ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
B2FKL1 | MSDILQTILARKAEEVAQRRAQRPLEELQAAVASAPPVRGFVRALQAAVANGDPAVIAEVKKASPSKGVIRPDFRPADIAVSYEFGGASCLSVLTDVDFFQGADAYLQQAREACTLPVLRKDFVIDAYQVYEARVLGADCILLIVAALDDTQLATLSELALSLGMDVLVEVHDIDELERALQVPAPMIGINNRNLRTFEVSLQTTLDMQQAVPRDRLLVTESGILGLQDVALMRDAGIHAFLVGEAFMRVEEPGEGLRQLFFAA | Catalytic Activity: 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate + H(+) = (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
Sequence Mass (Da): 28659
Sequence Length: 264
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 4/5.
EC: 4.1.1.48
|
Q4JWC7 | MSPTTPRSVEPSGLKPEQLPPSYFTWPGLLGRLGNGQELSEAQVRWAMNEIMEGNATDAQIAAFAFGIRVRGITAAELAAAAETMTSFATPVDFSDVPNCVDIVGTGGDGHHTVNISTMASFVVSAAGVPVVKHGNRAASSKCGGADMLEALGLDIERSPEDIRQDAHDTGFAFMFAKTYHPAMRFAGPVRSQLGAPTIFNLLGPMTNPAYPKFGLIGCAFKEFMPIMGGAFARQGSRVLVVRGMDGMDEISVCTPTEVVTVDAAGRTGEEVINPRNVGLDFYEDGSLVGGDAEYNADVAVRLMKGEISGAIKDAVLINA... | Cofactor: Binds 2 magnesium ions per monomer.
Function: Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
Catalytic Activity: diphosphate + N-(5-phospho-beta-D-ribosyl)anthranilate = 5-phospho-alpha-D-ribose... |
Q3Z6G6 | MIKEAIGSLVLGKSLTLEQSASVMDEIMEGKTTPAQIGAFLTALRVKGETAEEIAGLANVMRAKSTRISTSTPVLDIVGIGGDGINTFNISTTAAFVISGAGIKVAKHGNRAASSMCGSADVLEALGIKIDLNAEQVKICIEQIGIGFMFAPVFHPAMKFVAPSRREIGIRTVFNILGPLTNPASAQYQLIGVPEIGLGDKIISALCHMDIKHALVVHGLDGMDEMSISGDSVIWELKDKEIIKFRHTVSPREMGLEQVSLQAVKGGAAEENALTLRAILSGAKGPKRDVVLLNAAAALMVADKIDTIAEGISLAAEIID... | Cofactor: Binds 2 magnesium ions per monomer.
Function: Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
Catalytic Activity: diphosphate + N-(5-phospho-beta-D-ribosyl)anthranilate = 5-phospho-alpha-D-ribose... |
Q9RTJ5 | MQAQPIHARLMNGEVLSQDDATAFMREVMSGDMSGVRMAAALAALRVRGETPEEIAGFAQAMRESAVTVKVRPRDVLMDVVGTGGDGAHTFNISTTTAFVLAGAGVPIAKHGNRAASSRAGSADVLEALGVNLDASPEVIQEAIDTLGVGFMFARNYHPALRHAAPVRSDLAARTVFNILGPLSNPAGATHLVVGVFRADLTRTLAEALRHLGAKGATVVYGDGLDEFTVCGPNTVSGLRDGEIIDRTMHPEEFGVDLHPKTAIVGGSPAENAEITHALLTGGGTPAQKDIVALNAGAALRTAGRVGTIREGVEQAREVM... | Cofactor: Binds 2 magnesium ions per monomer.
Function: Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
Catalytic Activity: diphosphate + N-(5-phospho-beta-D-ribosyl)anthranilate = 5-phospho-alpha-D-ribose... |
B1I3Z8 | MIREALQKLVGGEDLEQHEAEAVMAEIMDGEATSAQIGALLAGLRLKKETAAEIRGFARAMRARAEQVPTRHELVADTCGTGGDGAQTFNISTTAAFVVAGAGVPVAKHGNTAVSSRCGSADVLRHLGVNLDLTPAQMGACLDEVGIAFLFAPRLHRAMQHAAGPRKELGIRTVFNILGPLTNPVRPRVQVLGVFDAAVAELVADALAGLEVERAFVIHGAGRLDEVSLAGPAQVWEVRPGSVRAGILDPVDLGFERADVESLSGGSPADNARITLEILHGASGPRRDAVLLNAGLALLAAGRAGDAAGAVRLAAESLDS... | Cofactor: Binds 2 magnesium ions per monomer.
Function: Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
Catalytic Activity: diphosphate + N-(5-phospho-beta-D-ribosyl)anthranilate = 5-phospho-alpha-D-ribose... |
Q24SK4 | MTYAIHESLTLLSQKQDLPEELTFTVVQDLLSGELTPAQIGGLLLGLSLKGETPEEIAAFAQALRGAGLKIKAPAGTLDTCGTGGDRSGTFNISTTAAFVIAGAGVPVAKHGNRFASGRCGSADVLEQLGISLKATPESSERHLQHIGMTFLFAQVYHPAMAKVAAERRELGIRTIFNLLGPLLNPAGAPYQLLGVSSPSLLPKMAKALQILGSKRAVVAVGEDGLDEVTLTGATQAILIDGGEIQPFIIRPEEYGLNLCSLQDLQGGTPAENGQITLRILQGKKGPQRDIVLLNAGTALYAANKAAGIREGIALAAESL... | Cofactor: Binds 2 magnesium ions per monomer.
Function: Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
Catalytic Activity: diphosphate + N-(5-phospho-beta-D-ribosyl)anthranilate = 5-phospho-alpha-D-ribose... |
A8ZZX1 | MFSQTLSKIINRKDLSREEMDRIFSDIFSGNLTDAQIGAFMAALATKGETFEELAGAAEAMRRKATRIQAASPVVVDTCGTGGDGAHTFNISTTSAFVVAGAGICVAKHGNRSVSSKCGSADVLEALGVKLDTQPEVAEEAVNEIGIGFLFAPLFHGAMKYAIVPRKELGVRTIFNMLGPLTNPAAANCQVLGVFAPQLTEMFADALNLLGARRAFVVHGHDGLDEISVCASTRVSELNDGRVQTYDISPEHFFEDRARPEDMAGGTPSENAQITRHILSGKEKGPRRNVVVVNAGAALVAAGKAEDLKAGVALAGQIID... | Cofactor: Binds 2 magnesium ions per monomer.
Function: Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
Catalytic Activity: diphosphate + N-(5-phospho-beta-D-ribosyl)anthranilate = 5-phospho-alpha-D-ribose... |
Q6AMS5 | MAVTLGKNNMNIRQAIARVVTGADLSESEMMASMEEVMSGQASPAQIASFITALRMKGEAVEEIVGAVRVMRDKATFIDCGLGPDDILMDIVGTGGDGADTFNVSTTTSFVVAAAGVAVAKHGNRAVSSRCGSADVLEALGVDLSLDPATVARSVQEIGIGFLFAPLLHAAMKHAIVPRREMGIRTIFNILGPLTNPAGANVQLIGVFERSLTTVLAEVLLRLGERRSLVVWGEGNMDEMTVTGTSYIADAHDGRVTSYAVEPEDVGLARAAVADISGGRTPEESAQQVRAVLAGEKGARLDMVLLNAGAALLAAGRVET... | Cofactor: Binds 2 magnesium ions per monomer.
Function: Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
Catalytic Activity: diphosphate + N-(5-phospho-beta-D-ribosyl)anthranilate = 5-phospho-alpha-D-ribose... |
P12320 | MQATLIKPTIFTHQPILEKLFKSQSMTQEESXQLFAAIV | Function: Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
Catalytic Activity: diphosphate + N-(5-phospho-beta-D-ribosyl)anthranilate = 5-phospho-alpha-D-ribose 1-diphosphate + anthranilate
Sequence Mass (D... |
A1ALX3 | MIKKAIARIVEQKDLTEGEMIEVMGQIMTGEATPAQIGAFITALRMKGETIDEITGAARVMREHATRIRAGKDLLDIDRDDINIDRETILDVVGTGGDGTNTFNVSTTVAFVVSACGVKVAKHGNRSVSSLCGSADVLEKLGVNLDITPETVEQCITKIGIGFLFAPALHGAMRYAIGPRREIGIRTIFNILGPLTNPAGADCQVMGVYRPGLVEKLAGVLHRLGCRHGFVVHGMDGMDEITTTTETLIAEVTTSGVSICTIHPEELGFSRCSMDELRGGDATANADIVRSVLQGVAGPRRDIVLINAAYALVAADRAAT... | Cofactor: Binds 2 magnesium ions per monomer.
Function: Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
Catalytic Activity: diphosphate + N-(5-phospho-beta-D-ribosyl)anthranilate = 5-phospho-alpha-D-ribose... |
A5D1S5 | MIKNAIKKVVSGQHLSEEEAGAVMEQIMEGGASPAQIASLLTAMRLKGETVDEITGFARVMRQKSTRVKSKHPVLVDTCGTGGDGAGTFNISTAAAFVVAGAGVPVAKHGNRSVSSRCGSADVLEELGVRVDLDREAVEECLNMVGMAFLFAPLLHRSMGYVAGPRREIGIRTVFNILGPLTNPAGANAQVLGVYSPFLAEMLAKVLARLGVSRAFVVHGAGGLDEISLAGPSILCEVRNGSVRRGLLDPARFGFRYAPVSVLAGGTPRENAAIALKILEGERGARRDVVVLNAALGLVAGGKARNIAEGLEIAALSIDS... | Cofactor: Binds 2 magnesium ions per monomer.
