEQLHGKELSYNNIKDADAAVQIVREFTEPAAVAVKHMNPCGVGTGKTIAEAFDRAFEADKTSIFGGIIALNREVDKATAEALHNIFLEIIIAPSFSQEALDVLTAKKNLRLLTLDVSAAVQKEKQLTSVQGGLLIQDLDMHGFDDAEISIPTKREPNEQEWEDLKLAWKVVKHVKSNAIVLAKDNMTVGVGAGQMNRVGSAKIAIEQAGEKAKGSALGSDAYFPMPDTVEEAAKAGVTAIIQPGGSIRDEDSIKKADEYGIAMVFTGIRHFKH | 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): 55753
Sequence Length: 512
Domain: The IMP cyclohydrolase activity resides in the N-terminal region.
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route): step 1/1.
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Q8A155 | MSESKRIKTALVSVYHKEGLDEIITKLYEEGVEFLSTGGTRQFIESLGYPCKAVEDLTTYPSILGGRVKTLHPKIFGGILCRRDLEQDIQQIEKYEIPEIDLVIVDLYPFEATVASGASEADIIEKIDIGGISLIRAAAKNYNDVIIVASQAQYKPLLDMLMEHGATSSLEERRWMAKEAFAVSSHYDSAIFNYFDAGEGSAFRCSVNNQKQLRYGENPHQKGYFYGNLDAMFDQIHGKEISYNNLLDINAAVDLIDEYEDLTFAILKHNNACGLASRPTVLEAWTDALAGDPVSAFGGVLITNGVIDKAAAEEINKIFFEVIIAPDYDVDALEILGQKKNRIILVRKEAKLPKKQFRALLNGVLVQDKDMNIETVADLRTVTDKAPTPEEVEDLLFANKIVKNSKSNAIVLAKGKQLLASGVGQTSRVDALKQAIEKAKSFGFDLNGAVMASDAFFPFPDCVEIADKEGITAVIQPGGSVKDDLTFAYCNEHGMAMVTTGIRHFKH | 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): 55880
Sequence Length: 507
Domain: The IMP cyclohydrolase activity resides in the N-terminal region.
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route): step 1/1.
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Q6G5S5 | MGVVAKNFPIPDLHRVRRVLLSVSDKTGIVAFAQALQTYNVELISTGGTAKVLMAAGLPVRDVAEVTGFPEIMDGRVKTLHPLIHGALLGVREDPSHAVAMEQYGIHGIDLLVVNLYPFEETVQSGADGQTILENIDIGGPAMIRAAAKNHVYTGVITAVSDYDAVLSELKQHDGCLSFSMRQQLAMRAYAHTAAYDTAIAAWFAKNLKIETPSWQSFSGHLKNVMRYGENPHQKAAFYRNGDKRFGVATAKLLQGKALSYNNMNDTDAAFELVAEFDPQNTAAVALIKHANPCGVAEGQTLKEAYLKALLCDNVSAFGGIIALNQPLDAECAEEVIKIFTEVIIAPDATMEAREIISGKKNLRLLLTGGVPDPRCGGFIAKTLAGGILVQSRDNVVVDDLKLQVVTKRAPSQEEMRDLQFAFRVVKHVKSNAIVYAKNSATVGIGAGQMSRVDSAKIAARKAEESAKRAGLTESLTKGSVVASDAFFPFADGLLAVAEAGATAVIQPGGSMRDEEVIAAADAQGLAMVFTGVRHFRH | 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): 57597
Sequence Length: 538
Domain: The IMP cyclohydrolase activity resides in the N-terminal region.
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route): step 1/1.
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Q1LU51 | MQRPIIIRRALLSVSDKTNICELAKSLLKRGVQLISTNGTARLLVNAGIHVTEVSNYTGFPEIMDGRVKTLHPKIHGGILARRNIDDTIMQQYKIEHIDMVVVNLYPFAEVVASATCNHEKVVENIDIGGTALLRSAAKNYSNVVVVVSINDYISIINEIDCNNGAVSLETRLNLAIKAFQHTATYDSQIKDYFTSQVYTDSSKCSSIFPPILNINFVKKQDMRYGENQHQLAAFYLDTRNKEKSIATTKQLQGRALSYNNIADADAALECVKEFSEPACVIVKHINPCSVAMGKTILVAYQRAYETDPTSAFGGVIAFNRSLDLCTAQEIIARQFIEVIIAPTVDQEALLILAKKKNIRVLSSGQWNKPIPNLNFRQVNGGLLVQERDLVMINLHDLRIVSQRQPTTMEIQDALFCWKVVKFVKSNAIVYARNQRTIGIGAGQMSRIDSAKIASIKAIDNKLNIRGSTMASDAFFPFRDGLDSAAKVGVSCVIQPGGSIRDQEVITAANEHNIAMIFTNIRHFRH | 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): 58384
Sequence Length: 526
Domain: The IMP cyclohydrolase activity resides in the N-terminal region.
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route): step 1/1.
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Q8G6B1 | MTNTNRPIRRALVSVFHKEGIEVLAEAFVKAGTEVVSTGSTAKKLAELGVKVTEVSDVTGFPECLDGRVKTLHPYIHAGILADMTNPEHAKQLEEFGIKPFDLVVVNLYPFADTVRSGANEADTIEKIDIGGPSMVRGAAKNHATVAIVTDPADYALVASRVADGTGFSLDERKWLAAKAFAHTAAYDATINEWTAKHWPKPASLDAVEVDKDDQGTEVDPAKFPAQFTRTWDRAHTLRYGENSHQQAALYIDPLNQTGFAHAEQLGGKPMSYNNYVDADAAWRTVWDMAPAIAVAVVKHNNPCGLAIGATAAEAHKKAHACDPMSAYGGVIACNSKVTLEMAESVRPIFTEVIVAPDYEPAALELLQTKKKNLRILEVAEPPKGHEAIRQIDGGLLVQDTDLINAVGDDPDAWKLVAGEAADADTLKDLVFAWRAIRCVKSNAILLAHDQATVGIGMGQVNRVDSCHLAVERANTLADGADRATGAVAASDAFFPFADGAQVLIDAGVKAIVQPGGSIRDEEVIEAAKKAGVTMYLTGTRHFFH | 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): 58413
Sequence Length: 545
Domain: The IMP cyclohydrolase activity resides in the N-terminal region.
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route): step 1/1.
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Q0VCK0 | MAPGQLALFSVSDKNGLVEFARNLASVGLNLIASGGTAKALRDAGLAVRDVSELTGFPEMLGGRVKTLHPAVHAGILARDIPEDSADMAKLDFNLIRVVVCNLYPFGKTVASPGVTVEEAVEHIDIGGVTLLRAAAKNHARVTVVCEPEDYAAVASEMQDSDSKDTSLETRRQLALKAFTHTAQYDEAISDYFRKEYSKGVSQMPLRYGMNPHQTPAQLYTLKPKLPITVLNGAPGFINLCDALNAWQLVKELKEALGLPAAASFKHVSPAGAAVGIPLSEDEANVCMVYDLYKTLTPVATAYARARGADRMSSFGDFVALSDVCDVPTAKIISREVSDGIIAPGYENEALKILSKKKNGNYCVLQMDQSYIPDENEVRTLFGLRLSQKRNNSVVNRSLFSNIVTKNKDLPESALRDLIVATIAVKYTQSNSVCYAKNGQVIGIGAGQQSRIHCTRLAGDKANCWWLRHHPQVLSMKFKTGVKRAEISNAIDQYVTGTIGEGEDLIKWKALFEEVPELLTETEKKEWIDKLNEVSISSDAFFPFRDNVDRAKRSGVAYIAAPSGSAADKVVIEACDELGIILAHTNLRLFHH | 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 and 10-formyltetrahydrofolate as the formyl donor in this reaction. Also catalyzes the cyclization of FAICAR to IMP. Promotes insulin receptor/INSR autophosphorylation and is involved in INSR internalization.
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): 64483
Sequence Length: 592
Domain: The IMP cyclohydrolase activity resides in the N-terminal region.
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route): step 1/1.
Subcellular Location: Cytoplasm
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Q89WU7 | MTDHPRRVTRALLSVSDKTGLIEFAKALAAHDVELVSTGGTAKAIAAAGLKVKDVSELTGFPEMMDGRVKTLHPKVHGGLLAIRDNKDHADAMKAHGIAPIDLLVVNLYPFEATVDKGAGFEDCIENIDIGGPAMIRAAAKNHDDVAVVVEAEDYKAVLDELAANKGATTLKLRRRLAAKAYARTAAYDAAISNWFNRQLEIDAPDFRAFGGKLIQSLRYGENPHQTAAFYATPDKRPGVSTARQLQGKELSYNNINDTDAAYECIGEFDAKRTAACVIVKHANPCGVAEGSDLVSAYRKALACDSTSAFGGIIAMNRALDADTAREITKIFTEVIIAPDASEEAIAIIGARKNLRLLLAGSLPDPRAPGLTAKTVAGGLLVQSRDNAVVDDMTFKVVTKRAPTDAEMRDLKFAFRVAKHVKSNTIIYAKDLATVGIGAGQMSRVDSARIAARKAQDAAVELKLAEPLTKGSVVASDAFFPFADGMLACIEAGATAVVQPGGSMRDDEVIKAADEHGIAMVFTGTRHFRH | 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): 56465
Sequence Length: 530
Domain: The IMP cyclohydrolase activity resides in the N-terminal region.
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route): step 1/1.
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A6WXV3 | MAVSSKHIPAPDLHRVRRALLSVSDKTGLIDFAKALHAQGVEILSTGGTAKSIAAEGIPVKDVSEVTGFPEIMDGRVKTLHPAVHGGLLAVRNDREHVAAMEEHGIGGIDLAVINLYPFEEVRFKGGDYDTTVENIDIGGPAMIRASAKNHAYVATVVDPADYADVVAELEKHAGSLPLAFRKKLAAKAFSRTAAYDAAISNWFAEAINEETPVYRSVAGKLHSVMRYGENPHQTAGFYLTGEKRPGVATATQLQGKQLSYNNINDTDAAFELVAEFDPARTAAVAIIKHANPCGVAEAATIKEAYLKALACDPVSAFGGIVALNKTLDEEAAEEIVKIFTEVIIAPDATEGAQAIVAAKKNLRLLVTGGLPDPRAKGIAAKTVAGGLLVQSRDNGVVDDLDLKVVTKRAPTEAELNDMKFAFRVGKHVKSNAIVYVKDGATVGIGAGQMSRVDSARIAARKAEDAAEAAGLAEPLTKGCVVASDAFFPFADGLLSAVQAGATAVIQPGGSMRDDEVIAAADEHGIAMVMTGMRHFRH | 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): 56639
Sequence Length: 538
Domain: The IMP cyclohydrolase activity resides in the N-terminal region.
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route): step 1/1.
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Q1H4G7 | MAVIKRALISVSDKTGILEFAKALAEFGVEILSTGGTAKLFRDNGIPVTEVSDYTGFPEMLDGRVKTLHPKIHGGLLGRRDLPEHVTAMQAAGIPDIDMIVVNLYPFEATVARPDATLEDAIENIDIGGPAMVRSAAKNWQDVAVLTDASQYEEVLAEMRSTGGATSKATRFALSVAAFNRISNYDGAISDYLSSFNADGTRNEFPGQINGRLVKVQDLRYGENPHQQAAFYRDLYPAPGSLVTAQQLQGKELSYNNIADADAAWECVKSFDSTACVIVKHANPCGVALGATPLEAYQKAFQTDPTSAFGGIIAFNHTLDGAAAEAVSKQFVEVLIAPDYTEEALAVFKAKANVRVLKIALPVGGDSPWSRGRNSHDTKRVGSGVLIQTADNHEISAADIKVVTKKQPTPEQLEDLLFAWRVAKYVKSNAIVFCGNGMTLGVGAGQMSRVDSTRIAAIKAQNAGLSLQGSAVASDAFFPFRDGVDVLAEAGASCVIQPGGSIRDDEVIAAADEHGLVMIFTNIRHFRH | 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): 56430
Sequence Length: 528
Domain: The IMP cyclohydrolase activity resides in the N-terminal region.
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route): step 1/1.
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Q8D244 | MEQSFLPIRCALISVSDKTGIFSLAKNLIKHKVKLITTSGTYKYLLEKGIFSTSVSEYINHPEIINGRVKTLHPKIHGGILSNNKNINENKNLNIKKIDMVITNFYPFKKKVKKENIKIENIIDNIDIGGVALARSAAKNYKYVTVVVNINQYSKLSSEMDKNSGSVSFKTRFYFSTLAFQYSYSYDKEIFNYFNKIYFKEIELKKNLKNKKFPELFSISFSKKEDVLYGENYHQKAAFYTDPVIHPGTVPFSIQRQGKKLSYNNIVDSDIAINCVMNFSEIACVIVKHSTPCGVSSGKNIIDAYRSAYYSDPDSAFGGIISFNRPLTIEAAEFIINKQFVEIIIAPVIEKDALLTLKSKSKIIVLECGYLSKNFLLNFKKVNCGLLLQDSDNKILKEKDIKIVSKRQPSKLEIESSIFIWKIIKFIKSNAIIYGKNKRTLGIGSGQTSRIFSTRIAAYKAIDQGFSLKGSVMASDAFFPFRDSIDFASKFGVSCIIQPGGSINDDKIISAVDENNMSMIFTNTRQFSH | 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): 59775
Sequence Length: 529
Domain: The IMP cyclohydrolase activity resides in the N-terminal region.
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route): step 1/1.