Function: Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
Catalytic Activity: diphosphate + N-(5-phospho-beta-D-ribosyl)anthranilate = 5-phospho-alpha-D-ribose... |
Q4FM53 | MRVFIDKLKDKQDLSFAESKNAFEILMNGKASDDEIFDFLTLLSSKGESSDEIAGGVFVLRDKSKRVNVDDCIDTCGTGGDGMNTLNISTASALLLSSMGIKVAKHGNKAVSSKCGSGDVLEALNIKIDLEPKDIEEQIKKNNFGFMFAPNYHSAMRFVGPTRKKIGKRTIFNMIGPLSSPALVDRQVIGVFDKKLLKIFANALNNLDIKFAWIVNSEDGLDEISPYSKTNVVQLKDGKISEMLIDPIKLNIGANKFENLLGDDAKFNANKMLDIFKGEDNDFSKAVCLNAAAGLIVSEKYTIFIDAYNEARTHILSGKT... | Cofactor: Binds 2 magnesium ions per monomer.
Function: Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
Catalytic Activity: diphosphate + N-(5-phospho-beta-D-ribosyl)anthranilate = 5-phospho-alpha-D-ribose... |
C0QR68 | MIKEYIRKITEGKDLSADEMKDLFNILMEGQATDAQIGAVLIGLKMKGESVEEISSAAQIMREKAVKVPVKDRSRLIDTCGTGGDKVDTFNVSTITAFVIAGAGVKVAKHGNRSVSSKCGSADIMEALGVKIDLSPEQAAEAIDRIGLGFLFAPVYHPAMKNVIRQRREIGVRTIFNILGPLSNPAGAKYQLLGVYDKDLVEPVARVLSLLGIERAYVVHGMEGLDEVSITTDTMVAEVDGGDISVYSVKPEDFGIERASLDDIRGGDLDFNLQIALDILEGKDRSRKTDFVSLNAGFAFHAVGVVDSVKEGIELAKETI... | Cofactor: Binds 2 magnesium ions per monomer.
Function: Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
Catalytic Activity: diphosphate + N-(5-phospho-beta-D-ribosyl)anthranilate = 5-phospho-alpha-D-ribose... |
A9BHQ6 | MFNYYLQKVVKGENLSLDEMEQAMEMIMEGKVTHSQLSGFLVALHMKGETVEEITASAKVMKEKATPISIESGELMDTCGTGGDAKGTFNISTAVAFILAAAGVVVAKHGNRSVSSKSGSADVLESLGINISLPPSSVERCLKEINIAFLFAQDFHKATKHAAVPRKELGIRTIFNVLGPLTNPANIKYQLMGIYDPKLVYPIAEVLNNLGVKRAMVVHGSEGIDEFSLSGKNKVAFLNEGKIEKLEISPEDLGLEKYSIQEIQGGSAEENKRIILNIFNGEMGPKRDVVVLNTAAGLYVANKVNSLEEGINFAQEIIDS... | Cofactor: Binds 2 magnesium ions per monomer.
Function: Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
Catalytic Activity: diphosphate + N-(5-phospho-beta-D-ribosyl)anthranilate = 5-phospho-alpha-D-ribose... |
Q7N488 | MQAIFNKLFNAQTLTQQESQQLFAAIIQGELSEPQLAAVLISMKLRGEQPQEIAGAAQALLANALPFPRPDYTFCDIVGTGGDGANSINISTASAFVASACQIKIAKHGNRSVSSQSGSSDLLAAFGIALDISAECARSALDEIGICFLFAPHYHLGFCHAMPVRQQLKTRTIFNILGPLINPARPPLALIGVYSPELVEPIARTLLVLGYQRAAVVHSGGMDEVALHAPTKVAEINDGEIIHYQLNAEDFGLQRHPMSALKGGSPVDNHEMLSLLLQGRGKKAHADAVAANVALLMKIHGQEDLRHNTQQALETIHSGR... | Cofactor: Binds 2 magnesium ions per monomer.
Function: Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
Catalytic Activity: diphosphate + N-(5-phospho-beta-D-ribosyl)anthranilate = 5-phospho-alpha-D-ribose... |
Q5V448 | MQSVETDRTTFTDLAADAHPAARVPVEVRVDVDDPFLAYRRARDETGGVYLATTGGQSGWGYFGTAPADFREVDPRAGGTLAALTEFLDGERLVRGDCDVPYPCGAVGWLSYDVARELESLPDSADADRALPNLQVARYDRFAAWEEPRGESVTLRVTACPRVDDFETPELAYEFGKQHALDLARAAAQGDPSVEDPPVETDEATFESDCTRESFADRVQTVKQYIRDGDTFQANVSQRLRAPAAVHPVEAFDALRTVNPAPYSALLEFPGVDLVSASPELLLHRDGDRIETEPIAGTRPRGETPDADDRLETDLLDDEK... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Catalytic Activity: chorismate + L-glutamine = anthranilate + H(+) + L-glutamate + pyruvate
Sequence Mass (Da): 53790
Sequence Length: 489
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 1/5.
EC: 4.1.3.27
|
Q5V213 | MTLDISREEFVEHAKADRPVVVRTAAELDVDVEPLTAYAALTGRTSDVAANDYTFLLESAEKVASSDPDGAFAPETDDRHARFSFVGYDPRAVVTVTGDESEVEAFDDRYADLVTTDGGDVVDDLRAAMPDVALRNFPAMDRQHLEGGLVGFLSYDAVYDLWLDEVGLDRPDSRFPDAQFVLTTSTVRFDHVEDTVSLVFTPVVRQGEDAGERYGELVAEAERVEAVLSDLSPLSTGGFRREDEVAGPRDEYEDAVERAKEYVLSGDIYQGVISRTRELYGDVDPLGFYEALRAVNPSPYMYLLGYDDLTIVGASPETLV... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Catalytic Activity: chorismate + L-glutamine = anthranilate + H(+) + L-glutamate + pyruvate
Sequence Mass (Da): 58526
Sequence Length: 536
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 1/5.
EC: 4.1.3.27
|
Q5V631 | MTEIRFSTDKESFIETARAAADGTRVPVEARVTVADPFEAYRRARDENTDGFYLETTGGQSGWGYFGIEPIERVEVSAGATPAQDGGSPSLEAIDDLLDREHLERGDCTVPYPCGAFGWLSYDVARELEDIPETTVSDGLPRLQFGVFDCIAAWEEPHDGNVEIHVTACPTVDGSPESAFERGRTMARELAQDAIHGEKHVQSQPTAASQATFESECGEAAFADRVRQIKQYVRDGDTFQTNVSHRLTAPAAVHPVDTFDAVRRVNPAPYSALLEFPGVDLVSASPELLLDVDGDQLLTEPIAGTRPRGATPSEDEDLEV... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Catalytic Activity: chorismate + L-glutamine = anthranilate + H(+) + L-glutamate + pyruvate
Sequence Mass (Da): 55112
Sequence Length: 503
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 1/5.
EC: 4.1.3.27
|
P14953 | MFYPTLDEVKIMAKDYNIIPVTMEVYADMETPISLFKRFEESSCCFLLESVEGGEKWARYSIIGKNPFLVVESYKNKTIIRERNGSQREVEGNPVEIIKGIMGKFKGANLPNLPRFNGGAVGYFGYDLIRHYENLPNVPEDDMGLPECHFMFTDEVLVYDHLKQKIHIIVNLHVNGNIERAYISAVDRIKTIHREILDTRWKTADNSVLSYNKKKNELAVTSNISKEDFCRNVLKAKQYIRDGDIFQVVLSQRLCVETNENPFNIYRALRVINPSPYMYYLKFGGYRIIGSSPEMLVRVENGIVETCPIAGTRKRGRTKE... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotra... |
Q9Y8T0 | MPSPPEPPLHWRDCRLEPILGFPRPRELAKSLEVQGEEWIALLESGGGLQHRSRYSFLAWGRRKSSETDAIRAYEELERLADDKCRALPCRSPTFFLVSYEAVVGEEPWLSRLVGRHEWPGMTAFSPEYVVVYDHAGGRVSVCPGDTPLPAPASRKESFSAEGPTYETSRKGFEAMVADALERIRAGEAFQVVLSRVERYRVWGSLFSAYERLADANPSPYLYYARLGGRVIIGSSPELLVKLEAGRVETHPIAGTRPRGSTPIEDIELEVELLNDEKERAEHVMLVDLARNDITRVSIPGTVQVTSFMDIERYETVMHI... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotra... |
O66849 | MNLNLSLEEVRKLSENYNVIPLYTELLVDTETPLSIFLKLKEKGQFNILLESAEGGEKWGRYSFIITGSSFYLRTRKDIGEIYERGKVNFFETKDPLSKIKEVVKKFIPYHDERLPRFWGGLVGYFAYDVVKFYEPVEDKNPDPIHTYDIYLVLTDVVVIHDNLTGKIKVVVPIFAQNGIEEEYERAKNLIRDTVKKLKERGTTFLNVVEKEPDFKNWRSNFTKEEFEDIVKKAKEYIAQGDVIQVVLSQRFRKRFKGNPDNIYRVLRFLNPSPYMYYLDFDQLKVIGSSPEILVRLEEGRIETRPIAGTRKRGRTEEED... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotra... |
P32068 | MSSSMNVATMQALTFSRRLLPSVASRYLSSSSVTVTGYSGRSSAYAPSFRSIKCVSVSPEASIVSDTKKLADASKSTNLIPIYRCIFSDQLTPVLAYRCLVKEDDREAPSFLFESVEPGSQMSSVGRYSVVGAQPAMEIVAKENKVIVMDHNNETMTEEFVEDPMEIPRKISEKWNPDPQLVQDLPDAFCGGWVGFFSYDTVRYVEKRKLPFSKAPEDDRNLPDMHLGLYDDVVVFDHVEKKAYVIHWIRLDGSLPYEKAYSNGMQHLENLVAKLHDIEPPKLAAGNVNLQTRQFGPSLDNSNVTCEEYKEAVVKAKEHI... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit of anthranilate synthase (AS) provides the glutamine amidotransferas... |
O28669 | MQKHEYVNPVKLYSAIRDEKFPFILESAEKSGRARYTYISFNPLYTVRVGSRTRVDGEVISKISDPFDALNEIHVKGLLVGYVAYEAVKNYIGKKPQTPSVFGCYDGYFVYDHYLRKLFSVNVENADKIVERAKRVEVEQVRGNSEVLRAGSREKFEKMVERGKEQIFEGEVYQIVLSREYVVDTDLSPFQMYLNLRETNPSPYMFLLEFDRALIGSSPETMGRVEGNSFIINPIAGTARREAGREKEIAEKLLSDEKERAEHVMLVDLARNDVRKVCRAGSVRVSRFMEVVEYPSVLHIESEVVGELKAGVTHFDAMKA... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotra... |
P50872 | MYPADLLASPDLLEPLRFQTRGGVTVTRRATALDPRTALDPVIDALDRRRGLLLSSGVEAPGRYRRHALGFTDPAVALTARGRTLRIDALNGRGQVLLPAVAEALRGLEALAGLEEAPSRVTASSASPAPLPGEERSRQPSVFSVLRAVLDLFAAPDDPLLGLYGAFAYDLAFQFEPIRQRLERPDDQRDLLLYLPDRLVALDPIAGLARLVAYEFITAAGSTEGLECGGRDHPYRPDTNAEAGCDHAPGDYQRVVESAKAAFRRGDLFEVVPGQTFAEPCADAPSSVFRRLRAANPAPYEAFVNLGRGEFLVAASPEMY... | Catalytic Activity: chorismate + L-glutamine = anthranilate + H(+) + L-glutamate + pyruvate
Sequence Mass (Da): 78042
Sequence Length: 732
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 1/5.
EC: 4.1.3.27
|
Q81GG6 | MKICGITDVETAKSACEYGADALGFVFAESKREITPKRAEEIIQELPANVLKIGVFVNESVEVIQKIADECGLTHVQLHGDEDNYQIRRLNIPSIKSLGVTSESDMKNAQGYEADYILFDSPKEKFHGGNGKTFSWELLRDMPKELRKKMILAGGLNALNIEEAIRTVRPYMVDVSSGVETEGKKDVEKIKQFIIKAKECSK | Catalytic Activity: N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Sequence Mass (Da): 22556
Sequence Length: 202
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5.
EC: 5.3.1.24
|
A9VJW1 | MKVKICGITDVETAKHACEYGADAIGFVFAESKRKITPGLAKEIIGEIPVHVFKVGVFVNESVEVIQKIAEECGLTHVQLHGDEDNHQIRRLNIPSIKAVGVALEKDIECAKKYDTDYLLFDSPKEKFHGGNGKTFSWELLAHMPNELREKTILAGGLNILNIEEAIRTVQPYMIDVSSGVETEGKKDLKKIKQFIKKAKECSK | Catalytic Activity: N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Sequence Mass (Da): 22721
Sequence Length: 204
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5.
EC: 5.3.1.24
|
P20167 | MKKPALKYCGIRSLKDLQLAAESQADYLGFIFAESKRKVSPEDVKKWLNQVRVEKQVAGVFVNESIETMSRIAKSLKLDVIQLHGDEKPADAAALRKLTGCEIWKALHHQDNTTQEIARFKDNVDGFVIDSSVKGSRGGTGVAFSWECVPEYQQAAIGKRCFIAGGVNPDSITRLLKWQPEGIDLASGIEKNGQKDQNLMRLLEERMNRYVSISE | Catalytic Activity: N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Sequence Mass (Da): 24041
Sequence Length: 215
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5.
EC: 5.3.1.24
|
Q2KYM1 | MRTRVKICGLTREADIAQAIEAGVDAIGLICYAGSKRYVDLARAARLRREVPAFVSVVTLFVNPAPDEVRAVLDHVGPDLLQFHGDESPEDCTRYGHRFMRAFRVGAAGLDSAGAIAAACRPYHEAAGWLFDSYSSGYGGSGLTFDHSLLAEVQADAGSRPLVLAGGLNPDNIAQALALVQPWAVDVSSGVESGPGLKSADKMKEFLKRIKKVDDDLHA | Catalytic Activity: N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Sequence Mass (Da): 23380
Sequence Length: 219
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5.
EC: 5.3.1.24
|
Q7VY68 | MRTRVKICGLTREQDIASAVQAGADAIGFVFYPASKRHVDPARAAQLRREVPAFVDVVALFVNPRPDEVQAVLDHVAPDLLQFHGDETPQDCGRYGRRYLRAFRAGAPGLDSAAGLAAACRQYADAAGWLFDSYSAGYGGSGQGFDHGLLAGVQADPASCAIVLAGGLHPGNVADAVRAVRPWAVDVSSGVEDAPGIKSAGKIRQLMAAIKSVDQVAR | Catalytic Activity: N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Sequence Mass (Da): 22896
Sequence Length: 218
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5.
EC: 5.3.1.24
|
C0ZCE4 | MTRLKICGIKRTETLALLKELEVDYVGLVFAPSKRQVDAQTAGQLLAAVPGHPPAVGVFVNPTMEELEEVLSEAPLSVIQLHGQETPQFCQQVRERFALPVWKALAVGGEADAALAIQSYQGIVSAFLFDTYDPGQAGGTGKKFSWEQIPALQAACEAADCIIAGGIHAENVGELMGQYQAGIVDVSSGVETDGVKDAQKIKTLVERVKAHEQHSNNYASRA | Catalytic Activity: N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Sequence Mass (Da): 23758
Sequence Length: 222
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5.
EC: 5.3.1.24
|
A7HPD4 | MSVQVKICGLSTPETIEASVSAGADYLGFVFFSRSPRHLSYELAARLSGYVPASVPKVALTVDADDAMLDAVVEALRPDILQLHGDETPQRLVEIKARYGLTLMKAICVAQPEDPLTAAIYRDSADLLLFDAKPPKSMAGALPGGNGLVFDWSLIAGHRPETPWMLSGGLNAENVAEAVRITGAEAVDVSSGIEEGPGRKTPELIEAFIRAAKRA | Catalytic Activity: N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Sequence Mass (Da): 22858
Sequence Length: 215
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5.
EC: 5.3.1.24
|
A9BHQ4 | MIRIKVCGITNIEDAINISKAGVDALGFILAESPRKVELSKVLEISKELPPFVSRVAVVVNPVKEEIEKIERSKVFDYVQFHGSEDVNIIKNCKLKTIKAIKIENKSSLEEISKYNDFVDYFLFDTKIGEKIGGTGHTFNWEILKEANIKKPFILAGGLSPENIVEAIKTIRPNAVDLNSKVELYPGKKDIRLIKETIDRINSIKIK | Catalytic Activity: N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Sequence Mass (Da): 23311
Sequence Length: 207
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5.
EC: 5.3.1.24
|
A6L7N0 | MIIKVCGMREPENIRAIEQAGADWMGFIFFPQSARYVSHRPEYLPEQCHRIGVFVNESSENILLKAQEFGLHHIQLHGRETPEQCRKLKAAGLGVIKVFSIAQESDLQSAGCYEGVCDYFLFDTACSGYGGSGKTFNWNILQAYRGKTPFLLSGGLRPGSLSLLLQFKHEQWAGIDLNSGFETAPALKDDAAVHTFINQLKQKIQ | Catalytic Activity: N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Sequence Mass (Da): 22897
Sequence Length: 205
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5.
EC: 5.3.1.24
|
O13504 | MALVKICGLQSLEAAETAVNNGASLVGVIMVPGRERTVKQEVAREISQMVREKRISKGSKYLDSRQLRKEWDDCPLEDWFEYNVKEINSSGPFLVGVFRNQSIDEIQQAIHTHGLDFVQLHGSEDFDSYIRNIPVPVITRYTDNAVDGLTGEDLAINRALVLLDSEQGGEGKTIDWARAQKFGERRGKYLLAGGVTPDNVAHARSHTGCIGVDVSGGVETNASKDMDKITQFIRNAT | Catalytic Activity: N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Sequence Mass (Da): 26177
Sequence Length: 237
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5.
EC: 5.3.1.24
|
P70938 | MLIKYCGIRSKQDIALIEKSAATHIGFIFYPRSKRYVKPERVNEFVTDEIKKQVSLVGVFVNTPVDQILEIASVTNLDVIQCHGQETAADVRQLKQRGYEVWKALPHNKETLQQMHVYEEADGYVIDSKVKEQFGGTGVAFDWSFVPQYESAAQRLGKKCFIAGGINACNIENLLPYQPGAIDISGGIETNGTKDYTKIIEIERKIIL | Catalytic Activity: N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Sequence Mass (Da): 23399
Sequence Length: 208
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5.