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Q9PC10 | MASDFLPVHRALLSVSDKTGLVELARALLAYNIELLSTGGTATIIREAGLPVQDVADLTGFPEMMDGRVKTLHPMVHGGLLGRAGIDDAVMAKHGIAPIDLLILNLYPFEQITAKKDCTLADAVDTIDIGGPAMLRSAAKNFARVAVATSPDQYPDLLAELQAHHGQLSAEKRFALAVAAFNHVAQYDAAISNYLSSVSDMHTTLPLRHEFPAQLNNTFVKMTELRYGENPHQTGAFYRDVHPQPGTLATFQQLQGKTLSYNNLVDADAAWECVRQFEAPACVIVKHANPCGVAVGKACSDAYEEAYATDPTSAFGGIIAVNRMLDVATMQSILDRQFVEVLIAPDYDADALAYATKKANVRVLRIPSTGVMNRYDFKRIGSGLLVQSTDSLNIHSDALKVVTQLAPTDAQQRDLLFAWHVAKYVKSNAIVYAKDNRTIGIGAGQMSRVYSARIAGIKAADAHLAVTGSVMASDAFFPFRDSIDAAAAAGIKAVIQPGGSMRDNEVIAAADEHGIAMVFTGIRHFRH | 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): 56715
Sequence Length: 527
Domain: The IMP cyclohydrolase activity resides in the N-terminal region.
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route): step 1/1.
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P91134 | MGSVTSKTNDELESFLNKRLGGSMTSSNKTVSVLLGAQWGDEGKGKIIDYLIENHKINVTARCQGGNNAGHTVVANGRKYDFHILPSGIISPTCFNVIGNGVVVNLDAFFSELAHNGILEESGWEKRIMISSEAHLVFGVHSQVDGRQEDSLAAKNKIGTTNRGIGPTYSSKCFRNGIRVADLMADFEEFSEKYRRLVEHYKKQFPSIEVNVDEELAKFKQHREKLAELKLVGDTVGFIHEQRNAGKQVLVEGANGALLDIDFGTYPYVTSSNSTVGGACTGIGVPPTAVGNVIGVVKAYQTRVGTGPFPTELFDSDGEKLQTIGKEVGVTTGRKRRCGWIDLFLLRRSAMINGYTAIALTKLDILDTFPTIKVAVGYKLNGQVLSSPPAQANAWGAIEVEYKEFEGWNEPTVGVRKFEDLPEKCRQYVKFIEDFIKVPIVYIGVGAERESLIVRQQ | 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.
Catalytic Activity: GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate
Sequence Mass (Da): 50161
Sequence Length: 457
Pathway: Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2.
Subcellular Location: Cytoplasm
EC: 6.3.4.4
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Q1IJT2 | MVSKGKTAVVIGAQWGDEGKGKIVDVLSENFRVVARYAGGHNAGHTVLIGGKKFVLQLIPCGVLRPGCRGVIGNGVVLDPIAFLNEVQRLRDLGVAVDGNLFVSSRAHVILPYHRMVELASENAPGRVKIGTTSRGIGPSYEDKMGRRGLRVADLLDSTLLKKHIENACKEKNTIVHALFNAEPIDPDKMYNEYAKAAEKVAPFVTDTAVLLNNAINSGESVMFEGAQGTMLDIDHGTYPFVTSSSATSGGAVIGTGVPPTSISTVIGVTKAYCTRVGEGPFPSELHDAMGDAIRKKGNEFGAVTGRPRRTGWLDLPLLRYSNMINGTEWLVVTKLDVLDELDEIPVATSYKIDGKESEEIPAQGCGFDKIEPIYTKLPGWKTDTTKISKYEDLPAKTKEYLKFVEQQSGAKVGILSTGPDRDQSIYTDAFVNALGLKHLGK | 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 Mass (Da): 47644
Sequence Length: 442
Pathway: Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2.
Subcellular Location: Cytoplasm
EC: 6.3.4.4
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Q71YP9 | MPNMEPTTKEIKEQKIYQEMGLTDSEYELVCSILGREPNYTETGLFSVMWSEHCSYKNSKPVLRKFPTEGKQVLQGPGEGAGIVDIGDGLGVAFKVESHNHPSYVEPYQGAATGVGGIIRDVFSMGARPIAMLNSLRFGELDTPHAKYLVSEVVAGIAGYGNSIGIPTVGGEIQFDPCYTKNPLVNAMCVGLIEAKDIQKGQAKGIGNPVMYVGAKTGRDGIHGATFASVEFSEEGEQQRSAVQVGDPFMEKLLLEACLDVIRDHSDILVGIQDMGAAGLVSSSSEMASKAGAGLELIMDDVPQRELNMTPYEMLLSESQERMLLCVKKGHVEEIQALFERYGLEAVVIGQVTDDKMYKIIHHGEVVANVPVDALAEDAPVYHKPSKEPARYQAFQEEESFVPVMEDVVGVWKELLAQPTIASKRHIYEQYDYQVRTDTAVVPGSDAAIVRVRGTEKAIAMTTDCNSRYLYLDPKVGGAIAVAEAARNIVCSGGKPLAITDGLNFGNPEKPEIFWEIEKAADGISAACLELDTPVISGNVSLYNETDGTGIYPTPVIGMVGLVEDLAHITTQDFKNSGDVIFLIGETKAEYSGSELQKLQQGKISGRAPELDLTTEKKYQQLLLTAIQEGLVASSHDLAEGGFGVALAEATFKAGLGADVEVPFELNQLFSESQSRFLVSVKPENEAAFAQLMELEKVYRLGVVTEDDTIRVKHKEDQVTAKTTELRSIWQGAIPCLLK | 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 of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL.
Catalytic Activity: ATP + H2O + L-glutamine + N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide = 2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ADP + H(+) + L-glutamate + phosphate
Sequence Mass (Da): 80218
Sequence Length: 739
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 1/2.
Subcellular Location: Cytoplasm
EC: 6.3.5.3
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Q58660 | MDENDLKYIEKVLGRKPNHIELAMFENLWSEHCAYRTSKKLLRMFAKTVNEKTSKNIVVGIGDDAAVIRLKNDICLAIAMESHNHPSYIDPYNGAATGVGGIVRDVLSMGAKPIALLDPLRFGDIFGKEGDKVRWLIEGVVKGIGDYGNRIGVPTVGGECEFDSSFDYNNLVNVVCVGLVKENEIITGKAKEPGLSLILIGSTGRDGIGGASFASKDLTEESEEERPSVQVGDAFSEKCLIDAVLEAVKTGKVKAMKDLGAAGLSGASSEMCYGGGVGCELYLENVVLREPLTPYEIMVSESQERMLLAVEPGSEEEIIEIFKKYELPASVIGKTIPEKRIIAKYKGEVVVDLPLDLLCEAPLYDREGKEDLKEKEDDKEKIKMPEDLNAVLLKLLESPNICSKEWIYQQYDHEVQIRTVVKPGKDAAVLRINEVYPMGIALTTDCNSRYCKLNPYVGAVNAVAEAVRNLATVGAEPIAMLDNLNFGNPERPERFWQLAECIKGLADAAEFFEIPVVGGNVSLYNETVIEGKEHPINPTPAIFVLGKVEDVEKVPGVLDNKIKEGDILIITNETKDEMGGSEYYKVIHNTEEGRVPRVDLEKEKKIYEEVREVVKEGLVSEAVDCSRGGLAVALAKMAVLNNIGLEVDLTEYNKNNLRDDILLFSETSGRIILAVRDENKDKVLSKLSSAYIIGKVGGSRLKIKINEKDVVNLDVEEMKKRYYEAFPKMMGEL | 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 of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL.
Catalytic Activity: ATP + H2O + L-glutamine + N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide = 2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ADP + H(+) + L-glutamate + phosphate
Sequence Mass (Da): 80866
Sequence Length: 733
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 1/2.
Subcellular Location: Cytoplasm
EC: 6.3.5.3
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Q8TY09 | MTLDERDLELIREELGRDPNATERAMFENMWSEHCAYRSTRHLLRQLPSEADHVIVGPGDDAAVVAIDDEWAVVVGIESHNHPSYVDPYNGAATGVGGIVRDVLSMGAFPIALLDPLRFGPLDGERVPYLVDGVVRGISDYGNRIGVPTVGGELEFDPSYERNPLVNVMCVGIVRRSEIVRGRADRPGDVLVLVGARTGRDGIGGAAFASEELGEESEEEDRPAVQIGDPFTERQLIIAIREAVERGLVKGCKDLGAAGLTCAATEMAADGGTGVEIDVFKVPLREEGMEPWEIMLSESQERMLLVVAPEDVDEVIEICRKYGLEASVVGRVTDDGYLTVKDGDDVIARVPAEFLADGAPEVEWEEEPYSYPENVDVPEPDPEDLVRSVLSSPNVSPALREWVYRQYDHEVQGRTVVKPGHDAAVMWLQHEGLEDVALALTTDSNPRHVLIDPKTGTEGCVAEALRNLATVGAEPLCLVDCLNFGSPENPRVYYQLRRSIEGLGKAAREFEVPVVGGNVSLYNEHEVDGPVNPTPVIGAVGVIRGLDYLEDFPREPEEGEAVIVLGETREELGGSLYLIEYHGIKGGKVPRVRYREERALHDLLRRIARKNMVSSVTDVSTGGLLAAVAELLGPVGASLSLSEVPNSVSRWDFLLLSESHGRAIVTTDRPDDVLGAAEEAGVPAQVVGEVTGDGVLRISVGPVDVSLDREELEELWRSPLHYLE | 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 of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL.
Catalytic Activity: ATP + H2O + L-glutamine + N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide = 2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ADP + H(+) + L-glutamate + phosphate
Sequence Mass (Da): 78777
Sequence Length: 724
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 1/2.
Subcellular Location: Cytoplasm
EC: 6.3.5.3
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Q8PYK1 | MLPEEDLKIIKKELGREPTLVEQGCFLNLWSEHCSYRSSAPLLKTFTTTGENVIIGPGDDAAIIKFEDGYVLAIGMESHNHPSYVDPYNGAATGVGGIVRDIISMGARPIALMDPLYFGPLDTPKNLFLFEQIIKGIAGYGNCIGVPVVNGETFFDRRYSGNPLVNVVAVGLCKEEKVMTSRSQKAGNKLILAGSSTGKDGLGGASFASRDLSESAEAEDRPSVQVGDPYTEKLVMEMTLEAIDKGYIKSCKDLGAAGLGGASSELAAKGGLGAYIIADAVPQREPEMNAYEILLAESQERMVFEVAPEDVDAVLALVQKYDLNGAVIGHLTEKPNYTVEFRGEIVADIPIGFLTGGAPTCEKPSEAPIHREEGKKPETPEDLKAAFMKVLSSHNIASKEWIYRQYDHEVQLRTVVKPGEDSGVLRITDKKGIALSCGCQPRATLLDPYTGGRTAIIENAMNLAVKGAEGLAIVNCLNFGNPENPETYWQFKNAVLGLGDAARELSIPVVGGNVSLYNESDEFRTAIPPTPSIGMIGKVDLETPLPSGFFAKTGDSIILVGETVPEMGGSEYYSCMGAGNAGKVPEVPKNAPEIIKAVIEAVKSGKLNSAHDISLGGIGAGLARMCKNMGGKVDVSEIAGGMKEDEFLFSEAPARALLATAEPEAVQELLKGVPHAVIGTVGGDALEIKGKDFELFISLEEIKNAHESLTKFMMMG | 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 of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL.
Catalytic Activity: ATP + H2O + L-glutamine + N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide = 2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ADP + H(+) + L-glutamate + phosphate
Sequence Mass (Da): 76311
Sequence Length: 716
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 1/2.
Subcellular Location: Cytoplasm
EC: 6.3.5.3
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Q8CSX5 | MKERFIKKTHYLDYQFDEPTDIKLGFTTRENGLSPYPNHSFNMARYISDSAHHITHHQDILANLIGYPRDEWVFPIQTHDSRIVEVTSEHKGTNIDELTDDLHGIDGMYTFDSHILLTMCYADCVPVYFYSEPHGYIGLAHAGWRGTYGQIVKEMLKKVDFDYEDLKIVIGPATSNSYEINDDIKNKFEELTIDSTLYIETRGKNQHGIDLKKANALLLEEAGVPSKNIYVTEYATSENLDLFFSYRVEKGQTGRMLAFIGRK | Function: Purine nucleoside enzyme that catalyzes the phosphorolysis of adenosine and inosine nucleosides, yielding D-ribose 1-phosphate and the respective free bases, adenine and hypoxanthine. Also catalyzes the phosphorolysis of S-methyl-5'-thioadenosine into adenine and S-methyl-5-thio-alpha-D-ribose 1-phosphate. Also has adenosine deaminase activity.
Catalytic Activity: adenosine + phosphate = adenine + alpha-D-ribose 1-phosphate
Sequence Mass (Da): 30306
Sequence Length: 263
EC: 2.4.2.1
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P45497 | MIGQRDTVNGAHFGFTDRWGGVSAVPYEELNLGGAVGDDPGAVTANRELAAKSLGVDPARVVWMNQVHGADVAVVDAPWGDRPVPRVDAVVTAERGLALAVLTADCVPVLLADPVSGVAAAAHAGRPGLVAGVVPAAVRAMAELGADPARIVARTGPAVCGRCYEVPEEMRAEVAAVEPAAYAETGWGTPALDVSAGVHAQLERLGVHDRAQSPVCTRESADHFSYRRDRTTGRLAGYVWLD | Function: Purine nucleoside enzyme that catalyzes the phosphorolysis of adenosine and inosine nucleosides, yielding D-ribose 1-phosphate and the respective free bases, adenine and hypoxanthine. Also catalyzes the phosphorolysis of S-methyl-5'-thioadenosine into adenine and S-methyl-5-thio-alpha-D-ribose 1-phosphate. Also has adenosine deaminase activity.
Catalytic Activity: adenosine + phosphate = adenine + alpha-D-ribose 1-phosphate
Sequence Mass (Da): 25144
Sequence Length: 242
EC: 2.4.2.1
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P45496 | MIVQHRTAPVTGSAHFAFTDRWGGVSAAPYGELNLGGAVGDDPAAVGANRERAARHLGLDPAHVVWMNQVHGRDVAVVDGPWGADAEIPAVDAVVTARRGLALAVLTADCTPVLLADPVAGVVGAAHAGRPGLVAGVVSAAVEAMVALGAHPSRITAHTGPAVCGRCYEVPEEMRAEVAGAVPGTWSETSWGTPAVDVTGGVHAQLAALGVTDRHASPFCTLESGDHFSYRRDRTTGRLAGYVWLD | Function: Purine nucleoside enzyme that catalyzes the phosphorolysis of adenosine and inosine nucleosides, yielding D-ribose 1-phosphate and the respective free bases, adenine and hypoxanthine. Also catalyzes the phosphorolysis of S-methyl-5'-thioadenosine into adenine and S-methyl-5-thio-alpha-D-ribose 1-phosphate. Also has adenosine deaminase activity.