EC: 5.3.1.24
|
B4S715 | MTRIKICGITTLEDALAAVEAGAHALGFNFSTTSPRAVTPQTARSIISAIPPFITTTGIFVEQSPDEINSICERCNLHCAQLHSEAYDAQSSLAVSAPSIIRVFRAGPSFHMDQVRSYAGKTGIRNFLFDAFREGQPGGTGESIEDTTAIRIFKETASIGSAILAGGLKPENVGRAIRLVSPYAVDTASGVESVPGRKDHDKIRAFVRAVQEADNDSSSPEA | Catalytic Activity: N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Sequence Mass (Da): 23597
Sequence Length: 222
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5.
EC: 5.3.1.24
|
Q59649 | MPAVRIKICGITRVEDALAAAAAGADAIGLVFYAKSPRAVDIHRAREIVRALPPFVTSVGLFVNASRCELGEILDAVPLDLLQFHGDERAEDCEGHRRPYLKALRMKPGDDIVGRAAAYPGAAGILLDTYVEGVPGGTGAAFDWSLVPTDLGKPLVLAGGLTPDNVGRAVEQVKPYAVDVSGGVEASKGIKDAARVRAFVDAVRSRRRDET | Catalytic Activity: N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Sequence Mass (Da): 22299
Sequence Length: 211
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5.
EC: 5.3.1.24
|
Q4KEZ9 | MPAVRSKICGITRIEDALAAVAAGADAIGLVFYAKSPRAVNVQQARAIIAALPPFVTSVGLFVNASRCELGEILDAVPLDLLQFHGDESAADCEGYHRPYIKALRVKAGDDIAAACLAYPRASGILLDTYVEGVPGGTGEAFDWSLVPQGLSKPIILAGGLTPDNVAAAIARVRPYAVDVSGGVEQGKGIKDPAKIQAFMQAVRRSNESM | Catalytic Activity: N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Sequence Mass (Da): 21917
Sequence Length: 210
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5.
EC: 5.3.1.24
|
Q8XLQ0 | MRNIKITLDYDGSKYKGWQKQNQKGSNVSTVQDKLEKVLTKMTSEEIQLIGCGRTDSGVHAKNYVANFKTNSLMTLEQIIEYINEYLPEDIRVTEIREASERFHARFNVKSKTYEYTIDNNKFKDVFLRKYAWHVEEKLDLEAMEEGAKYLLGTHDFKSFTSLKSKNKSTLRTINSIEFHENNNILSIKINGNGFLLNMVRIMVGTLVDVGLGKIEPKYINDILEAKERAKASEKAPAHGLCLLELNY | Function: Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
Catalytic Activity: uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA
Sequence Mass (Da): 28556
Sequence Length: 248
EC: 5.4.99.12
|
Q893H3 | MRNLKMILEYDGTRYKGWQKQKKDVLTIQDKIETVLSKMTGEDIQVIGCGRTDAGVHAENYVANFHTNCDFTVDYMLDYLYEFLPEDIVVKTMKDTSERFHARYNVKSKTYVYRINNNKFRSVFNKKYAYHDNEKLNISAMKDAAEFLIGTHDFKSFTRLKSNSKSTIRAIKYINITENQGIISIEVNGNGFLLNMVRIVAGALLEVGKENIKPIDIEKMLNEKKRADASLILPAKGLCLKDIQY | Function: Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
Catalytic Activity: uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA
Sequence Mass (Da): 28264
Sequence Length: 245
EC: 5.4.99.12
|
Q6ANM1 | MRNICLLIAFDGTDYSGWQKQHHANTIQGEIEARLKRLSVKEISLHGAGRTDAGVHADGMTAHFHTDTRLTCNDFQRALNRMLPGAIRILQVREMADDFHARFAATGKEYHYRLFTGGVIPPQKRLYMLHQEKPIDQEAMQKCLQIIIGTHDFSSFENTGSRDKTRTGGKGAVRTILEARYEQFEEDSWHFVFIGDGFLRNMVRNIVGSILEVGRGKESVEWFEQALKEKDRNAAGPTAPAHGLKLFQVFY | Function: Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
Catalytic Activity: uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA
Sequence Mass (Da): 28550
Sequence Length: 251
EC: 5.4.99.12
|
Q6MEE7 | MHCYKLTIAYDGTNYSGWQIQPNASSIQQKIQEALCILLKKEKVVLVGSGRTDAGVHAKGQVAHFHFQDYIDLSRLHVSLNGLLPRDIRIKAVEPVSPRFHSQYSAIRKEYHYYLHLNKVMDPFQRLYSWHFQRKIDVNILKKAAILFTGTHDFTSFANEAHRGTAAKNPVRTLYRLDIKPNEGGLRLEFEGDGFLYKMVRNIVGTLMDVASHKRAIEEINQIFAAKNRRQASLAAPPEGLFLIQVFYENENGCLD | Function: Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
Catalytic Activity: uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA
Sequence Mass (Da): 29303
Sequence Length: 256
EC: 5.4.99.12
|
Q813Z9 | MHNYKLTIQYDGARFKGWQRLGNNDNTIQGKIESVISEMVGKEIEIIGCSRTDAGVHALNQVANFQSDEKLVEHKVKKYLNQYLPNDISITNVEEVHDRFHARYNSKAKTYLYKIWNEEHTNPFMRKYSMHVNKKLNVKSMKAAAKHLVGSHDFTAFSNAKSKKKSMVREVYTLDVMEEAGFVQIRVSGNGFLHNMVRKIVGALIEVGLGQLDAEAIPNILEEKQRNQINCLAEASGLYLENVEF | Function: Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
Catalytic Activity: uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA
Sequence Mass (Da): 27993
Sequence Length: 245
EC: 5.4.99.12
|
Q8XHV5 | MRNIKLTIEYDGTSYFGWQKQPIGNTIQQKVEEAIKKVTKEEVEILGSSRTDSGVHAKAYVANFKTNSNIPGKNFKAALNSKLPKDIVIINSEEVAEDFHARYMTTGKTYCYTILNREEPPALERNYVYHVKKQLDVESMKEACKYFLGKHDFKAFQRPGGTVKTSVRTITDIHIETEGNKIKIYVSADGFLYNMVRLIVGTLLKVGRGKEKPEYIKEVIDSGDRKKAGICVPPTGLCLEKVFY | Function: Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
Catalytic Activity: uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA
Sequence Mass (Da): 27656
Sequence Length: 244
EC: 5.4.99.12
|
Q890R5 | MARNVRLKVEYDGTNYSGWQKQKDKNIKTIQSSIEKAIEEATKEEVELIGSSRTDAGVHALAYTANFKTCSTIPGEKFKHALNRFLPEDIVILESEEVPMEFHSRFDCIGKTYVYKILNRPLFSPIQRNYIYHVKDELDINSMIEASKFLIGTHDFNAFKKSGGNLKTTVRTITNINILKSNDIVEIHVSGDGFLYNMVRIISGTLIEVGLSRRKPEDISIILQSKDRCKAGMCAPARGLYLKELFYN | Function: Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
Catalytic Activity: uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA
Sequence Mass (Da): 28206
Sequence Length: 248
EC: 5.4.99.12
|
Q6AKP0 | MNYFRVKIAYKGTHYFGWQAQSIDTLHEEKPTVEGTILNALKKITNYQPCTVSGASRTDGGVHARGQIAKITISQKISPEHLLLGLNSLLPTDIRILECVPSTKEYQASRGSVSKEYHYYFIASPVDNVATSDIALHLPIDSIGPDDLALLRSACRLFVGRHDFYNFSSRGSGTSFREIFYCDIHRANFSPLANDMFYLKIIGDGFLKYMIRYIMGALLELVRGRIVLDDISLYLQQHQEDKLSPRAKAKGLHLIRIEGPK | Function: Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
Catalytic Activity: uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA
Sequence Mass (Da): 29428
Sequence Length: 261
EC: 5.4.99.12
|
Q6MDE3 | MDYTTQSDLSLSKSMQNIKLKIAYDGQAYFGWQKTPAGPSVEKTLQNSLEQILQHTISLQAASRTDKGVHARGQIVNFLTTKSITDLQKFILSLNSLLPTDLRILSAEKMPSTFHPTLNCVAKEYCYYICYDFVQLPEYRPYSWHCPFPLMLGKMTQAISVLIGEHDFSAFCNFKKNVNYTDYIRRVQAIHLEVLNHKRLCIRIKGNHFLYKMVRNIVGTLIYIGKGKLMVEDIPSILQSQDRKMAGVTAPAHGLFLQTVLY | Function: Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
Catalytic Activity: uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA
Sequence Mass (Da): 29935
Sequence Length: 262
EC: 5.4.99.12
|
Q6FEV2 | MMQRYAVGIEFCGIRYRGWQTQQAGVPSIQETIEKVLSKIADEPIILHGAGRTDAGVHATNMVAHFDTNAIRPQRGWLMGANSQLPKDISIQWIKEMNTDFHARFKATARRYRYVVYNTLNRPALLHKQVTHVYQTLDVDKMMLAARKFEGTHNFETFRAASCQSSQPVRHLSHCRLTRHGRYLVLDIQADGFLHHMVRNIMGCLLEIGQGCYEIEHIDTMFAAQDRKAAGVTAPADGLYFIQAYYPEHFELPQHPLGPHWLNLPDEIPNI | Function: Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