Catalytic Activity: adenosine + phosphate = adenine + alpha-D-ribose 1-phosphate
Sequence Mass (Da): 25269
Sequence Length: 246
EC: 2.4.2.1
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P74606 | MTMGDDLWGWQNINGSPYLTCALLAPWPHAFFTRAFYPQLPEQLITYLDPQGKAFRVKQVHGDVTLTATEIGQTPLAPDSTHPPADGIISDAPHQGVWVASADCTPVLIGDLIGKRVAAIHAGWRGTKARIVPKTIDKFLALGSELKDLRVALGPAIAGEVYQVDPWVALEVGQSVQAVQKLATEEQQWDHLSTMVNPPVLPDAEPEKYRLDVRRINQLQLLELGFAQEQIAVAPHCTFQMEELFFSYRRTHTKEVQWSGIVSY | Function: Purine nucleoside enzyme that catalyzes the phosphorolysis of adenosine and inosine nucleosides, yielding D-ribose 1-phosphate and the respective free bases, adenine and hypoxanthine. Also catalyzes the phosphorolysis of S-methyl-5'-thioadenosine into adenine and S-methyl-5-thio-alpha-D-ribose 1-phosphate. Also has adenosine deaminase activity.
Catalytic Activity: adenosine + phosphate = adenine + alpha-D-ribose 1-phosphate
Sequence Mass (Da): 29346
Sequence Length: 264
EC: 2.4.2.1
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Q1EIR0 | MIELEKLDFAKSVEGVEAFSTTRGQVDGRNAYSGVNLCDYVGDDALRVLDARLTLAMQLGVDLDDLVMPRQTHSCRVAVIDERFRALDIDEQEAALEGVDALVTRLQGIVIGVNTADCVPIVLVDSQAGIVAVSHAGWRGTVGRIAKAVVEEMCRQGATVDRIQAAMGPSICQDCFEVGDEVVEAFKKAHFNLNDIVVRNPATGKAHIDLRAANRAVLVAAGVPAANIVESQHCSRCEHTSFFSARRLGINSGRTFTGIYRK | Cofactor: Binds 4 Cu cations per subunit.
Function: Purine nucleoside enzyme that catalyzes the phosphorolysis of adenosine and inosine nucleosides, yielding D-ribose 1-phosphate and the respective free bases, adenine and hypoxanthine (By similarity). Also catalyzes the phosphorolysis of S-methyl-5'-thioadenosine into adenine and S-methyl-5-thio-alpha-D-ribose 1-phosphate (By similarity). Also has adenosine deaminase activity (By similarity). Also acts as a multicopper oxidase able to oxidize a wide variety of polyphenols and related compounds in vitro . Displays substrate preference as follows: syringaldazine > 2,6-dimethoxyphenol > veratryl alcohol > guaiacol > tetramethylbenzidine > 4-methoxybenzyl alcohol > 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) (ABTS) >> phenol red > 1-hydroxybenzotriazole . Cannot use 3,4-dimetoxybenzyl alcohol and violuric acid as substrates . As this enzyme is derived from a rumen microbial community, it may have a role in the digestion of complex plant materials such as ryegrass lignin .
Catalytic Activity: adenosine + phosphate = adenine + alpha-D-ribose 1-phosphate
Sequence Mass (Da): 28282
Sequence Length: 262
EC: 3.5.4.4
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Q9PET8 | MGRFPSWVLVADWPAPPGVMVLSTLRGGPGVSVAPFDRLNLGNCSGVAGDAPVCVERNRSRLVEMLGLPSVPHWLRQVHGVEVLRVDALLQSIARVVEPTADAAVTSVVGAVLAILTADCLPVVLAAVDGSEIGVVHAGWRGLADDVLGRTVAALRTSPEYLQAWLGPAAGPQAYEVGVDVYAAFVERDSGAACAFSVTRPGHWYVDLYALARQRLMRAGLSAVSIYGGGLCTISDPQRFFSHRRDRRSGRFATLAWIGC | Function: Purine nucleoside enzyme that catalyzes the phosphorolysis of adenosine and inosine nucleosides, yielding D-ribose 1-phosphate and the respective free bases, adenine and hypoxanthine. Also catalyzes the phosphorolysis of S-methyl-5'-thioadenosine into adenine and S-methyl-5-thio-alpha-D-ribose 1-phosphate. Also has adenosine deaminase activity.
Catalytic Activity: adenosine + phosphate = adenine + alpha-D-ribose 1-phosphate
Sequence Mass (Da): 27613
Sequence Length: 260
EC: 2.4.2.1
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Q5UZ65 | MYVGRFVVVSPEVGAYRVSSRSFPNRQAVQRDGTVTVEPTPDAPETDNPYISYNGVRVTERGAVVGNGSHVDPIAEKLELGYPARDAIAEPLLSLDFEKDDYDTPRVAGIVGVDAADPTTNADGPGAVIGTVRRDALLVEEVTEPTLVATYEENSPTAFDLAATDASDVAREVYDHEYEHAVCSAGVAGSAGEFDVAVYNGE | Function: Catalyzes the cyclization of 5-formylamidoimidazole-4-carboxamide ribonucleotide to IMP.
Catalytic Activity: H2O + IMP = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Sequence Mass (Da): 21452
Sequence Length: 202
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; IMP from 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide: step 1/1.
EC: 3.5.4.10
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Q92PI1 | MKSAVVQLPGLNRDCDMIAALTKISGKAPVTVWQTETEIPDVDLIVIPGGFSYGDYLRCGAIAARMPVMQAIKAKAEQGVRVLGVCNGFQILVEAGLLPGALMRNASLKFVCREVKLEVVNADTAFTRAYAKGQVIRSPVAHHDGNYFADAETLKAIEGNGQVVFRYAEGTNPNGSVNDIAGVLNAKGNVLGMMPHPENLIESAHGGADGRGLFASALDVIAA | 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 of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL.
Catalytic Activity: ATP + H2O + L-glutamine + N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide = 2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ADP + H(+) + L-glutamate + phosphate
Sequence Mass (Da): 23492
Sequence Length: 223
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 1/2.
Subcellular Location: Cytoplasm
EC: 6.3.5.3
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Q5LS78 | MRAAVVVFPGSNCDRDLAVAFEQAGFDVSMVWHKDADLPQGIDIVGIPGGFSYGDYLRCGAIAAQSPICKAVVAHTARGGYALGVCNGFQVLTETGILPGALLRNAGLKYICKTVGLKVETSNSVFTEGYNAGDVIGIPIAHHDGNYYADDETLAALKAEDRIAFTYTDNPNGARDDIAGILSANRRVLGMMPHPERAADAGHGGTDGVALFRALAGALTPA | 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 of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL.
Catalytic Activity: ATP + H2O + L-glutamine + N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide = 2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ADP + H(+) + L-glutamate + phosphate
Sequence Mass (Da): 23153
Sequence Length: 222
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 1/2.
Subcellular Location: Cytoplasm
EC: 6.3.5.3
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Q9UX21 | MIAIIKFPGTTCETDVYKALIEAGVPTVIVKYKDFDPDRYNGVILPGGFSFGDYLRAGSIAASTETMKKVKQMAEDGKIVIGICNGFQILVESGLLKGALLPNLKLRFISKWVYLKVIRADTILTKGLDKKIIRMPIAHAEGRYYVDDIDYAKTHMVLQYCDENGNISEDVNPNGSLLNIASIANEEGNVIGMMPHPERASFKLTSIDGTVDGLILLRRLGEWA | 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 of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL.
Catalytic Activity: ATP + H2O + L-glutamine + N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide = 2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ADP + H(+) + L-glutamate + phosphate
Sequence Mass (Da): 24686
Sequence Length: 224
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 1/2.
Subcellular Location: Cytoplasm
EC: 6.3.5.3
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Q2N8K3 | MPHTAKILLLGSGELGREFVISAKRLGAYVVACDAYAAAPAMQVADASEVLSMLDADALRAVVAKHHPDYVVPEIEAIRTEVLAEIEADGFNVVPSAYATQMTMNRDAIRDLAAQELGITTSRYRYAKNLEEVRAAAEFTGYPCVIKPVMSSSGKGQSTVRSADKLEEAWDYAVANMRGDRKRVIVEQFIDFDYEITLLTVRHKDGITFCPPIGHRQERGDYRESWQPATMSKPAIAAAQEMAEKVVTALQGNGKGFGLFGVEFFVKGEEVIFSELSPRPHDTGMVTSVSQNLSEFDLHARAIMGLHVPSEILARPSASAVILAEQESETVSYSGLAAAMEGGADIRIFGKPNTRPYRRMGVALATGGDTDYARTAAVAAANKLHIHYGD | 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-ribosyl)glycinamide = ADP + H(+) + N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide + phosphate
Sequence Mass (Da): 42303
Sequence Length: 390
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5-phospho-D-ribosyl)glycinamide (formate route): step 1/1.
EC: 6.3.1.21
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Q9VSK9 | MGKDRGRGRRNNHSGPYNKSNWRGQKKDRPQNNGGGQRNSAPQQKSTLLETQVGITEFTNPEAPGFTGILKSRFSDFHVNEIDSNGKVLELNDLSVPKVAIVAVAENELDNWRKELEAVIGPEVWQDIANLAKAKNDPAIEQKVEIDVTTLDKEQRTQVHQMIKQLYKGKLLSTTIGQQQAKPKVQEEASLENKDAAEGETSTQKDSQVPAEEKKTIKVFKPKPGRGDKRWSFPADYVTFLVHKTNLVTSDVASTLAARLNLRPSQVNYSGIKDKRAKTTQKFSVKRRTPESILVAARSQRNVHIGNFGFESNTLKLGDLQGNRFRIALRHIAKEKREEIEQALQSLKERGFINYYGLQRFGNSASVPTYEVGVALLKHDYKLACELILKPRDSDVEFLRPIREEWWKNRDSAAAAAQIYGEKFIEKKLLDGLARFGESDYSSALRQIPRNMLMLYPHAYQSLIFNRIASRRIKEFGLKLIPGDLVYVEQDQSEASEEQAQQGEALEEQKEEEPNDEPLEVPEGDEAIEEESIFKRKVRPLTAEDIASGKYKLCDVVLPLPGHDITYPSNECGAWYEEMLAEVGLSSDQLKHKEKTYALAGAYRKMIISSSDLKWSFRMYNTPEDTLIASDWELLKNIPVAPEPAEAEANYMALLLEFSLPTAAYATMFLRELLKQDTSSASQTQLEKQAMAKEDNEKKAVGTQEEQMEVVKEVADEDGQETEQAETQGAEEAV | Function: Pseudouridylate synthase that catalyzes pseudouridylation of RNAs, such as tRNAs and mRNAs.
Catalytic Activity: a uridine in tRNA = a pseudouridine in tRNA
Sequence Mass (Da): 82800
Sequence Length: 734
EC: 5.4.99.-
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Q96PZ0 | MEMTEMTGVSLKRGALVVEDNDSGVPVEETKKQKLSECSLTKGQDGLQNDFLSISEDVPRPPDTVSTGKGGKNSEAQLEDEEEEEEDGLSEECEEEESESFADMMKHGLTEADVGITKFVSSHQGFSGILKERYSDFVVHEIGKDGRISHLNDLSIPVDEEDPSEDIFTVLTAEEKQRLEELQLFKNKETSVAIEVIEDTKEKRTIIHQAIKSLFPGLETKTEDREGKKYIVAYHAAGKKALANPRKHSWPKSRGSYCHFVLYKENKDTMDAINVLSKYLRVKPNIFSYMGTKDKRAITVQEIAVLKITAQRLAHLNKCLMNFKLGNFSYQKNPLKLGELQGNHFTVVLRNITGTDDQVQQAMNSLKEIGFINYYGMQRFGTTAVPTYQVGRAILQNSWTEVMDLILKPRSGAEKGYLVKCREEWAKTKDPTAALRKLPVKRCVEGQLLRGLSKYGMKNIVSAFGIIPRNNRLMYIHSYQSYVWNNMVSKRIEDYGLKPVPGDLVLKGATATYIEEDDVNNYSIHDVVMPLPGFDVIYPKHKIQEAYREMLTADNLDIDNMRHKIRDYSLSGAYRKIIIRPQNVSWEVVAYDDPKIPLFNTDVDNLEGKTPPVFASEGKYRALKMDFSLPPSTYATMAIREVLKMDTSIKNQTQLNTTWLR | Function: Pseudouridylate synthase that catalyzes pseudouridylation of RNAs . Acts as a regulator of protein synthesis in embryonic stem cells by mediating pseudouridylation of RNA fragments derived from tRNAs (tRFs): pseudouridylated tRFs inhibit translation by targeting the translation initiation complex . Also catalyzes pseudouridylation of mRNAs: mediates pseudouridylation of mRNAs with the consensus sequence 5'-UGUAG-3' . Acts as a regulator of pre-mRNA splicing by mediating pseudouridylation of pre-mRNAs at locations associated with alternatively spliced regions . Pseudouridylation of pre-mRNAs near splice sites directly regulates mRNA splicing and mRNA 3'-end processing . In addition to mRNAs and tRNAs, binds other types of RNAs, such as snRNAs, Y RNAs and vault RNAs, suggesting that it can catalyze pseudouridylation of many RNA types .
Catalytic Activity: a uridine in tRNA = a pseudouridine in tRNA
Sequence Mass (Da): 75035
Sequence Length: 661
Subcellular Location: Nucleus
EC: 5.4.99.-
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Q91VU7 | MEMTSTSLKRGCLVVEDNDSVTPHDETKKQKVSEGCLTSSQDGVENDGLHRSENEPGPPEAESTVKDDENSSAQVQEEEEEEEEEDGLSEAGEEEEAESFADMMKHGLTELDVGICKFVSSHHGFSGILKERYSDFVVHEIGKDGRISHLDDLSVPVDEEDPPEDALTVLTAEDRQQLEELQLFKNKETSVAIEVIEDTKEKRTVIHQAIKSLFPGLETKTEDREGRKYIVAYHAAGKKALANPRKHSWPKSRGSYCHFVLYKENKDTMDAINVLSKYLRVKPNIFSYMGTKDKRAITVQEIAVLKISAQRLAHLNKCLMNLKLGNFSYQKTPLKLGALQGNHFTVVLRNITGTDEQVQQAMQSLRETGFINYYGMQRFGTTAVPTYQVGRAILQNSWTEVMDLILKPRSGAEKGYLVKCREEWAKTKDPASALKKLPVKRCVEGQLLRGLSRYGMKNIVSAFGIIPRNNRLMYIHSYQSYVWNTMVSRRIEEYGLRPVPGDLVLKGATPTYIEEDDVDNYSIHDVVMPLPGFDVIYPKHKISEAYREMLAADNLDIDNMRHTIRDYSLSGAYRRIIIRPQSVSWEVVAYDDPKIPLFNTDVDNLEGKPPPVFASEGKYRALKMDFSLPPSTYATMAIREVLKMDTSIKNQTQLNTSWLR | Function: Pseudouridylate synthase that catalyzes pseudouridylation of RNAs. Acts as a regulator of protein synthesis in embryonic stem cells by mediating pseudouridylation of RNA fragments derived from tRNAs (tRFs): pseudouridylated tRFs inhibit translation by targeting the translation initiation complex. Also catalyzes pseudouridylation of mRNAs: mediates pseudouridylation of mRNAs with the consensus sequence 5'-UGUAG-3'. Acts as a regulator of pre-mRNA splicing by mediating pseudouridylation of pre-mRNAs at locations associated with alternatively spliced regions. Pseudouridylation of pre-mRNAs near splice sites directly regulates mRNA splicing and mRNA 3'-end processing. In addition to mRNAs and tRNAs, binds other types of RNAs, such as snRNAs, Y RNAs and vault RNAs, suggesting that it can catalyze pseudouridylation of many RNA types.
Catalytic Activity: a uridine in tRNA = a pseudouridine in tRNA
Sequence Mass (Da): 74793
Sequence Length: 660
Subcellular Location: Nucleus
EC: 5.4.99.-
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O74343 | MSQENHVDVPRKRIRIDQSESSRNLERNGLEDEANAPSDLSGQKFYMTESDVGIDAFLNPNLPSIDGIIKARFTDFAVFEVDTDGNIVHLTDMEAHDPILSKATGDKETEDAKDSSNQDISNDQKAPSFKEQEPATLPILPNDLQSIIPKGIGNEFIQSLHKLSVGEITDPISLILPENTPPMDKGQRTILHQFIRNNFSGLESSTKGNGTFTVSKTTRKNQPRSRRDPRLSWKALGGEYCHFHLYKENRDSMDCLGKIARLLKVPTRTLSIAGTKDRRGVTCQRVAIHHVRASRLAQLNSGSLKNSTYGFLLGNYSYKNSNLRLGDLKGNEFHIVVRNVITPKEKVVEALNSLKEHGFINYFGLQRFGTSSVGTHTIGVRLLQSDWKGAVDLILSPRPEHTGSVKEAIDLWHSTHDAEASLRILPRRMIAESSILETWSRSGNQTDYLGAFQRIPRHLRSIYPHAYQSYVWNRVASWRIKNLGDRPVVGDLVYSTESNGLSQKSPIVDPEAPDLLEDLPVSSKLSARPIEEDEVNNFSIYDIVLPLPGRNVIYPKNETFDIYKSVMNEASLDPLNMSRKDRELSLPGDYRKLLVRPENMEFNFIKYDNMEQQLILTDKDRLENRSISVSSEVGKHTAVTLKFVLPSSAYATMALREALRTATASGDQRMLMPAVLKDSI | Function: Catalyzes pseudouridylation at position 35 in U2 snRNA stem-loop II region which induces particular conformation of the mRNA-U2 snRNA duplex and places the nucleophile in an accessible position for the first step of splicing. Also catalyzes pseudouridylation at position 56 in U2 snRNA. Catalyzes also pseudouridylation at position 50 in 5S rRNA, position 13 in cytoplasmic tRNAs, and position 35 in pre-tRNA(Tyr). Pseudouridine residues in tRNAs may stabilize the local RNA conformation, favor interactions with protein partners and play an important role in the stabilization of the codon-anticodon interaction with mRNA. Also catalyzes pseudouridylation of mRNAs in response to heat shock: mediates pseudouridylation of mRNAs with the consensus sequence 5'-UGUAR-3'.
Catalytic Activity: uridine in 5S rRNA = pseudouridine in 5S rRNA
Sequence Mass (Da): 76438
Sequence Length: 680
Subcellular Location: Nucleus
EC: 5.4.99.-
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Q08647 | MSDSSEATVKRPLDAHVGPSENAAKKLKIEQRTQADGIHEADVGITLFLSPELPGFRGQIKQRYTDFLVNEIDQEGKVIHLTDKGFKMPKKPQRSKEEVNAEKESEAARRQEFNVDPELRNQLVEIFGEEDVLKIESVYRTANKMETAKNFEDKSVRTKIHQLLREAFKNELESVTTDTNTFKIARSNRNSRTNKQEKINQTRDANGVENWGYGPSKDFIHFTLHKENKDTMEAVNVITKLLRVPSRVIRYAGTKDRRAVTCQRVSISKIGLDRLNALNRTLKGMIIGNYNFSDASLNLGDLKGNEFVVVIRDVTTGNSEVSLEEIVSNGCKSLSENGFINYFGMQRFGTFSISTHTIGRELLLSNWKKAAELILSDQDNVLPKSKEARKIWAETKDAALALKQMPRQCLAENALLYSLSNQRKEEDGTYSENAYYTAIMKIPRNLRTMYVHAYQSYVWNSIASKRIELHGLKLVVGDLVIDTSEKSPLISGIDDEDFDEDVREAQFIRAKAVTQEDIDSVKYTMEDVVLPSPGFDVLYPSNEELKQLYVDILKADNMDPFNMRRKVRDFSLAGSYRTVIQKPKSLEYRIIHYDDPSQQLVNTDLDILNNTRAKESGQKYMKAKLDRYMPDKGGEKTAVVLKFQLGTSAYATMALRELMKLETSRRGDMCDVKENI | Function: Catalyzes pseudouridylation at position 35 in U2 snRNA stem-loop II region which induces particular conformation of the mRNA-U2 snRNA duplex and places the nucleophile in an accessible position for the first step of splicing . Also catalyzes pseudouridylation at position 56 in U2 snRNA . Catalyzes also pseudouridylation at position 50 in 5S rRNA, position 13 in cytoplasmic tRNAs, and position 35 in pre-tRNA(Tyr) . Pseudouridine residues in tRNAs may stabilize the local RNA conformation, favor interactions with protein partners and play an important role in the stabilization of the codon-anticodon interaction with mRNA . Also catalyzes pseudouridylation of mRNAs in response to heat shock: mediates pseudouridylation of mRNAs with the consensus sequence 5'-UGUAR-3' .
Catalytic Activity: uridine in 5S rRNA = pseudouridine in 5S rRNA
Sequence Mass (Da): 77002
Sequence Length: 676
Subcellular Location: Nucleus
EC: 5.4.99.-
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Q12069 | MQRNNRLRNLFTVPVIMARQLKRNALSAGLAFAGNATSNEFDEHLQNEVEREREIQKKKKIKRTQSKKSPDLINKSTFQSRTIGSKKEKHRQLDPEYEIVIDGPLRKIKPYHFTYRTFCKERWRDKKLVDVFISEFRDRESEYYKRTIENGDVHINDETADLSTVIRNGDLITHQVHRHEPPVTSRPIKVIFEDDNIMVIDKPSGIPVHPTGRYRFNTITKMLQNNLGFVVNPCNRLDRLTSGLMFLAKTPKGADNIGDQLKAREVTKEYVAKVVGEFPETEVIVEKPLKLIEPRLALNAVCQMDEKGAKHAKTVFNRISYDGKTSIVKCKPLTGRSHQIRVHLQYLGHPIANDPIYSNDEVWGNNLGKGGQADFDIVITKLDEIGKRKPAKSWFHSNGGYGEVLRQEKCSICESDLYTDPGPNDLDLWLHAYLYESTETEEGTEKKKWCYKTEYPEWALRR | Function: Responsible for synthesis of pseudouridine from uracil-32 in mitochondrial transfer RNAs.
Catalytic Activity: uridine(32) in tRNA = pseudouridine(32) in tRNA
Sequence Mass (Da): 53399
Sequence Length: 462
Subcellular Location: Mitochondrion
EC: 5.4.99.28
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A2X8M8 | MADTGGRPEVSLATVRSPGHPAASTTAAAAADLGHADTGQEKPTVESAQPANGAAPMGECGTEYRGLPDGDAGGPMPSSARTVSMIPLIFLIFYEVSGGPFGIEDSVGAAGPLLAIIGFLVLPVIWSIPEALITAELGAMFPENGGYVVWVASALGPYWGFQQGWMKWLSGVIDNALYPVLFLDYLKSGVPALGGGAPRAFAVVGLTAVLTLLNYRGLTVVGWVAICLGVFSLLPFFVMGLIALPKLRPARWLVIDLHNVDWNLYLNTLFWNLNYWDSISTLAGEVKNPGKTLPKALFYAVIFVVVAYLYPLLAGTGAVPLDRGQWTDGYFADIAKLLGGAWLMWWVQSAAALSNMGMFVAEMSSDSYQLLGMAERGMLPSFFAARSRYGTPLAGILFSASGVLLLSMMSFQEIVAAENFLYCFGMLLEFVAFILHRVRRPDAARPYRVPLGTAGCVAMLVPPTALIAVVLALSTLKVAVVSLGAVAMGLVLQPALRFVEKKRWLRFSVNPDLPEIGVIRPPAAPDEPLVP | Function: Cell membrane polyamine/proton symporter involved in the polyamine uptake in cells. Possesses high affinity for spermidine and lower affinity for spermine and putrescine. Transports paraquat, a polyamine analog, and thus confers sensitivity to this chemical which is used as herbicide (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 56626
Sequence Length: 531
Subcellular Location: Cell membrane
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P09368 | MIASKSSLLVTKSRIPSLCFPLIKRSYVSKTPTHSNTAANLMVETPAANANGNSVMAPPNSINFLQTLPKKELFQLGFIGIATLNSFFLNTIIKLFPYIPIPVIKFFVSSLYCGGENFKEVIECGKRLQKRGISNMMLSLTIENSEGTKSLSSTPVDQIVKETISSVHNILLPNIIGQLESKPINDIAPGYIALKPSALVDNPHEVLYNFSNPAYKAQRDQLIENCSKITKEIFELNQSLLKKYPERKAPFMVSTIDAEKYDLQENGVYELQRILFQKFNPTSSKLISCVGTWQLYLRDSGDHILHELKLAQENGYKLGLKLVRGAYIHSEKNRNQIIFGDKTGTDENYDRIITQVVNDLIINGEDSYFGHLVVASHNYQSQMLVTNLLKSTQDNSYAKSNIVLGQLLGMADNVTYDLITNHGAKNIIKYVPWGPPLETKDYLLRRLQENGDAVRSDNGWPLIKAIAKSIPKRVGL | Function: Converts proline to delta-1-pyrroline-5-carboxylate.
Catalytic Activity: a quinone + L-proline = (S)-1-pyrroline-5-carboxylate + a quinol + H(+)
Sequence Mass (Da): 53271
Sequence Length: 476
Pathway: Amino-acid degradation; L-proline degradation into L-glutamate; L-glutamate from L-proline: step 1/2.
Subcellular Location: Mitochondrion matrix
EC: 1.5.5.2
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P78568 | MATAQLATFKIPPVSNEPMLSYAPGSPERAGLQAALAEMQSQLPFEVPCIINGQEVRTNNIQKQPMPHDHARHLCTFHEGSPELVEKATCGALQAKDGWETMPWNDRAAIFLKAADLASGKYRYKLMAATMLGQGKNTWQAEIDAAAELADFFRFGVSYVEELYAQQPPKNAPGCWNRTEYRPLEGFVLAVSPFNFTAIGGNLPGSPALVGNVVVWKPAPAATYSNYLVFKILSEAGVPPGVIQFIPGGAEIVQAAIQSPNFRSLHFTGSTNVFKSLWKDISSNLDKYKVYPRIVGETGGKNWHVIHKSAEVRNAVLQSVRGAFEYQGQKCSALSRLYVSRSVWENGFKTQYLEEIAKIKVGPCLDWNNYMGPVIGRRAYDNITGFIKKAKEEGGEVLIGGSGDDSKGFFIQPTVILTKVPRSTTMVGEIFGPVVTAYVFEDSDYEKTLELIDTTSIYGLTGAIFASERQALLTATNRSRNAAGNIYYNEKCTGAVVGQQPFGGARGSGTNDKAGSISIFYRFVSARSIKENFVGLEDFHYPSNLV | Catalytic Activity: H2O + L-glutamate 5-semialdehyde + NAD(+) = 2 H(+) + L-glutamate + NADH
Sequence Mass (Da): 59757
Sequence Length: 546
Pathway: Amino-acid degradation; L-proline degradation into L-glutamate; L-glutamate from L-proline: step 2/2.