Catalytic Activity: uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA
Sequence Mass (Da): 31008
Sequence Length: 271
EC: 5.4.99.12
|
B2I367 | MQRYAVGIEFSGIQYRGWQTQQPGVASVQETIELVLSKIADEPITLHGAGRTDAGVHATNMVAHFDTNAIRPERGWIMGANSQLPKDISIQWIKQMDEEFHARFKATARRYRYVVYNAPHRPALLHKQVTHIYQKLDVQKMIKAASKFEGTHNFETFRAAACQSNQPVRHVKHCRLFEHGRYLVLDIQADGFLHHMVRNIMGCLLEIGQGMYEIDHIDAMFAAEDRKAAGITAPPDGLYFIQCYYPEQFDLPQPPLGPHWLNLPE | Function: Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
Catalytic Activity: uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA
Sequence Mass (Da): 30292
Sequence Length: 265
EC: 5.4.99.12
|
A1UUB6 | MARFKLTLEYDGSNYAGWQRQAELRTVQGAVEQAIFHFSGQQLTITTAGRTDAGVHATGQVAHVDFEKDWHVNTIHNALNAHLRQQGDNIAILNVENIPDSFDARLSAVKRHYLFKILNRRAPPALNAKRVWWLPRPLNADAMHKAAQKLVGKHDFTTFRSAHCQAKSPIRTLECLDVQREGEEIFLYARARSFLHHQIRSFAGSLMEVGIGRWTAQDLEEALHAKDRARCGMVAPPSGLYLTQVDY | Function: Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
Catalytic Activity: uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA
Sequence Mass (Da): 27935
Sequence Length: 247
EC: 5.4.99.12
|
Q6G547 | MPRFKLTLEYDGSNYAGWQRQAELRTIQSALEQALFHFSGQQLTITTAGRTDAGVHATGQVAHVDFEKNWRTHTVRDALNAHLQKQGDNIAILHVQNVPDSFDARFSAIKRHYLFKILNRRSPPALNTKRVWWIPKPLNAQAMHEAAQKLVGKHDFTTFRSAHCQAKSPIRTLERLDVQREGEEIFLYAQARSFLHHQIRSFAGSLMEVGIGRWTTQDLEAALHAKDRTRCGMVAPPSGLYLTKVEY | Function: Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
Catalytic Activity: uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA
Sequence Mass (Da): 28169
Sequence Length: 247
EC: 5.4.99.12
|
Q6MQH6 | MTTKVRFTVAYDGTGFCGWQKQKPEDQISVAQVIEEALSKVFNEKITLFASGRTDAGVHALNQVCHFSTHRKIDPNKKWDLCWALNSHLPPSIVAKKAWIAPDDFHATLSATHKTYRYLIVNKPRPSAHLNRYADWVRLPIDIEHLQESSKYLLGNQDFKSFQSVGTPVPDTVREIYKADWEWRKPGVMQFTITGSGFLKQMVRNIVGTSLFLERKGLDPSKMQEIIAAQDRMKAGPPAPAQGLYLMKVYYPQDLDNRCLEL | Function: Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
Catalytic Activity: uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA
Sequence Mass (Da): 29866
Sequence Length: 262
EC: 5.4.99.12
|
B8DW40 | MTRLRIDLAYNGAAFHGWAAQPGCRTVQGTVEEALRRITRMPDAGSLRLTVAGRTDAGVHATHQVCHVDVPDQTLGQCVGHMNLTPVQALQTRLSRMMPDDIAIHGISVAPAGFDARFSALERTYVYRIADARVPWDPRLKDFAWRTDRELDIAQMNAAAALTLGLHDFGSFAIANPGGTTIREVKTAYWQRVPTRPLLGPGMGERYHTPAVESGLLCFTIVADAFARNMVRSLVGACVQVGMGKRDVDWFAGKMRVPLREGSTGPIAPQGLTLEHIAYPADDELAARAERIRAKRTL | Function: Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
Catalytic Activity: uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA
Sequence Mass (Da): 32607
Sequence Length: 298
EC: 5.4.99.12
|
Q2KYM0 | MTRIALGLSYDGSSWQGWQTQPHGQTVQDTLEAALGQFSGTGAPLDTLCAGRTDTGVHAAMQVVHVDTHLNRRAESWVRGVNAFLPSSISIHWAKEVGEDFHARFSARSRTYVYLLWRGRVRPALWAHRAGWCFQPLDVTAMRQAAQALLGEHDFSSFRSSQCQARHPVRHLTRLDIAERGSFLVFTLQANAFLHHMVRNIMGALLQIGQGRESVDWMASLLRARDRRLGAPTFSPDGLYLSAIDYPTLFELPDLDGGSSLLAPFTA | Function: Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
Catalytic Activity: uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA
Sequence Mass (Da): 29683
Sequence Length: 267
EC: 5.4.99.12
|
P70830 | MKKILAEIAYDGSIYHGFQIQPTKPTVQGEIEKALMKINKKKVKIHSSGRTDKGVHAKKQIITFDIKINIQLNNLKKALNAILLKNSIKILKLRYVKNSFHPRFSAQKRKYSYCILNSDNYYPWEGYQAHYVNKKLSISNLNQMAKTLIGKHDFTTFSCIKDKSKSKFRHIYFAKFKKRGKYIIFEIIGSSFLWKMVRSIIGTMLDIEIKNESISTFETILKSKNRNLARTTAPANALFLERVYYE | Function: Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
Catalytic Activity: uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA
Sequence Mass (Da): 28657
Sequence Length: 246
EC: 5.4.99.12
|
A5N4T0 | MKNIKLVIEYDGTNYSGWQRQYNAITIQQRLEEAIEKATGEFSPVIGSSRTDAGVHARGFVCNFFTASKIPTSNIKMVLNTLLPEDIAVLDSKEVDSSFHSRYFTTGKEYSYTIVTGDRPPVIGRQYVYYFRRKLDIEKIKNSCEYFIGTHDFSAFKKKGSTARSSIRTIKELTVLKEKNIIKFNIVGDGFLYNMVRIIIGTLLEVGLGRFSIEYVKYILESKDRAKAGKPVPAKGLCLEKVFY | Function: Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
Catalytic Activity: uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA
Sequence Mass (Da): 27753
Sequence Length: 244
EC: 5.4.99.12
|
B5Y955 | MVKYAGLLQFKGTNYAGFQRQKNGTAIQNVLESTLSQINNRATVVRYSGRTDAGVHAWGMPFVFWGREDLSADKWMFILNRMLPKDMRVISVVRTSPEFDPQLSAVAKQYLYCATQERLGPLWDDFFAYLPNLSIETSAVISAARKLVGEHDFKGFSKKGSSVKSTRRKLYEVSVMFTHSRMYFSFVGNGFLYGMVRLMVGTLLQIGWGKQDVNFIDEVLSGNAVANYSAPAQGLHLVKVWLEPDPFLESVKANERDFS | Function: Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
Catalytic Activity: uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA
Sequence Mass (Da): 29254
Sequence Length: 259
EC: 5.4.99.12
|
Q8NSV0 | MRIRLDLAYDGTDFHGWAKQGTSDLRTVQKVLEDNLSMVLRETVELTVAGRTDAGVHAAGQVAHFDIPAHALEQRSIDGDPSKLVRRLGRLLPDDIRVHGVRFAEPGFDARFSAMRRHYVYRITTHPAGALPTRRHDTAQWPKPVELERMQLAADALLGLHDFVAFCKAKPHATTVRELQKFAWKDVSTDIEPQVYEAHVVADAFCWSMVRSLVGSCMAVGEGRRGSGFTAELLDASERSPMVPVAPAKGLSLVGVDYPSADKLQERALETRAVREFPDASASLKLDDE | Function: Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
Catalytic Activity: uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA
Sequence Mass (Da): 31992
Sequence Length: 289
EC: 5.4.99.12
|
Q0K8H3 | MNRIALGLHYDGAAFSGWQSQPHRNTVQDHLENAIERFAGVRLLTTVAGRTDTGVHALGQVIHLDTALEREPFSWVRGVNAFLPPSIALQWALPVDQGFHARFLAFERMYYYALYTGPHRVPLVHGRAGYQMLPPGQRLDVDAMREAAACLLGEHDFSAFRAAECQAKSPVKTMYDVTIRDDGNWVFLRFRASAFLHHMVRNLMGCLVAVGRGRYPAHWLAQVLAGRERKLAAPTFMPDGLYLVGVKYPDPYQIPAADPSASLFHGVFDDAA | Function: Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
Catalytic Activity: uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA
Sequence Mass (Da): 30329
Sequence Length: 272
EC: 5.4.99.12
|
Q6A6S8 | MTRWRLDIAYDGANFSGWATQPDRRTVQGELETWIPRVLRLDQPTPLTVAGRTDAGVHARGQVAHVDLPDNVDTSAMLRRLSRVLTPDVVVKSVRPVPSTFDARFSALWRRYVYRLWDESSRPDPVTRFHVAPVRGHLDLDRLNTAGTSLLGLRDFAAFCKHREGATTIRTLLDCHAKRLDDPCGTVEVTVRADAFCHSMVRSLVGALTAVASGRRSQDWLDNVAASTSRASSVLVMPACGLTLEEVGYPSDEDLAQRAAQARSRRSHNDICDTCWEDR | Function: Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
Catalytic Activity: uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA
Sequence Mass (Da): 31092
Sequence Length: 279
EC: 5.4.99.12
|
Q9RS37 | MDADPPRLYAPPPGFTRLRLTVAWDGRDYAGWQEQRNAVSVQETLQTALHALGGEGALRPVSAGRTDAGVHAEAMPLHWDVPTTFRVPLVQLPRALNAWLPASVSVLSAEVAPAGFHARFSCTERRYVYRLWVAPQRHPLWAGRALHVPGPLDAEAMNRAAQSLIGLHDFAAFATREDRQTVRDLLRLEVQPQGELWDIHVAGESFLRHMVRGLVGTLLLVGQGKLGAAEVEGILASRERARAGANVPPGGLYFAGAEYGVRRVEGRSGNGGEPGTHRGR | Function: Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
Catalytic Activity: uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA
Sequence Mass (Da): 30455
Sequence Length: 280
EC: 5.4.99.12
|
B1I1B5 | MPNVRLTLAYDGTAYHGFQKQSGSGLPTIQETLERCLAELSGAALKVTGASRTDAGVHARGQVVNFVTGRWGIPTERIPAALNGVLPGDIAALDAREVPADFHARYSAVAKTYSYTLYNHPVRSPFQRLYSLHVPRALDLRAMRLAARHLMGRHDFSTFQAAGRPVQSAVRTLTRADIEAQAPLVRLVFRADGFLYNMVRIMAGTLLEVGLERLDPEALPDIIASGDRARAGPTVPPHGLCLEEVEYDST | Function: Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
Catalytic Activity: uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA
Sequence Mass (Da): 27244
Sequence Length: 250
EC: 5.4.99.12
|
Q8PWT1 | MRVALKLAYIGTEFHGSQIQPSVETVEKELFKALRNLRIIESPKSANYICAGRTDAGVHALGQVIAFDTDRPNLAIPRIINSGLPPTIWVWAHAEVPYDFDARRHAVSRHYRYVISGEGYDISKMREASKLLLGTHDFENFSRSNGEKSTVRTLERINVRVDGDITKIDVVGNSFLWNMVRKIVTALSMIGKGVRDNDWLIQMLNPDIYEEGIEPAPAYGLTLMGVNYGEEINWIEDNYSIRRASDQNSKRILRYRVMAEVLEELIYHE | Function: Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
Catalytic Activity: uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA
Sequence Mass (Da): 30684
Sequence Length: 269
EC: 5.4.99.12
|
A3CXX4 | MNLAFRFSYFGDRFFGSQMQPDLCTVEGEFIGACRLLRLFDDWREANFATAGRTDRGVHARSQVCSFLTDKPERAIEALNRVLPADIWCTGWAEAPDGFHPRYSAVSRTYRYYFSAPGDAAAMHEAAQEFLGRHDFSAFARAGDRNPERRILASRVFIDGEFAVFEVTGESFLWNMVRCMATMLGRVGRGEAEAGEIARLLTGPVERRVAAAPPEGLILWDIDYGIPFTPLPIDAGSSRHLGDRHRYHVLMAKISAHLAQDHRQPDTPGI | Function: Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
Catalytic Activity: uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA
Sequence Mass (Da): 30287
Sequence Length: 270
EC: 5.4.99.12
|
B8GFU5 | MRLAFQLSYDGNQFRGSQLQPAYRTVEGELITACQRVQLFDDPCKAGFALAGRTDRGVHARGQVGAFSTPFPERAVEALNGQLSPDLWCNGFAEVPPSFHPRFDAISRTYRYFFADWPLDIRAMDQAAAALIGTHDFSRLARVREKSPIRTVKSARVFQDRGIPVFEVTAHTYLWHMVRCMAAALLLIGTHEREPELMERLLSGKCRRNPPAAPADGLVLWDVDCGVTFTPTEPDPRSRDWIGSARREAMVRERIIGLLDRSGVDRRGKEPGDDSGRDLL | Function: Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
Catalytic Activity: uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA
Sequence Mass (Da): 31429
Sequence Length: 280
EC: 5.4.99.12
|
A5ULI2 | MKRTALKIGYIGTNFHGFQRQPDLRTVEEELIYHLRKLGYIDDLKKSRFRIAGRTDAGVHSLGNVISFQSEKEVRVNEINNSLPDDIQILAKAPVRFGFKPRYAEMRQYRYVLFRSDLDLYKLNEVAEIFKGTHNFTNFTKRFQKTTTRTIDDIKITKANLNDYHKKEFPNLHDTLSPVFVDIYGESFLWNMVRKMMRVFVDVAIGKLSLEKVEELLNPAENDPRANIKVLDPDYLILMDIKYDGVKFVYDDYACERFKRNLVDSLGDLQRKYAIRESMIKSLEDLERIN | Function: Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
Catalytic Activity: uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA
Sequence Mass (Da): 34124
Sequence Length: 290
EC: 5.4.99.12
|
Q2NHB4 | MRRVALKIAYIGSNFHGYQRQPNYRTVEGELLRVFKETNIIEDTWTAHYSVAGRTDKGVHSTGNVISFITDEDIHINQLNGLLPDDIKIIGEARVPYGFKVRFPLTRTYTYIQPISPFEKKNLDITKMHVAMESFIGKHNFRNFSKRNEKNPNRKIIDVNLEVDEDVLIFTIVGESFLWNMVRKMVTSIMEVGYGKLDINDINELLKPKELRQFIRLQPAPANGLILSDMEYKNIKFKDSEYAKNKLVEFLKKEYMLHEQEKKADCRLIKILKK | Function: Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
Catalytic Activity: uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA
Sequence Mass (Da): 32045
Sequence Length: 274
EC: 5.4.99.12
|
O26928 | MRKIALKVAYIGTNYHGFQRQPDVPTVEGKLLEALEGAGIIEDPKRARFQIAGRTDRGVHALGNFVSFFTEEDIHVNQINDLLPRDIRVLAWASVMYPFKVRYPLERHYRYILHREESMDTYSMAEAAAHFRGTHDFSNFSRRSDRDPVRRINDVRISEVGDSIIIDVYGESFLWQMVRKMVRALLMVSEGELAPDDMAGLLDTDRRVFLEPMPPENLILMDLKYGVKIKLRHDEYAFKRFISLLEEEFKVYREMSMVRRAMSDHLRDLQEHELD | Function: Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
Catalytic Activity: uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA
Sequence Mass (Da): 32253
Sequence Length: 275
EC: 5.4.99.12
|
A0B7V0 | MKIALKIAYLGDRYYGFQRQPGLRTVESVMRDALLRIGVANGDFCYAGRTDRGVSALGQVIDFWIEEDRAYLAFPRVINSLLPSDVWAWARAVAPVGFSARWSALWREYRYFLFSPDIDLSAVREAAGHLVGTHDFRNFSMSKVDTVRRIISIDVNAHCGIVVFDVRAEGFIWNMVRRIVGALELIGIGEKPVDWILELLDPSTPHGAPTAPPEGLMLMDVGYSDLEWEEDRYTKQRVSRMLISEARRRAAMSGVIQEMLRRMRDTF | Function: Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
Catalytic Activity: uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA
Sequence Mass (Da): 30422
Sequence Length: 267
EC: 5.4.99.12
|
P65847 | MSLTRRPPKSPPQRPPRISGVVRLRLDIAYDGTDFAGWAAQVGQRTVAGDLDAALTTIFRTPVRLRAAGRTDAGVHASGQVAHVDVPADALPNAYPRAGHVGDPEFLPLLRRLGRFLPADVRILDITRAPAGFDARFSALRRHYVYRLSTAPYGVEPQQARYITAWPRELDLDAMTAASRDLMGLHDFAAFCRHREGATTIRDLQRLDWSRAGTLVTAHVTADAFCWSMVRSLVGALLAVGEHRRATTWCRELLTATGRSSDFAVAPAHGLTLIQVDYPPDDQLASRNLVTRDVRSG | Function: Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
Catalytic Activity: uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA
Sequence Mass (Da): 32620
Sequence Length: 297
EC: 5.4.99.12
|
Q7NAQ9 | MVYLVHQNEWRSVWVKTLAKLNKNVLINISYHGTKFHGYAVQNDYETVQSKLQDALAWIYESKIYVNASGRTDKGVHAINQYISFYIDDRISLEKLREILNRYGQNKWYIKWIKEVDRNFHARFSAKAKTYLYLIDYCANNPLFYDHAWIVNFQLDFNLIEKAIPILEGTHNFWSFSTADKDKGLRTIHKIDLKQEDNKVYIYITGDGFLRSMVRMIVGALYNIGIKKYDLNHLKWLLDNPKKGRAITKAPASGLYLYEVYYE | Function: Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
Catalytic Activity: uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA
Sequence Mass (Da): 31104
Sequence Length: 263