Subcellular Location: Cytoplasm
EC: 1.2.1.88
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Q9P8I0 | MQSSMLLRVRALPKTASVLSRTKTATYATYKVPRIDNEPNKHYAAGSPDRKALQEALARTQRNAPLSVPLVIAGKEVKSSSSLTQSNPASHGPVATYSNATAKDVQAAIESALEARKSWASTPFADRASVFLKAADLISTKYRYDVMALTMHGQGKNAWQAEIDSAAELCDFFRFGVKYAEDLYAQQPVHHAPGVWNRVEYRPLEGFVYAISPFNFTAIGGNLAGAPALMGNVVVWKPSPSAIASNWLVHQILLEAGLPKNVIQFVPGEAEEVTKTVLDHPDFAALHFTGSTNVFRNLYGQISTRVAAGKYRSYPRIVGETGGKNFHLIHKSADIRNAAVQTVRGAFEYQGQKCSATSRVYVASSIADSFLEQVASEAKSLKVGPPSDFTNFCGPVIHEASFTKLAKVIDEAKNDPELELLAGGSYDSSKGWYIQPTVYRTTNPDHPLLTRELFGPILVVYAYPDATEADFARIAQKIDATGEYGLTGSVFAQDREALAVANDVLRNAAGNFYINCKSTGAVVGQQPFGGARASGTNDKAGSGNLLSRFVSLRSIKEEFVPTYKVAYPSNEA | Catalytic Activity: H2O + L-glutamate 5-semialdehyde + NAD(+) = 2 H(+) + L-glutamate + NADH
Sequence Mass (Da): 61936
Sequence Length: 572
Pathway: Amino-acid degradation; L-proline degradation into L-glutamate; L-glutamate from L-proline: step 2/2.
Subcellular Location: Mitochondrion matrix
EC: 1.2.1.88
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O74766 | MSQFAEFKLPAIKNEPPKHYGPNSADREGIVKAYKELEAELPVTIPVIIDGKEVETNTIGEQRCPFEHKKVVARYHRAGAKHVEDAIEAALRGKKVWESLPFADRSAIFLKAAHLISTKYRYKLMAATMIGQGKNIWQAEIDAGMEIIDFLRFNTKYASELYASQPPENTPGVWNRMEYRPLEGFVYAITPFNFTAIAGNLAAAPLLMGNVVLMKPSDHAVLSSYIVYQIFREAGLPAGALQFIPGDAVEVSKVCFNHPEFAGLHFTGSTAVFRSLWGTIGENVANGKYRTYPKIVGETGGKNFHLVHSSAEIKSAVVNAVRAAFEYQGQKCSALSRLYVSKYAWENGFRDELTKQVKSLKVGAPLTDFANFVGPVIHQASFNKLKKVLESAASDSEIEVLAGGKADDSEGFFVEPTVLLSKNPKHDIFVNELFGPVLSVYVYEDDNLDAVCDLIDTTTPYGLTGSIFAQDRVVVRKLTDRLRNAAGNFYINDKCTGAVVGEQPFGGARASGTNDKAGSGMILSRFVSPRSIKDTFAYADSVLYPSNF | Catalytic Activity: H2O + L-glutamate 5-semialdehyde + NAD(+) = 2 H(+) + L-glutamate + NADH
Sequence Mass (Da): 60219
Sequence Length: 548
Pathway: Amino-acid degradation; L-proline degradation into L-glutamate; L-glutamate from L-proline: step 2/2.
EC: 1.2.1.88
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P07275 | MLSARCLKSIYFKRSFSQLGHIKPPKHIRNEPVKPFRNIDLKDWDLLRASLMKFKSSSLEVPLVINGERIYDNNERALFPQTNPANHQQVLANVTQATEKDVMNAVKAAKDAKKDWYNLPFYDRSAIFLKAADLISTKYRYDMLAATMLGQGKNVYQAEIDCITELSDFFRYYVKYASDLYAQQPVESADGTWNKAEYRPLEGFVYAVSPFNFTAIAANLIGAPALMGNTVVWKPSQTAALSNYLLMTVLEEAGLPKGVINFIPGDPVQVTDQVLADKDFGALHFTGSTNVFKSLYGKIQSGVVEGKYRDYPRIIGETGGKNFHLVHPSANISHAVLSTIRGTFEFQGQKCSAASRLYLPESKSEEFLSDMFGILQSQNVVPMNTSASPISGGNLRGFMGPVIHEQSFDKLVKVIEDAKKDPELEILYGGQYDKSQGWFVGPTVIKAKRPDHPYMSTEFFGPILTVYEYPDTEFNEICDIIDNTSQYALTGAIFAKDRKAIEYADEKLKFSAGNFYINDKCTGAVVSQQWFGGARMSGTDDKAGGPNILSRFVSIRNTKENFYELTDFKYPSNYE | Catalytic Activity: H2O + L-glutamate 5-semialdehyde + NAD(+) = 2 H(+) + L-glutamate + NADH
Sequence Mass (Da): 64435
Sequence Length: 575
Pathway: Amino-acid degradation; L-proline degradation into L-glutamate; L-glutamate from L-proline: step 2/2.
Subcellular Location: Mitochondrion inner membrane
EC: 1.2.1.88
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Q9C9M3 | MTTTPDWIMIGGDGPESYNQQSSYQRALLEATKDKMTKAISANLDLDLISNRFIVADFGCASGPNTFVAVQNIIDAVEEKYRRETGQNPADNIEFQVLFNDFSLNDFNTLFQTLPPGRRYFSAGVPGSFFERVLPKESFHIGVMSYAFHFTSKIPKGIMDRDSPLWNKDMQCTGFNPAVKKAYLDQYSIDTKILLDARAEELVPGGLMLLLGSCLRDGVKMSETPKGTVMDFIGESLSDLAKQGVTEQEKVDTFRTSIYFAEQGEIRQIIEENGKFTIEAFEDIIHAKNEFPFDPKTLAISFKAFYGAFISAHFGVEVMRKAFELVEVKAREQISRLHNSKPGMQYLIVLRKN | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Methyltransferase that may methylate 1,7-paraxanthine . Prevents seed germination and modulates root architecture during early seedlings development . Plays a minor role in defense responses toward pathogenic bacteria (e.g. P.syringae) .
Sequence Mass (Da): 39780
Sequence Length: 353
EC: 2.1.1.-
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O04200 | MSDALINGLAGAGGGIIAQLLTYPLQTVNTRQQTERDLKREKRKLGTIEHMCQVVKQEGWERLYGGLAPSLAGTAASQGVYYYFYQVFRNRAEATALARKKKGLGDGSVGMFASLLVAAFAGSVNVLMTNPIWVIVTRMQTHRKMTKDQTAAPESPSSNAEALVAVEPRPYGTFNTIREVYDEAGITGFWKGVIPTLIMVSNPSMQFMLYETMLTKLKKKRALKGSNNVTALETFLLGAVAKLGATVTTYPLLVVKSRLQAKQVTTGDKRQQYKGTLDAILKMIRYEGLYGFYKGMSTKIVQSVLAAAVLFMIKEELVKGAKLLLSNATSS | Function: Mediates the NAD(+) import into peroxisomes. Favors the NAD(+)(in)/AMP(out) antiport exchange, but is also able to catalyze a low unidirectional transport that might be essential under special conditions. Transports CoA, dephospho-CoA, acetyl-CoA, adenosine 3',5'-diphosphate (PAP), NAD(+), AMP, ADP and NADH, but has no activity with ATP, GTP, GDP, NADPH, NADP(+) or FAD. Required for peroxisomes proliferation.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36213
Sequence Length: 331
Subcellular Location: Glyoxysome membrane
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Q9Y7M1 | MSISFSELVAKTLLDLEVKVVFGIVGIPVIEICEAIQASGIRFVGFRNEQSAAYAATAYGYLTQRPGVCVVVGGPGVVHAMAGVFNSKTNRWPLLLLAGSSETFQQNCGAFQELDQVSYLSPHTKLAVRPPSPKMVVDSIRRAYRVSMTGTPGTCYVDLPANYIESTVDDFPKDPLPPIPSSPKCAPDPTQLQKAAYYLKNAKAPLLVVGKGAAYACAEKQLLEFVEHTGIPFLPSPMGKGLLPESHPLNVSSARSAALRNADVVLLAGARLNWIFQYGLPPKWSPNAKFIQIDTNAETLGNNAADLDLAIWADVGLTIDCLFKLVQTWKYSVGISTPYLRTLNETRSKNEKKALESRKSSIPLQMNYALYVVNEELQSLSLKSKRNITWVSEGANTMDRGRQLLEVTHPRGRLDAGTMSTMGVGMGYAIASAFAHSSDKIVVVEGDSAFGFSAMELETAIRNQLDLLVIVINNNGVYHGLDTDAYETLRDNHQLPTTALGTSIRYDQICEACGGKGFFVKNEEDLRSSLRKAWQTSSVSLINVMVDPEAARKLTFAWMSSTKVKPKL | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes a carbon-carbon cleavage reaction; cleaves a 2-hydroxy-3-methylacyl-CoA into formyl-CoA and a 2-methyl-branched fatty aldehyde.
Sequence Mass (Da): 61937
Sequence Length: 568
Domain: Peroxisomal targeting signal 1 (PTS1) is a tripeptide located at the C-terminus of more than 95% of all peroxisomal matrix proteins. The prototypical PTS1 is the terminal tripeptide SKL (serine-lysine-leucine) but the consensus of PTS1 is defined as [S/A/H/C/E/P/Q/V] [K/R/H/Q] [L/F]. However, this description of the PTS1 consensus must probably be expanded beyond the terminal tripeptide.
Subcellular Location: Cytoplasm
EC: 4.1.-.-
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P39994 | MTTTATQHFAQLLQKYGIDTVFGIVGIPIVQLADTMVANGIKFIPCRNEQAASYAASAYGYISDKPGVLLIVGGPGLIHALAGIYNSMSNRWPLLVIAGSSSQSDIHKGGFQELDQVSLLSPFLKFTGKLTPDNIDMITQKALNYCIQGTAGVSYIDVPADFIEYEKPLEGNDRTGNELPMILTPNICGPDPSKIKKVVQLILQHKNKNILIVIGKGAVKNSHEIRRLVNTFNLPFLPTPMAKGIVPDSSPLNVSSARSQALKIADIVLVLGARLNWILHFGTSPKWNSESIFIQFDSNPETLGDNNVSPGADLSIWGDIGLSVTALVEELTRQDSCWKYSGVKQEIREKIQLNQTRLLRKEKTRGAQLNYNQVYGTLRPLIDDYRTILVTEGANTMDIARISFPTDAPRRRLDAGTNATMGIGLGYALACKASHPELDVVLIQGDSAFGFSAMEIETAVRCQLALVIVVMNNSGIYHGEKDIEGDLPPTALSKNCRYDLVGKGLGANDFFVNTISELSRCFQQAVQLSRTKRETSVINVIIEPGEQKQIAFAWQNKPRL | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes a carbon-carbon cleavage reaction; cleaves a 2-hydroxy-3-methylacyl-CoA into formyl-CoA and a 2-methyl-branched fatty aldehyde.
Sequence Mass (Da): 61288
Sequence Length: 560
Domain: Peroxisomal targeting signal 1 (PTS1) is a tripeptide located at the C-terminus of more than 95% of all peroxisomal matrix proteins. The prototypical PTS1 is the terminal tripeptide SKL (serine-lysine-leucine) but the consensus of PTS1 is defined as [S/A/H/C/E/P/Q/V] [K/R/H/Q] [L/F]. However, this description of the PTS1 consensus must probably be expanded beyond the terminal tripeptide.
Subcellular Location: Cytoplasm
EC: 4.1.-.-
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O74758 | MTHNTMLQRFNGLLEPTHLYIVSVVAYSACNRPDKISGIAKEAMEHVGPSIYPKLREALVKSSPLVGFPRTINSLREMTTNIPPPFPDEFARAADADIDTGKRGKIYFEKTYGKVTQRVLRSMQSSSLDLANIALDYAYGKVLSFNEVVSPLETSLMIIAALVPQDVNPQLRGHLKGALNHGATKEQVMSARNIALEISKECGIQFKGDIETL | Function: Probably involved in peroxisome formation or maintenance as well as in amino acid metabolism.
Sequence Mass (Da): 23489
Sequence Length: 213
Domain: Peroxisomal targeting signal 1 (PTS1) is a tripeptide located at the C-terminus of more than 95% of all peroxisomal matrix proteins. The prototypical PTS1 is the terminal tripeptide SKL (serine-lysine-leucine) but the consensus of PTS1 is defined as [S/A/H/C/E/P/Q/V] [K/R/H/Q] [L/F]. However, this description of the PTS1 consensus must probably be expanded beyond the terminal tripeptide.
Subcellular Location: Peroxisome matrix
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P47148 | MNQILNAQRLIQLSQFHPKLKNIWYLVAAATFSVCNEPQEIPKLYHYAMLLSNDNAHMYRFTLASQTIDLLRSELPMRKTLINENYQQPTFFQKQLTAKFREVILKTGPLAGLPRAINGLTMLKETTPDILVPHLDPIDPWEAAMGNSSPLSETSMRRKHDKTIQERDHTIQNGLRHWNSIYNKVSTRVVNNLNSSYPDLWYYTLVHVYGPLFAFDEILSAQETSLVIIASLVPQDVNPQLRGHLKGALNIGCDKETVEAVRGLAILISQWCGVSWKSGVVKL | Function: Probably involved in peroxisome formation or maintenance as well as in amino acid metabolism.
Sequence Mass (Da): 32208
Sequence Length: 283
Domain: Peroxisomal targeting signal 1 (PTS1) is a tripeptide located at the C-terminus of more than 95% of all peroxisomal matrix proteins. The prototypical PTS1 is the terminal tripeptide SKL (serine-lysine-leucine) but the consensus of PTS1 is defined as [S/A/H/C/E/P/Q/V] [K/R/H/Q] [L/F]. However, this description of the PTS1 consensus must probably be expanded beyond the terminal tripeptide.