EC: 5.4.99.12
|
P47428 | MARYLGIVSYDGSYFKGWAIQPNLATIQGLLEQSFSLIIGRKIKVIGSGRTDKGVHAINQTFHVDINGEINLNLLIRKINQLIKPHCIVKTLVLVNDSFHARFQVKTKVYEYLINCGNLNPLQFNYVWQLNQQLDLEKLKADATLFLGKKNFLSFSSSIHTDSIRTISKITIQKETNQLVRLTFFGSGFLRSQVRMIVACLVNLNTNKMALETVAKLFEHPKKGSCVVKAPSCGLYLKTVVYEK | Function: Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
Catalytic Activity: uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA
Sequence Mass (Da): 27597
Sequence Length: 244
EC: 5.4.99.12
|
Q49ZD7 | MRVLVNISYQGSQFLGFQIQQHGRTIQQQFEKILKRMHKHEVRIHPSSRTDRGVHAIEQYFHFDTELNIPEQQWQYAMNRALPDDIYVNDVSFVNDDFHCRYDCVGKSYRYKIYQSAHKDPFLCGLKTYVPEQLDIEKMNMAAQHFIGTHDFTGFCSQKTEVESKIRTLYESRIEKTESGFDYIVTGSGFLYNMVRVLIAFLIEVGKGKREPQEVPQLLEARDRNQVPFTAPAEGLYLEKIYLTPNELIQDFGNNIKIHQKKSSQNL | Function: Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
Catalytic Activity: uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA
Sequence Mass (Da): 31296
Sequence Length: 267
EC: 5.4.99.12
|
Q82DM1 | MSDEVQPGFVRVRLDLSYDGTEFSGWAKQAAGRRTVQGEIEDALRTVTRSGETTYELTVAGRTDAGVHARGQVAHVDLPGELWAEHQEKLLKRLAGRLPKDVRVWSLTEAPSGFNARFSAIWRRYAYRVTDNTGGVDPLLRSHVLWHDWPLDVDAMNEAARRLVGEHDFAAYCKKREGATTIRTLQELSLVRGDDGVITATVCADAFCHNMVRSLIGALLFVGDGHRGPDWPGKVLAVGVRDSAVHVVRPHGLTLEEVGYPADELLAARNKEARNKRTLPAAGCC | Function: Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
Catalytic Activity: uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA
Sequence Mass (Da): 31388
Sequence Length: 285
EC: 5.4.99.12
|
O86776 | MSDEVEAGFVRVRLDLSYDGSEFSGWAKQAGGRRTVQGEIEDALRTVTRSRETYELTVAGRTDAGVHARGQVAHVDLPREVWAEHHVKLLKRLAGRLPRDVRVWALREAPSGFNARFSAVWRRYAYRVTDNPGGVDPLLRGHVLWHDWPLDVDAMNAAARGLLGEHDFAAYCKKREGATTIRTLQELSLVRGEDGIVTATVRADAFCHNMVRSLIGALLFVGDGHRGPEWPAKVLAAGVRDSAVHVVRPHGLTLEEVGYPADELLAARNKEARNKRSLPGAGCC | Function: Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
Catalytic Activity: uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA
Sequence Mass (Da): 31312
Sequence Length: 284
EC: 5.4.99.12
|
Q89WB1 | MGGNSQPHQEPRRVNNDPRAKQQKGNQVRRDRRDVHGWVVLDKPIGMTSTQAVAVLKRLFNAKRAGHAGTLDPLASGGLPIALGEATKTVPFVMDGRKRYQFTVCWGEERDTDDIEGRVTATSELRPTREAILALLPRFTGVIEQIPPRYSAIKIQGERAYDLARDGEVVELAPRPVEIHRLTLVDQPDNDRAVFEAECGKGTYVRALARDMGRILGTYGHICALRRTLVGPFGENDMIPLDQLEALCDRAASGEGSLADALLPVETALDDIPALAVTRADAARLHRGQAVLLRGRDAPTCSGTVYVTVAGRLLALAEVG... | Function: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Mass (Da): 37572
Sequence Length: 345
EC: 5.4.99.25
|
Q8YEB5 | MARRGKKKGRPISGWVIFDKPKGMGSTEAVSKIKWLFSAEKAGHAGTLDPLASGMLPIALGEATKTVPYAMDGTKVYRFTVTWGEERSTDDLEGQPTKTSDKRPSREEVEALLPDYTGVISQVPPQFSAIKIDGERAYDLAREGETVEIPAREVEIDRLEIVGFPDADRTEFEVECSKGTYVRSLARDMGRDLGCYGHISDLRRVEVAPFTDEDMVTLAKLEAVWPPLPPKDEDGNVIEPAPRRDFSALDALVIDTGAALDCLPQVPLSDDQAQRVRLGNPVILRGRDAPLEADEACVTTRGKLLAIGYIEHGQFKPKRV... | Function: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Mass (Da): 35567
Sequence Length: 324
EC: 5.4.99.25
|
P57456 | MFFHKKRDVHGLLLLDKPQGISSNNALQKVKMLFSAKKAGYIGTLDPLATGMLPICFGECSKFSHYLMESNKKYHVIAKLGEKTSTSDSDGIIIKKRPILINSFKIKSALKELTGLIEQIPPMYSAIKHNGVPLYKYARQGLNIKRSIRKVLIHDISSIHQEKNLIEFKIFCSKGTYVRTLVEDLGEKLGCGAHVIFLRRLEMASYLHSQLVTISYLHKLLRKEKNNNFNFFEKIDNLLMPIDSPVSFLPKVYLFPQQSYNFQLGQTVIFFSDIKNSLVRVIALENNKFIGLGRINTEELLIPYRLVSRSIN | Function: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Mass (Da): 35653
Sequence Length: 312
EC: 5.4.99.25
|
Q89AF6 | MYSEFRSIDGIILIDKPYGLSSHETLQKVKGILKIKKMGHTGTLDPLATGMLPMCCGRATKFSQFLMNFKKRYRVIAKLGQKTSTSDSEGQIIHVRPITFTNLQLQKVLKSFHGKIKQIPSMYSAIKYHGHALYKYARQGIVISRKVRDAIIYELKVLGYSYKHKYLELDIICSKGTYIRTLIEDVGEKLNCGAHVISLRRLQVGNYTSFQMIDIKTLNKLVKYNINVLEHILLSVDNAISCFPEVNIVPNVIKNLQNGQKVKTHSGFINQFVRITEGINRRFIGIGKINNINELYSYRLII | Function: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Mass (Da): 34502
Sequence Length: 302
EC: 5.4.99.25
|
Q39H28 | MRPPRTTELDRPMTTAASQRPRVPRRLLDGVLLLDKPVGLSSNDALIRAKRLLLAKKAGHTGTLDPLASGLLPLCFGEATKFSQDLLEADKTYEATMRLGQRTATGDAEGEVIDTRPVECDRAAVEAALVRFTGEIVQVPPMYSALKRDGKPLYEYARAGQTVEREGRNVTILALALLACDLPDVTFRVTCSKGTYVRTLAEDIGEALGCGAHLTMLRRTGVGALTLEHAVTLDALSDADDASRDAWLQPVDALLSTFPLVRLDETSAKRFLHGQRLPLSALDPIDAAEGERVRVYDATRLLGVARKANGVLAPERLVVT... | Function: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Mass (Da): 34803
Sequence Length: 322
EC: 5.4.99.25
|
P59879 | MDFNNKIVIIDKPKNISSAFCLNLFKKRFNIKKAGHNGTLDPLASGVLVVATNKRTKELSQLNQDDKQYLVKLKFNTHTDSYDRLGKVIRTTNYVPEIKQLNDYLTSLDNHSFYQLPPNFSALKVNGVRAYQLARKAVDFELEKRPTTIYKAKLISYYDDYAEILLDVKKGFYVRSFVVDLASQFNTTAMMVDLVRTRSGQYSLKDVIDYQFNK | Function: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Mass (Da): 24718
Sequence Length: 214
EC: 5.4.99.25
|
Q9Z5I4 | MSESSTGAGLGPGIVVIDKPSGMTSHDVVARCRRIFCTRRVGHAGTLDPMATGVLVLGVDRATKILGLLAGASKEYVATIRLGQTTSTEDAEGELLQCVSARHVTDEAIATAIGRLRGDIKQVPSAVSAIKVDGRRAYRLVREGHVVELQARPVRIDRFEVLAVRPGPEVGLADVIDLDVEVECSSGTYIRALARDLGDAFGVGGHLTSLRRTRVGRFELDQAWSLEDLAELPRLSRTLDETCLLMFPRRDLTVSEVEATSNGRPISSAGIDGIYAASDADGRVIALLRDEGPRTKSVVVLHPVFVRVSIGRGIVGVIEA | Function: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Mass (Da): 34180
Sequence Length: 320
EC: 5.4.99.25
|
Q98Q19 | MFYLIYKEKGISSFKAIKDFAWQNNIKKIGHSGTLDPEATGLLLLASDEDTKLLDYVDKKFKSYRATMILGLQSQSFDSQGKIINSSNLKVDNLTIEKTIKNFVGPFVQIPPIFSAKKINGKRAYEYARQGSEISMKAQEVFVKSIEIEKIDFPKVIFKAKVSRGTYIRSLINQIGLELKTYALMDDLERIELSGLSKNDLGVVSDLDIIDLEVLSLEKHEILTLAKGQKFSKDLADGKYAFIYKNTKKILGICKIESKIIAPIKIFNKKIEKSLKKDEKNE | Function: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Mass (Da): 31961
Sequence Length: 282
EC: 5.4.99.25
|
P60346 | MLCLSLMRIFCSKCLEEQECPLPWELEKYEIWVKKEAETNEKWGEDPYNRPIERLLKYSVINLDKPSGPTSHQVVAWVRDIVGVKAGHGGTLDPKVTGVLPIAIGEATKVLQTLLIAGKEYVALMHLHKEVSEKDIIKVMSKFVGTIIQTPPLRSAVKKRPRKKKVYCIKIIEIDGKDVLFRVSTQGGVYIRKLIHDIGVKLGVGAHMQELRRIKSGPFHENNSVYLQDIVDSLYFWKEEGNEEYIRKVFLPVEEAVKHLKKIYILDSAVAAIVHGANLAVPGIAKLYSNIKKGDLVSIHTLKGELVAIGIALMDSKEML... | Function: Could be responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Mass (Da): 39259