Subcellular Location: Peroxisome matrix
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Q8U920 | MAAIDLNSDLGESYGAWRMGDDEAMLAIVSSANIACGFHAGDPAGIYRTVKAAAEKGVVVGAHVSYPDRVGFGRRDLDATSEELIADVIYQIGALKGVAAAAGTTVRYVKPHGALYNRIANDAKQGQAVIDGIKAIDPSLVLMGLANAPILDLARKAGLAVVAEAFADRAYTPEGQLVSRREAGAVLHDAAKIAERMVQLAREGTLEAIDGSIIKIEAQSICVHGDSPGAVAIAQEIRRRFEADGIAIRSFASDR | 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): 26709
Sequence Length: 255
EC: 3.5.2.9
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Q89P49 | MKIGINSDMGEGFGNYRICDDEALMSIVSSANVACGFHAGDPIIMDRMVRLAKQKGVEVGAHPGLPDLLGFGRRVIQMDAAELEKHMVYQIGALQAIAANAGHRVTHVSFHAAMGNMVNADPDMADVVARAIATINRDFIVFSQPDAEIVRAARKVGLRTLTLFLADRAYDENGHLVSRKLPNSVVTSTEAVAERVKRFLDSGTVQTIEGKSIKVEARSILIHSDTPGSVNLAGTVRRVIEQGGGEVTPATVLLN | 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): 27341
Sequence Length: 255
EC: 3.5.2.9
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Q9I626 | MTEVDLNSDMGEGFGPWTIGDGVDAAIMPLISSANIATGFHAGDPSSMRRTVEMAAEHGVAIGAHPGFRDLVGFGRRHIAAPAIELVNDMLYQLGALREFARLQGLSLQHVKPHGALYMHLARDEVAARLFVETLQRLEPELLLYCMPGSATWRIGRELGQPLVREFYADRDYDRSGSIVFTRRVAALDPQQVADKVLRACREGKVRTVEGEDLDIAFDSVCIHSDTPGALELVASTRARLEGAGIRIKAPR | 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): 27559
Sequence Length: 252
EC: 3.5.2.9
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Q881H6 | MRIDLNADLGEGFGAWTMGEDEALMQLISSANVACGFHAGDPLIMDSTVRRAKALGIDLGAHVGFPDLQGFGRRRMNIELKELCAIVVYQLGALAGIATAAGYRVTHMSFHGALGNMAAADAELAGPLVKAVARFDPQMIISSSSSEAIEQAAQACNLRVATTFLADRAYDENCLLVPRGIAGAVVKDPEQVRARVAQLLQDGTVTTLSGKRVAVNAQSILLHGDTPGAVELARSIRHSIEEQGGVITPVSQLLGS | 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): 26890
Sequence Length: 256
EC: 3.5.2.9
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B2GE66 | MTRIDLNSDLGESFGRYTIGNDDQVLDLITAANVACGFHAGDPDVMAQTVALAETKGVAIGAHPGFPDLGGFGRRKLDMTPAEVKNMVTYQVSALMGFTKDHRLHHVKPHGALYNAAAKDLALARAICEGVAQVDDQLPLYGLAGSQLLEAAKEVGLPAYSEVFADRGYQADGSLVPRSQPNAVLTDPLAVAERALSMVQTQSVTAVTGETVPLKVDTICVHGDNQAALALVDQLRQTFTANGITIQAC | 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): 26271
Sequence Length: 249
EC: 3.5.2.9
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B9E7M7 | MYIDLNADLGESFGNYKIGNDEAIIPLITSANIACGMHAGDFNVLNQTIELCKAHGTGIGAHPGYPDLQGFGRRNLDMTYDEVENLITYQLGAIDAFCIKHGMKMNHVKPHGALYNATSGNEGLAEAIVNAIYNFNPELKVMGISGGTLVKATEAKGMTAINEVFADRNYTDAGTLVSRKQSNAMIHHQQAAVEHVLRMVRDNQVKTETGKLIDLRADSICVHGDGPEALAFVKAIIETLNNEGIKVQTI | 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): 27043
Sequence Length: 250
EC: 3.5.2.9
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A4T5K5 | MSSVDLNADLGEGFGVWALGDDDAMLDIVTSANVACGFHAGDPATLRRVCEAAAARGVRIGAQVSYRDLAGFGRRFIDVSSEDLIADVMYQIGALSALAAAAGSSVSYVKPHGALYNAVVTNRLQAHALAAAVHAVDPALPVLGLAGSVFFGAAEELGLRTVPEAFADRAYRPDGRLVSRRERNSVLHDVDEIAERVISMVSRGRVHAVDGSTIPITVESVCVHGDSPGAVQIATAVRKRLVAEGVTLASFS | 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): 26252
Sequence Length: 252
EC: 3.5.2.9
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B8ZUB2 | MACIDLNADLGEGFGVWRLGDDEAMLRIVTSANVACGFHAGDPAGLLRVCRLAAERGVRIGAQVSYRDLVGFGRRFIDVTADDLLADVVYQIGALQAIAQTAGSAVSYVKPHGALYNTIVTNREQGAAVAAAIQLVDSTLPVLGLAGSTFFDEAARIGLRTVAEAFADRTYRPDGQLISRREPGAVLHDPAVIAQRVVTMVTTGKATAVDGTQLAVTVESICLHGDSPNAIQMATAVRDQLNAAGIDIRAFC | 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): 26453
Sequence Length: 252
EC: 3.5.2.9
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B2HJ17 | MPYIDLNADLGEGFGIWQLGDDDAMLGIVTSANVACGFHAGEPAGLLRVCRAAAERGVRIGAQVGYRDLAGFGRRFIDVDPEDLVAEVVYQIGALQAIAQSCGSTVSYVKPHGALYNTIVTHRDQAAAVAEAVQMVDATLPVLGMTGSVFFQQATDLGLRTVAEAFADRAYRSDGQLVSRREHGAVLADAAAIAQRAVSMVASGKVTAVDGTQVPITMESICVHGDSPGAVQIATAVRDRLTAAGNEIRAFC | 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): 26337
Sequence Length: 252
EC: 3.5.2.9
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Q8WXC3 | MGTKREAILKVLENLTPEELKKFKMKLGTVPLREGFERIPRGALGQLDIVDLTDKLVASYYEDYAAELVVAVLRDMRMLEEAARLQRAA | Function: Associates with PYCARD/ASC and modulates its ability to collaborate with MEFV/pyrin and NLRP3/cryopyrin in NF-kappa-B and pro-caspase-1 activation. Suppresses kinase activity of NF-kappa-B inhibitor kinase (IKK) complex, expression of NF-kappa-B inducible genes and inhibits NF-kappa-B activation by cytokines and LPS.
PTM: Phosphorylated.
Sequence Mass (Da): 10107
Sequence Length: 89
Subcellular Location: Cytoplasm
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A0A8F4NV97 | MLQEDKSSETMHDPSTRGVETRNVTAVDSPLETATTSESPETERTNVAPAKRDWRFWALLVSISLAGLLTALEGTITSTALPSIVNDLGGGHLYVWVVNGYLFAMTAMQPMYGQLANIFGRRWPMLGATALFVLGSGICGGATNIETLIAGRILQGIGASGTTVLTETIICDVVPLRERSKFLAIVMGMIFLGTALGPFFAGLIVQYSTWRWTFYLALPVGGAALVALFSFLKVKYQKETNLATKISTIDWAGNALFVAAISSVLIGLSWAGSVYAWSSFRVLVPLFVGIAGMGLFMVFEGSRFAPNPTVPLHLFGNRTSVGVMIMTFFHGIITIWQLYFMPVYFQGVLGSSPSRSGVQILATILAILPAAGIGGFLMTKMGRYKPIHYASWAVTLIGLGLFSLLDSGSSTGAWVGFQIVYSMGAGMLVPTLLPALLAPLSESDTALGAATWSFVRSFGMVWGTAIPAAVFNTRSDQLAPELINSPALRADIMGGKAYEHATSAFLGTLSDAASEQMKNVFSRSLRQTWLVSLAFAGMGLLAATLAREVPMRSELDTEYGMEERKPKKASEA | Function: MFS-type transporter; part of the gene cluster that mediates the biosynthesis of pyrrocidines, fungal natural products containing a macrocyclic para-cyclophane connected to a decahydrofluorene ring system that show potent antibiotic activities toward Gram-negative bacteria.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 61340
Sequence Length: 572
Subcellular Location: Membrane
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A0A8F4NVX8 | MSSTMRGWVRQHRGPYESSLKLIDSLPVPPDPGSDSSDIIVRVSYVALEFSIAHIMGIFPALPFAPPLVPEICVSGTVASAGGKAPEELRQPGTQVLAMTDPMSMMLFGTGALKEYMRLPEQYVVPLLQPSHSVTTDHPHGTAERPQALTLAEGAGLISNGSAAQAVVRAANVLSGQRVLVNGASGSVGHIVSQLCRARGAYVVGVASGVNQDFVRRYGCNEFVDYTKHTDLPEYLASTYGSQPFDSILDCVGSQDLYANSPRYLLPGRPLVNIGAFSMTDSLLSTLYQWSMNSWCPTWLGGVPRPYILFSNTPDMQGVLSLVEMVQQGKLKVHIDSEFEMEDLIKAYERVTSKRARGKVLIRIH | Function: Medium chain reductase; part of the gene cluster that mediates the biosynthesis of pyrrocidines, fungal natural products containing a macrocyclic para-cyclophane connected to a decahydrofluorene ring system that show potent antibiotic activities toward Gram-negative bacteria . Within the pathway, pydE functions synergistically with pydB, pydX and pydZ to form the cyclophane . The pathway begins with the PKS-NRPS pydA which, with the help of the trans-enoyl reductase pydC, synthesizes the polyketide-tyrosyl acyl thioester product which can be reductively off-loaded by the terminal reductase (R) domain in pydA. The alpha/beta hydrolase pydG is then required to catalyze the subsequent Knoevenagel condensation that affords the 3-pyrrolin-2-one ring, whereas the four proteins pydB, pydE, pydX and pydZ then function synergistically to form the cyclophane. PydB and the membrane-bound pydX and pydZ are lipid-binding proteins that can sequester and mold the pdyG product into the inverse S-shape. Binding of the medium chain reductase pydE to the complex would trigger the cascade oxidative cyclization. PydY is involved in the Diels-Alder cycloaddition that forms the decahydrofluorene core. Additional non-enzymatic hydroxylation yields pyrrocidine A2 which can be further reduced into pyrrocidine B by an endogenous reductase (Probable).
Sequence Mass (Da): 39654
Sequence Length: 365
Pathway: Mycotoxin biosynthesis.
EC: 1.-.-.-
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A0A8F4NUC6 | MATPGNVTFKNTHDSWGMNWGLCDSSEQMLTMQGMPWIMRKLASWISVTVVIKTWTDPETGETRFLLQHNPPMGLPGMSEERALDYVPDELTVPNLGKLRVRTRWGTAKELDQLDKYLARGLEKGPHSMIHMMTEHLDIDAVTHQIFGYEEIDGTRYHVRRIVVRKGHEVARLRLVYNYLGPRAG | Function: Pericyclase; part of the gene cluster that mediates the biosynthesis of pyrrocidines, fungal natural products containing a macrocyclic para-cyclophane connected to a decahydrofluorene ring system that show potent antibiotic activities toward Gram-negative bacteria . Within the pathway, pydY is involved in the late Diels-Alder cycloaddition step that leads to the formation of the decahydrofluorene core . The pathway begins with the PKS-NRPS pydA which, with the help of the trans-enoyl reductase pydC, synthesizes the polyketide-tyrosyl acyl thioester product which can be reductively off-loaded by the terminal reductase (R) domain in pydA. The alpha/beta hydrolase pydG is then required to catalyze the subsequent Knoevenagel condensation that affords the 3-pyrrolin-2-one ring, whereas the four proteins pydB, pydE, pydX and pydZ then function synergistically to form the cyclophane. PydB and the membrane-bound pydX and pydZ are lipid-binding proteins that can sequester and mold the pdyG product into the inverse S-shape. Binding of the medium chain reductase pydE to the complex would trigger the cascade oxidative cyclization. PydY is involved in the Diels-Alder cycloaddition that forms the decahydrofluorene core. Additional non-enzymatic hydroxylation yields pyrrocidine A2 which can be further reduced into pyrrocidine B by an endogenous reductase (Probable).
Sequence Mass (Da): 21246
Sequence Length: 185
Pathway: Mycotoxin biosynthesis.
EC: 5.-.-.-
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O30130 | MMRHLISIGDLDREDINYILKKAEEFEDVARGEKKLRILEGKILGNLFFEPSTRTRMSFETAMKRLGGDVINMTAQEASSIAKGETLADTIRVVSGYCDAIVIRHPLEGAARFAAENSSVPVINAGDGAGQHPTQTLLDLYTIKKECGRLDGITIALMGDLKYSRTIHSLIKALALFDMRIYLISPEALALPEDIIEDVSAEIRRARLEEVISEIDVLYVTRIQKERFPDEEEYRKVSGSYRITAETLKSAKDSMIVMHPLPRVDEIHPSVDSTKHARYFQQSFYGVPVRMAILSEVML | Catalytic Activity: carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-aspartate + phosphate
Sequence Mass (Da): 33634
Sequence Length: 299
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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A0JX76 | MKHLLSTEDLSLANAIRILDTAEEMAAVGDREVKKLPALRGRTVVNLFFEDSTRTRISFEAAAKRLSADVINFAAKGSSVSKGESLKDTAQTLAAMGADAVVIRHWASGAPHRLAATDWIDAAVINAGDGTHEHPTQALLDAFTMRRHWARLHGTPSAGADLKGMRVAIAGDVLHSRVARSNVWLLRTLGAEVTLVAPPTLLPIGVGQWPCSVSYDMDETLAKGVDAVVMLRVQGERMNASFFPTTREYSRRWGFDDNRLRALDSLGLKDTIIMHPGPMNRGLEISSAAADSPRSTVLAQVRNGVSVRMAALYLLLSGDTREPALTPNAAYSTKESH | Catalytic Activity: carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-aspartate + phosphate
Sequence Mass (Da): 36429
Sequence Length: 337
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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Q2GGK2 | MKTLLEVSNLTSDDIESIFNLTIQYFNNTNLNHNILTGKVIVNLFFESSTRTLSSFEIAEKSLGAHSITLNINTSSINKGESIIDTISNIDAMNPDLIIIRSQYSQFIKKISEYLPSCSIINAGDGHHEHPTQALTDYCTIRYIKKDINNLNISICGDILHSRVARSNIRLLSRYGANISLVAPPTLSCNLTGISHIYHNLIEGIRNADVIMLLRLQKERIINCVIPSEQEYSHLYMLNHEKLLHAKKDVIVMHPGPTNKGIEISNNVAEKNSVILLQVKMGVAARKAILHYLLYNKSI | Catalytic Activity: carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-aspartate + phosphate
Sequence Mass (Da): 33550
Sequence Length: 299
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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A6H0I8 | MKELSVNNLLGIKYINENDINLVFETADHFKEVINRPIKKVPSLRDITIANIFFENSTRTKLSFELAQKRLSADVINFAASSSSVTKGETLVDTVNNILSMKVDMVVMRHASPGAAVFLSKNVKASIVNAGDGAHEHPTQALLDAYTIREKLGDVAGKKIVIVGDILHSRVALSNIYSLQKLGAEVRVCGPKTLIPKYIEALGVKVEPNLRKALEWCDVANMLRVQNERLDISYFPSTREYAMQYGLDKNLLDSLNKEIVIMHPGPINRGVEITSDVADSRQSVILNQVENGVAVRMAVIYLLASKIK | Catalytic Activity: carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-aspartate + phosphate
Sequence Mass (Da): 34072
Sequence Length: 308
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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Q2J833 | MGSTSRVRGTGVNRHLLSTEDLDRDDALLVLDTAERMARVAEASVRKLPTLRGRTVVNLFFEDSTRTRTSFEVAAKRLSADVINFSARGSSVSKGESLKDTAQTLEAMGADAVVCRHAASGAPHRLASWVRGSVVNAGDGTHEHPTQALLDAFTMRRRLGRIDGLAVTIVGDVLHSRVARSNVWLLATLGATVTVVAPPTLVPLGISSWPVEVSYNLDAVLPKSDVVMMLRVQRERMSAAFFPTEREYSRRYGLDADRAEMLPDHALVMHPGPMVRGMEIASRVADSARSTVVEQVANGVSVRMAVLYLLLGGSGEVS | Catalytic Activity: carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-aspartate + phosphate
Sequence Mass (Da): 34343
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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B9M4S3 | MAFKHKDIIGLQDLTREEIELLLSTAENLKEINSREIKKVPTLRGKTVVNLFYEASTRTRTSFEIAAKRLSADTINITASTSSVTKGETLSDTARNVLAMNPDIIVMRHAVSGAHHYLAKRVSCSVINAGDGAHEHPSQGLLDMLTMRQQFGKLEGLKVAIVGDITHSRVARSDIYGLTRMGANVFLAGPPTMMPPGIERLGNVTVCKDMREAVADADVVMMLRIQLERQGKTLLPTMKEYSRYFGLNQSVLKLAKKDAMVMHPGPINRGVELSSDVADGSQSHILKQVENGVAVRMSMLYHVSGGELPTE | Catalytic Activity: carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-aspartate + phosphate
Sequence Mass (Da): 34095
Sequence Length: 311
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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Q59711 | MTPIDAKRPLQLNDQGQLRHFLSLDGLPRELLTEILDTADSFLEVGARAVKKVPLLRGKTVCNVFFENSTRTRTTFELAAQRLSADVISLNVSTSSTSKGETLFDTLRNLEAMAADMFVVRHSDSGAAHFIAEHVCPDVAVINGGDGRHAHPTQGMLDMLTIRRHKGSFENLSVAIVGDILHSRVARSDMLALKALGCPDIRVIGPKTLIPIGIEQYGVKVYTDLAEGLKDVDVVIMLRLQRERMAGGLLPSEGEFYRLFGLTTARLACAKPDAIVMHPGPINRGVEIESAVADGKHSVILNQVTYGIAVRMAVLSMAMSGQNAQRQFDQENAQ | Catalytic Activity: carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-aspartate + phosphate
Sequence Mass (Da): 36410
Sequence Length: 334
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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Q4FUA5 | MSNSIDSQSIPTISPTDYTKFDPDTIHEKLDASLSRPQLNTDGSIRHFLGIEGLNKAQLRAIIAKAETFFDDKGQLINRPELEGYTVMNLFFEPSTRTRTTFEVAEKRLGANVLNIDIERSSTKKGESLRDTLWNLQAMTADIFVVRHSASGAAHFMATEVTPDIAIINGGDGWHAHPTQGMLDMLTIHREAPRPFEELSVAIVGDIKHSRVARSDISALQTLGVKDIRVCAPRTLLPKGIERFGVQVYENMNECVTDCDVIMGLRIQNERIGSPLLASSSEYYKHYGITPERMALAKPDAFVMHPGPMNRGVEIASSVADGAQSVILKQVNNGIAIRMAVLSLAMEGQRAHQAAGN | Catalytic Activity: carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-aspartate + phosphate
Sequence Mass (Da): 39238
Sequence Length: 357
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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Q9PBB8 | MNLKAITLMQFDSNGRLRHLLTLEGLSRDTLLQLLDCAAQNCALGVDPMGKRNVLAGMAVCTLFFEPSTRTRHSFHLAAQRLGADVLNFDASMSSTSKGESACDTLKNLEAMGVRGFIVRHPEEIVIAQLAAVVGEGTVLINAGAGRSTHPTQALLDMLTLCQAKGNDFSKLKLLFVGDIKHSRVARSNLHALRTLGAGQIRVCGPTALLPHDGLLSGCVVSQDFDAMLEGVDVLMMLRLQRERMEEGLVPSLEHYHANYGLTAARLARAAPDAVVLHPGPINRGVEITDEVADGPQSWILRQASNGVMVRMAVLETLLGCA | Catalytic Activity: carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-aspartate + phosphate
Sequence Mass (Da): 34637
Sequence Length: 322
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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O81355 | MASKSQILFIGGTGYIGKFIVEASAKAGYPTYVLVREASLSDPAKSKVIENFKALGVNFVLGDLYDHESLVKAIKQVDVVISTVGHGQLADQGKIIAAIKEAGNVKRFFPSEFGNDVDRSHAVEPAKSAFETKAKIRRAVEAEGIPYTYVSSNFFAGYFLPTLNQPGASSAPRDKVVILGDGNPKAIFNKEDDIGTYTIRAVDDPRTLNKVLYIRPPANTISFNELVSLWEKKIGKTLERIYVPEEQLLKNIQEAAVPLNVILSISHAVFVKGDHTNFEIEPSFGVEATALYPDVKYTTVDEYLNQFV | Function: Oxidoreductase involved in lignan biosynthesis . Catalyzes the NADPH-dependent reduction of phenylcoumaran benzylic ethers . Converts dehydrodiconiferyl alcohol (DDC) to isodihydrodehydrodiconiferyl alcohol (IDDDC) .
Catalytic Activity: (-)-dehydrodiconiferyl alcohol + H(+) + NADPH = (S)-isodihydrodehydrodiconiferyl alcohol + NADP(+)
Sequence Mass (Da): 33823
Sequence Length: 308
EC: 1.23.1.-
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A5D1A4 | MKLLIKGGTVVDPVAGKIEEKDVFIVDGKIARAGAHVNTAGAEVLDASGKLVVPGLIDMHVHLREPGFEARETIYTGTRAAARGGFTSVACMPNTSPVADNGAVISFIKACGLKGAVNVYPIGAITRGSKGEELAEMGDMKEAGAVAFSDDGMPVMNAGLMRRALQYAGMLGMVVISHCEDKNLSAGGVMHEGYVSTMLGLKGIPASAEEVMVARDILLAEETGSRVHIAHVSTAGSVRLIREAKARGVRVTAEVAPHHFTLTDEAVLGYDTSTKVNPPLRSAGDVAAVREGLADGTIDVIATDHAPHTEEEKDVEYDLAPFGMVGLETAVGLVWTELVAAGVLTPLQAVVKMTLNPARVLGIPKGTLEPGADADITIIDPDLSEPVDPARFASKGRNTPFRGRLLKGLPWATIVGGRVVMQDRVIR | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate.
Catalytic Activity: (S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate
Sequence Mass (Da): 44760
Sequence Length: 427
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3.
EC: 3.5.2.3
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A8MIU4 | MTRRNMGVHIAGIQLKNPVMTASGTFGSGREYSEFVDLNQLGAVVVKGVANEPWSGNPTPRIAETYGGMLNSVGLQNPGVEAFIKDDIQFLRQYDTKIIVNIAGRTVADYCKVTEKLGDADIDLIELNISCPNVKAGGVNFGTNPAMVEEVTKAVKKVARQPLIVKLTPNVTDIVEIAKAAVAGGADAISLINTLLGMAIDIHGRKPILANVVGGLSGPAIKPVALRMVYQVANAVQVPIIGMGGIATGEDAIAFMLAGATGVAVGTANFMNPRATMEVLEGIEDYMDQYNIEDIHEIIGKL | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the conversion of dihydroorotate to orotate with NAD(+) as electron acceptor.
Catalytic Activity: (S)-dihydroorotate + NAD(+) = H(+) + NADH + orotate
Sequence Mass (Da): 31887
Sequence Length: 302
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (NAD(+) route): step 1/1.
Subcellular Location: Cytoplasm
EC: 1.3.1.14
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O29513 | MNPLETEIGGLRMKNPLMLASGIMGSKVHSLNLIARDAGAVVTKSVGVEEREGYRNPTVVNWKCGLINAVGLASPAAKDFAEELKDYTNEAPLLISLYGHSVEEFSDLVDTFDSALPYLHGYELNLSCPHVKGAGLDIGMDLELSAAIVEELKGKTKNPVFAKLSAMHDYLKLAKVLEDAGVDGITISNTLRGMKIDIMSGKPVLSNLSGGVSGPAIKPIALKCVYDLYKEIEVPIVGCGGITSFEDVLEFIMAGARAVQIGSAVYYSRRIFYSLKESLIAFTRARDCTISDLIGIAHS | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the conversion of dihydroorotate to orotate with NAD(+) as electron acceptor.
Catalytic Activity: (S)-dihydroorotate + NAD(+) = H(+) + NADH + orotate
Sequence Mass (Da): 32114
Sequence Length: 299
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (NAD(+) route): step 1/1.
Subcellular Location: Cytoplasm
EC: 1.3.1.14
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B6YRL9 | MADLNINIGKLKFKNPVLAASGTFGYGIEYSDFVDLSKIGGIFTKGITLYHREGNDYPRMAETSSGMLNAVGLQNRGVTYFIKNIYPKVKNIETNIMVNISGSTIEDCVSCAEKINELDKIPAIELNISCPNMKQGGMAFGTNCSNASEIVNAVRKVYHKILIVKLSPNVTDITEIAKAVEIAGADAVSLINTLIGMAIDIKIKKPILSTVTGGLSGPCIKPIALRMVYQTYKIVKIPIIGLGGISNSDDAIEFILAGASAIQVGTYNFIDPTISTKIVDGINAYLDKYHLLSIKELVGELL | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the conversion of dihydroorotate to orotate with NAD(+) as electron acceptor.
Catalytic Activity: (S)-dihydroorotate + NAD(+) = H(+) + NADH + orotate
Sequence Mass (Da): 32512
Sequence Length: 302
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (NAD(+) route): step 1/1.
Subcellular Location: Cytoplasm
EC: 1.3.1.14
|
P57443 | MFYYFIRKLLFLLEPEKAHFLTLKYLNIKNIQFFDFFFYKTIILSKKIKCMGLIFDNKLGTAAGIDKNGEYIDALSKLGFGFIEVGTVTPLPQVGNPKPRMFRIVSMEGIINRMGFNNLGIDNLIRNIKKSNFKGIIGVNIGKNKSTSLENSVDDYLICIEKIYCYAGYIAINISSPNTTNLRNLQYGILFKKLLYKIKKKQKELHKKYLKYVPIAIKISPDLSIKELVDISKQLIRYKIDAVIATNTTLDHSSLFGLKNSSEQGGLSGLPLQKKSTNTISILSKSLQKKIPIIGVGGINSINSAKEKIESGATLIQIYSGLVYHGPKLIKKIINHI | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.
Catalytic Activity: (S)-dihydroorotate + a quinone = a quinol + orotate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 37955
Sequence Length: 337
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (quinone route): step 1/1.
Subcellular Location: Cell membrane
EC: 1.3.5.2
|
Q92S77 | MIGQLEHLARRGLFLFDPEAAHGLSIKALKSGLVPSCAAPADPRLGQTVAGLVFSNPIGMAAGYDKNAEVPEALLKIGFGFTEIGTVTPRPQAGNDKPRLFRLVEDEAVINRLGFNNEGHGAALARLKACSREALIGVNIGANKDSADRIADYVTGIRTFYAVARYFTANISSPNTPGLRDLQARESLSALLSAVLAARDDEARKGGRQVPVFLKIAPDLTEEGMDDIAAEVLAHGLDGLIVSNTTLSREGLKDRRQANEAGGLSGKPLFEKSTAVLARMRKRVGPHLPIIGVGGVCSAETAAEKIRAGADLVQLYSCMIYEGPGLPGRIVRGLSALCEREKLASIRDIRDSRLDYWSGRNV | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.
Catalytic Activity: (S)-dihydroorotate + a quinone = a quinol + orotate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 38635
Sequence Length: 362
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (quinone route): step 1/1.
Subcellular Location: Cell membrane
EC: 1.3.5.2
|
Q07TQ6 | MIRAFDALSLPLLRLLDPEDAHRLAIQGLRLLPQAAPPADQPNLSVRAFGLNFSNPVGIAAGFDKNAEAPDALLRMGFGFVEIGTVTPKPQSGNPRPRLFRLERDEAVINRMGFNNDGGEVVLRRLAARSARGGIVGVNVGANKDSEDRVADYVRLIEMFAPVASYFTVNVSSPNTPGLRNLQQAAALDDLLAKVIEARERVRAIAGDTPVLLKIAPDLTLNELDDVVHIARSRKVDGMIVANTTLSRTHTLREQARAKEQGGLSGRPLFRLSTRMVAETYVRAEGAFPLIGVGGIDSGGAALTKIRAGASLIQLYSALIYKGLGLVESIKQDLASTLLRTGRDQLSEIVGADAPMITAEDWPV | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.
Catalytic Activity: (S)-dihydroorotate + a quinone = a quinol + orotate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 39111
Sequence Length: 364
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (quinone route): step 1/1.
Subcellular Location: Cell membrane
EC: 1.3.5.2
|
Q2RX27 | MADWYRLAWPLICGLDPERAHHLAIRALALGLAGHDRAADDPVLACSLWGRRFANPLGLAAGFDKNGEVADALFDLGFGFVEVGTVTPRPQAGNPRPRLFRLTQDRAVINRMGFNNQGMEAMAARFVRARPRGVLGINLGKNKTTEDAAGDYEAGIAKLAPLADYLVINVSSPNTPGLRALQGREPLSLLIARARAALDAACPGLRPPLLLKVAPDLTDEDMADIAEVALGGGLDGLICTNTTIARPKSLVSDHAGETGGLSGLPLRYRARQVIARLYGLTKGALPLIGVGGIGDGAEAYARIRAGASLIQIYSALVYEGPGLVGRIKRDLAQRLRADGFASVAEAVGADHRDPKGASGKLAPRSPL | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.
Catalytic Activity: (S)-dihydroorotate + a quinone = a quinol + orotate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 38648
Sequence Length: 367
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (quinone route): step 1/1.
Subcellular Location: Cell membrane
EC: 1.3.5.2
|
A7NLW9 | MLYHLIRPLLFRLDAERAHDVVTAMFRATSRMPLLPRLISALYAWDDPALMVEWAGLRFASPLGVAAGFDKRADLVDALALLGFSHVEVGTVTPRPQPGNPGPRLFRLPEDMALINRLGFNSHGMVAVAKALRARRSRRVIVGVNIGKNRDTPLERAVEDYAATFVALAPLADYVAVNISSPNTPGLRRLHERAALEELLRELMRLNHGLLYPRPIALKISPDETLDQIEEVVRAGCEAGVAAFIATNTTLAREGLRSRLANETGGLSGRPLAPRARQVIRAIYRLTRGTPPVIGVGGVLTADDAYAHIRAGARLVQLYTGMVYAGPAIAREIKRGLAQLLRRDGFVSVTQATGVDAEWEGAIRQRG | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.
Catalytic Activity: (S)-dihydroorotate + a quinone = a quinol + orotate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 40043
Sequence Length: 367
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (quinone route): step 1/1.
Subcellular Location: Cell membrane
EC: 1.3.5.2
|
A5UX75 | MTSLYALIRPLLFRLDAERAHDLTAKALRVTSRAPLLPRLIRALYAWEDPLLAVDWSGLHFANPVGVAAGFDKRADLVDGLALLGFGHIEVGTVTPRPQPGNPRPRLFRLPEDTALINRLGFNSPGMVAVARALRARRSRDVIVGVNIGKNRDTPLERAVEDYVATFVALAPIADYVAVNISSPNTPGLRRLHERAALETLLHELTRLNRALPHPRPIALKVSPDETPDQLEAVVRAGCDAGIAAFIATNTTLARDDLHSRLAIETGGLSGRPLTQRARQVIGAIYRLTHGAPPVIGVGGIATAEDAYQHIRAGARLIQIYTGMVYAGPAIARDIKQGLARRLRRDGFTSLEEAVGVMVAA | Cofactor: Binds 1 FMN per subunit.
Function: Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.
Catalytic Activity: (S)-dihydroorotate + a quinone = a quinol + orotate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 39052
Sequence Length: 361
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (quinone route): step 1/1.
Subcellular Location: Cell membrane
EC: 1.3.5.2
|
Q7WEU9 | MSASASTAADFVRFALDEGVLRFGSFKVKSGRISPYFFNAGLFNSGRSVGALAGFYAQALVDSGVAFDMLFGPAYKGIPLATATSVALAGHRAMAGRDVPFAFNRKEAKDHGEGGTLVGAPLTGKVVIIDDVITAGTSVRESVEIIRAAGAEPAAVLIALDRMERAGPDDALSPHSAVQDVARTYGIPVVSIASLADIMTLLQDDAQFAEHREAVQAYRSKYGV | Function: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP).
Catalytic Activity: diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate
Sequence Mass (Da): 23428
Sequence Length: 224
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2.
EC: 2.4.2.10
|
Q89BL4 | MSKSASRARLFEIIRRRSFGRGEVTLASGRKSDFYFNLKPTMLDPEGATLLAELTYEALKDDNLDFIGGLEMGAVPLAGALAQISWIKGHPIAAFFVRKKPKEHGAKLAIEGLPRGETLQGKRVVIVEDVTTTGGSAMKAVESVRETGAEVVLVLTMVDREEGATDTFGAAGLPFRSLYKASEFLKA | Function: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP).
Catalytic Activity: diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate
Sequence Mass (Da): 20219
Sequence Length: 187
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2.
EC: 2.4.2.10
|
Q8Y342 | MSQNSELRQSFIRFAVEAGVLSFGEFVTKAGRTSPYFFNAGKFSDGALLGQVAQFYAKTLLDSGVQFDMLFGPAYKGITLASATAVALAGMGRNVGFAYNRKEAKDHGEGGSLVGAKLQGRVVIVDDVISAGTSVRESVELIRNAGATPAAVLILMDRMERSGNAVDIGERSAVQDVQAQYGMPVVSIANLDDLLGYLDHAGDPALAGYRAKAAAYRDKYGVSAVV | Function: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP).
Catalytic Activity: diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate
Sequence Mass (Da): 23827
Sequence Length: 226
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2.
EC: 2.4.2.10
|
P42719 | MIQTTFPDRAVMAELLAKMLWEIKAVHFNAAQPYKLASGMASPVYIDCRKLLSFPRIRSTVMDFAASTLLRDAGFEQFDCIAGGETAGIPFAALLADRLGLPMIYVRKQPKGHGRNAQIEGNMPEGSRVLVIEDLTTAGGSMFKFIDAVRAAGGIVDHGIALFFYGIFGEQRFADGKVRLHHIATWRNVLPSPGSRSSSTTRRCRKSSPSSMRRWLGRERMVA | Function: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP).
Catalytic Activity: diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate
Sequence Mass (Da): 24623
Sequence Length: 223
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2.
EC: 2.4.2.10
|
Q92SC6 | MFSNAFTDKAVMAELVAKMLWEIKAVHFRADEPYRLASGMASPVYIDCRKLVSYPRIRSAVMDFAAATILREAGFEQFDVVAGGETAGIPFAAMLAERLGLPMIYVRKAPKGHGRNAQIEGYMPEGARVLVIEDLTTAGGSMFKFIDAIRAAGGVVEHGIALFYYDIFPEARGNMKSKGVDLHYIATWRNVLAVARELALFDEKTLNEVEAFLNAPLDWSGRNGGVRALAVQ | Function: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP).
Catalytic Activity: diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate
Sequence Mass (Da): 25466
Sequence Length: 232
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2.
EC: 2.4.2.10
|
A5VD53 | MTDEQVLAEFRAAEALLEGHFILSSGLRSSRYLQCARVLMNPARAARLAEALAFKIPDKLKIQLGSVVSPAMGGVIAGHEMGRALGLDAMFVERPDGVFHLRRGFRLEPGQKVLLMEDVVTTGLSSREAIKAVEEAGGQVIAAAALVDRSNGTADLGVPFYPLIRLDVPTYQPESLPPELAAIPAVKPGSRAAVAA | Function: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP).
Catalytic Activity: diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate
Sequence Mass (Da): 20811
Sequence Length: 196
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2.
EC: 2.4.2.10
|
Q7UYX5 | MSSDSANRDLAPLIALMETEALQRGEFTLASGKKANYYLDCRRVTLHPKGACLIGRAMLDVVLANAKESGVMPAAVGGMAIGADPITASIVTLAGGDDVDLKGFMVRKEPKGHGMGQQVEGPVTPGQKVVIVEDVITSGGSALKAVEAVQAFGLEVQYVLAIIDRLAGGAEAFAQKGLELKTLTTIRDFGLEP | Function: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP).
Catalytic Activity: diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate
Sequence Mass (Da): 20109
Sequence Length: 193
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2.
EC: 2.4.2.10
|
Q757S1 | MSTKSYAERAKAHNSPVARKLLALMHEKKTNLCASLDVRTSRKLLELADTLGPHICLLKTHVDILTDFDIETTVKPLQQLAAKHNFMIFEDRKFADIGNTVKLQYSSGVYRIAEWADITNAHGVTGPGVIAGLKEAAKLASQEPRGLLMLAELSSQGSLARGDYTAGVVEMAKLDKDFVIGFIAQRDMGGRADGFDWLIMTPGVGLDDKGDGLGQQYRTVDEVVSDGTDVIIVGRGLFDKGRDPNVEGARYRKAGWEAYLRRIGETS | Catalytic Activity: H(+) + orotidine 5'-phosphate = CO2 + UMP
Sequence Mass (Da): 29210
Sequence Length: 267
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
EC: 4.1.1.23
|
O13410 | MSSKSQLTYGARASKHPNPLAKRLFEIAEAKKTNVTVSADVTTTRELLDLADRLGPYIAVIKTHIDILTDFSVDTINGLNVLAQKHNFLIFEDRKFIDIGNTVQKQYHGGALRISEWAHIINCSVLPGEGIVEALAQTASAQDFPYGPERGLLVLAEMTSKGSLATGEYTKASVDYARKYKNFVMGFVSTRALTEVQSDVSSASEDEDFVVFTTGVNLSSKGDKLGQQYQTPASAIGRGADFIIAGRGIYAAPDPVEAAQRYQKEGWEAYMARVCGKS | Catalytic Activity: H(+) + orotidine 5'-phosphate = CO2 + UMP
Sequence Mass (Da): 30267
Sequence Length: 278
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
EC: 4.1.1.23
|
P07817 | MSSKSQLTYTARASKHPNALAKRLFEIAEAKKTNVTVSADVTTTKELLDLADRLGPYIAVIKTHIDILSDFSDETIEGLKALAQKHNFLIFEDRKFIDIGNTVQKQYHRGTLRISEWAHIINCSILPGEGIVEALAQTASAPDFSYGPERGLLILAEMTSKGSLATGQYTTSSVDYARKYKNFVMGFVSTRSLGEVQSEVSSPSDEEDFVVFTTGVNISSKGDKLGQQYQTPASAIGRGADFIIAGRGIYAAPDPVQAAQQYQKEGWEAYLARVGGN | Catalytic Activity: H(+) + orotidine 5'-phosphate = CO2 + UMP
Sequence Mass (Da): 30196
Sequence Length: 277
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
EC: 4.1.1.23
|
Q9P8X9 | MSRHATITQSYQERASLPKTSPVASYLLRLIAAKKTNLCVSADVSTTRELLQLAEEVGDSICMLKTHADIINDFGPRTIEGLKEIAAKKHFLVFEDRKFGDIGSTVQKQFTAGPLQIVRWANIINAHIFPGPAIITALSQARPRCRQLLILAEMSSAGNLMTGSYTEQCVVEARKNPEFVMGFIAQRTLNEQPGDNFITMTPGVQIGATGDGLGQQYNTPEKVIGEAGTDIIIVGRGVYGAQDKRAKAEEYRVRAWKAYEGNWRCYCNKR | Catalytic Activity: H(+) + orotidine 5'-phosphate = CO2 + UMP
Sequence Mass (Da): 29840
Sequence Length: 270
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
EC: 4.1.1.23
|
Q39VY5 | MTRDQAREKVIFALDTGEFAHVQYWAETLSDKVGMYKIGKQLFTACGPAAVRMIQKFGGEVFLDLKFHDIPNTVAMASVEAARMGVKLFNLHALGGYEMMAKTVEALDKEFKGGDRAKVLAVTILTSSTEETLKDLGIEHTVPDMVVRLATLARKAGIDGVVASPREIPLIREACGSDFLIVTPGVRPSFAALNDQKRVMTPAEAVKAGSDYLVIGRPIGDAPDPAAAAELILGEIVAG | Function: Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP).
Catalytic Activity: H(+) + orotidine 5'-phosphate = CO2 + UMP
Sequence Mass (Da): 25631
Sequence Length: 239
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
EC: 4.1.1.23
|
Q74D58 | MTRDQAREKVIFALDSSEFAHVQYWAETLSDRVGMFKVGKQLFTACGPATVRMIQKFGGEVFLDLKFHDIPNTVAMASLEAARLGVKLFNLHALGGYEMMARTVEALDKEFKGGERAKVLAVTILTSSTEETLRQVGIESPVEEMVVRLATLARKAGIDGVVASPREIPLIREACGPDFLIVTPGVRPAFAALNDQKRVMTPAEAVRAGGDYLVIGRPIGDAPDPAGAAEMILDEIMAG | Function: Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP).
Catalytic Activity: H(+) + orotidine 5'-phosphate = CO2 + UMP
Sequence Mass (Da): 25818
Sequence Length: 239
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
EC: 4.1.1.23
|
A5G5A2 | MTRDEARAKVIFALDVHEFSDVEQWADMLAPHVGMFKVGKQLFTSCGPAAVRMIQKCGGEVFLDLKYHDIPNTVAMASLEAARMGVKLFNLHALGGYEMMAKTVETLDKEFKGGERGKVLAVTILTSSNEQTLQDVGINIPVPEMVVKLALLARKAGIDGVVASPQEVPLIRKACGKDFLIVTPGVRPAFASSDDQKRIMTPAEAVRTGADYLVIGRPIAAAPKPVEAAEAIIDEIMAVEG | Function: Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP).
Catalytic Activity: H(+) + orotidine 5'-phosphate = CO2 + UMP
Sequence Mass (Da): 25932
Sequence Length: 241
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
EC: 4.1.1.23
|
Q7NK22 | MGGAERVIVALDLADAQAARALVERAPAVRFWKVGLELFTAAGPGLIEWLKARGCRVFLDLKFHDIPNTVAGACRAATRLGVDLLTVHATGGQPMLMAAVSACTGEAARLGSPAPAVLAVTLLTSLDAQLLEQQLLVNVGVSGYVEHLAVLAVSSGVQGVVCSPLETALLRERCGNDFLIVTPGIRPGGSGEGDQRRTLTPGEAFARGADYLVVGRPVTTAPDPQVAFKAIVAEVGG | Function: Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP).
Catalytic Activity: H(+) + orotidine 5'-phosphate = CO2 + UMP
Sequence Mass (Da): 24470
Sequence Length: 237
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
EC: 4.1.1.23
|
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