Sequence Length: 348
EC: 5.4.99.25
|
Q9JYY1 | MNTGKPQKRAVNGVLLLDKPEGLSSNTALQKARRLFHAEKAGHTGVLDPLATGLLPVCFGEATKFAQYLLDADKAYTATLKLGEASSTGDAEGEIIATARADISLAEFQTACQALTGNIRQVPPMFSALKHEGKPLYEYARKGIVIERKARYITVYAIDIAEFDAPKAVIDVRCSKGTYIRTLSEDIAKHIGTFAHLTALRRTETAGFTIAQSHTLEALANLNETERDSLLLPCDVLVSHFPQTVLNDYAVHMLHCGQRPRFEEDLPSDTPVRVYTENGRFVGLAEYQKEICRLKALRLMNTAASAA | Function: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Mass (Da): 33632
Sequence Length: 307
EC: 5.4.99.25
|
Q2Y7W4 | MSPGSKRHISGVLLLDKASGLSSNQALQTAKRIFSAHKAGHTGTLDPMATGLLPICFGEATKFSSALLGADKTYEAVLRLGYMSTTGDAEGEISIAAGMESQYVDLTREKIEAVRKSFIGVITQVPPMYSAIKHRGKPMYTFARAGVEIERQPRAITIHDLSIEAYQGNEMRIRVTCGSGTYIRTLAEDLGHALGCGGAYLTALRRSALGGFDLPQAYTLTGLEAMPPSQRDSCLLPADSLLRSLPPVVVDSAAALSLLQGRAIPGTHPAGESLLPGRQVRLYDKAQRFLGLGEISTEGYISPKRLIRFEQSL | Function: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Mass (Da): 33564
Sequence Length: 313
EC: 5.4.99.25
|
Q72GS9 | MALYAVDKPLHLTSHDVVEEARRRLSTRRVGHTGTLDPLATGLLLLVTNESTKLVPFLSGEDKEYIAWVSFGATTPTLDAEGPISEEAPARFDRKDLEAALPRFLEVREQVPPLYSAIKVGGKRAYEAAREGKPLALGPRPVRYLEVELLAFDPEPIPHPIAPSARGWRLAERRGRPVRLPRPLGAYPTAVVRLVVGPGTYVRAFARDLGEMLGTKAFLSGLVRTRVGRVGLERAVALSDLSPEKAIPELDVLPFPVVELSHTEARRVLEGMPLPIPAMGYVTLVDSKRRLLAIAEGDGFKLKIRRVFAKEA | Function: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Mass (Da): 34292
Sequence Length: 312
EC: 5.4.99.25
|
Q8CWM3 | MFGFLNLNKPAGCTSHDCINELRRRLRLKRIGHGGTLDPMATGVLPIALGAATRLLPYLSDRKAYIGTVRFGMSTTTDDITGEICQEQGASHLTLAAIQEQLPQFIGEIEQLPPAYSAIQVAGQRLYARARAGEVVSVPPRIVTVYRIEVLHWQPGRYPELTLHITCGSGTYIRALARDLGTALGVGGTLAALQRIESGGLRIEESHSLESIAPEHLPLCSPQEVLSHLPWLELNAAQLNDWYHGRAVICEGLPPADSCVGVTFATACVGVGISGGDRLHPKVVLKE | Function: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Mass (Da): 30954
Sequence Length: 287
EC: 5.4.99.25
|
Q97BU9 | MIEEIQKLNGFIVIDKPQGPTSHQVDYWVRQILGTEKVGHIGTLDPNVTGVLVMAIGKAVRLIDVVHEKPKEYVGVMRFHSDISEEEVREVFRKFTTRIYQLPPVRSAVSRKVRIKTIYELDMIEKKDKIVLFHVKCESGTYIRTLCTDIGYVSGKGGQMVDLRRISTGPFKEDIAITLQDLQAYVDLAKEGKDELFRSHFLDMTYAFIDYPKIVAKKSAVENIAHGSDLYVGGVKLIDGNFQKGDRVCVLSEDNELLGTGIARCDSSNLFMKVVDFDHIFVEAKHGKGDVVRDREKDVQRPGQQVHRNIRDAAHGPDSR... | Function: Could be responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Mass (Da): 39859
Sequence Length: 353
EC: 5.4.99.25
|
Q3SKX3 | MKPARQAVDGVLLLNKPVGITSNAALQKAKWLLNAKKAGHTGTLDPFADGLLPLCFGEATKFSAYLLDADKRYRAILQLGVTTRTGDPEGEVLATREVRATCADIRAALPAFVGEIEQIPPMHSALKHQGRPLYEYARAGVEIARAPRRVHIRALDLFKCAPPRAVVDVQCSAGTYVRTLAEDLGNALGCGAHLTALTRTASGGFLLEQAHTLAELEATNAGARQALLLPADCLVAHLPSVHLGETAAASLRQGRSVPDAADRRGLVRVYDGHGVFVGLAEAEAGKLVPRRLIATVQA | Function: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Mass (Da): 31607
Sequence Length: 298
EC: 5.4.99.25
|
Q73NP8 | MELNKNLIIPFAKQAGLTSFASMSAVKKALSTKKVGHTGTLDLFADGLLVLLTGQLTRLADIISAEKKTYEAWVEFGTETDTLDPEGEPVLTAPLPSYKNLTESIPSFLGKILQRPPEFSAIKINGKRASDRIRSGEKIKIAEREIEIFKIELKGIITDSGLEFTEKDFTNINAELKIRYAHIVVECSKGTYIRSLVRDLARKASSCAYVRALRRTAVGNFKLEDAAGFDLLNNFSAAPENLFLKEKKILDAAAGKKFYKQKEIDFLEIMAKSIIFSPKTAENLKLPYLFLDRKYLNDFYNGKKIKFNWFLNTDEVLENI... | Function: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Mass (Da): 40131
Sequence Length: 357
EC: 5.4.99.25
|
O83859 | MCRLSMPDAIVPFAKVSGLTSFAALAQVRRLLGVKKVGHTGTLDRFADGLLLLLVGGFTKLAPVMTRLEKSYEARIQFGVQTDTLDPEGAVVRCSLFPTFARVRAALPHFTGSIDQVPPEYSALKFGGVRASDRVRRGEAVCMKARRVFVFDLQVLGCEADLGEFKKTQAGRGAAIADLDLTRVRAVTLYVRCSAGFYVRALARDIAAACGSCAYVSHLRRTRIGPFDLAQAAGVSRLGSWTWGKERASCGAACFDVGAPPPPSSGGVATDSVSFGCEDLTVREIKQAVVSCDVDFANRIGLTACSVHAQYASRFLHGER... | Function: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Mass (Da): 39471
Sequence Length: 366
EC: 5.4.99.25
|
Q112N2 | MQGFLNLNKPSGMTSHDCVAKVRKLLRLKRVGHGGTLDPAATGVLPIAVGKATRLLQFLPSEKAYFGTVKFGIITTTDDLEGEIVQSAPVPELMLSDIEKVLPNFLGKIEQVPPSYSAIQVEGKRLYDLARQGKTVEVPTRIVEVFNIKILDWRSGDFPEVDLAIACGTGTYIRAIARDLGRTLSIGGTLAALTRIESSGFSEENSLTFAEVENQLQENKFSLLSIEIALAHLPVIVLITEDAKRWCQGQRLPYQVKWQIETKKAEHYFRVYNYKGDFLGIGQLIKSEENLLLAPQVVISN | Function: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Mass (Da): 33313
Sequence Length: 301
EC: 5.4.99.25
|
Q820Y5 | MLGKVERSEMYILFAMTQVLLVDKISGITSHTAVAKIRHLTGIKKIGHCGTLDPAACGLLIMGCGTATRLIRYMSNLDKRYIATITLGTQTTTDDSEGEIIYSAPKPSLDKITLESIGRAAEKLSGTIKQIPSAYSAIKVSGNRAYNLARQGIIPKLNAREVRVHWKFLGDFENNQVHVQITCSSGTYVRALARDMGKFLGVGGHLSYLKRLSIGPFHLHEIYREINKKEATMSERTPSGNTQGLTDNMAISESDKHDCTEPGINCTELGIKDTCTALREVHYTQGDTLSFTRLTALQALSRIYKPIEVSQKQADDLSCG... | Function: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Mass (Da): 41136
Sequence Length: 377
EC: 5.4.99.25
|
B5ZBG4 | MYTINKNIIVINKPINWTSNDVVQKVKRIIKAKKVGHAGTLDPNASGILVLGINEGTKLLTKLTLDSKTYVAEIQFGISTNTYDSTGEIISKINKFITLTEIESAIENLYKNEYWQKPPKFSALKINGKKAYELARNNISFEIEPRLVKIFEYNILDFNYEKQILKIIIKVSKGFYVRSFAVDLAARINNLAHLLSLVRTESGQFSINDAIEIEQVYDYWNNINKHSTN | Function: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Mass (Da): 26151
Sequence Length: 229
EC: 5.4.99.25
|
A1WLI1 | MPPASRTRVQRRPVHGVLLLDKPLALSSNQALQKAKWLLRAEKAGHTGTLDPLATGVLPLCFGAATKFSQLQLDAPKTYEAIALPGVTTSTGDAEGAVLQRCAVDPAQLAPERLSAVQRQFTGPISQLPPMHSALKKDGRALYTYARAGIALERAARAVVIHALELSLVQHAPAQTAIKIAVTCSKGCYIRTLAEDIGAALGCGAHLSALRRTDSGGIGIERCISLERLQALPEAERLACLQPPQSLLTRHLRVTLDSDNAARFLSGLPRRGAWPDAPAVAVFGADPPALLGVGHIAGGCLLPDRLLSALEIAQILASQP... | Function: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Mass (Da): 34990
Sequence Length: 331
EC: 5.4.99.25
|
Q8EBR4 | MSELHYLYGKPTGTADLRTVNSDFIVKEILPFSPSGEGEHHLVHIRKDGLNTVQVAEMLAKFAKVHPKEVTYAGQKDKNAITEQWFGIRIPGKETPAWIELNSDRLTVLSSSRHSKKLRIGALLGNRFILTLRNVTNVEDIISRIEKVSQIGVPNYFGEQRFGHDGKNLVLGRQMLAGKKVKDRNKRSMYLSAVRSHLFNTVVSYRLTHYGTRPLAGDCVMLAGSKSFFVTPEWDLVVLKRLIEKDIQLSAPLWGRGKMLPQGEAAEVETQAMADLTEDCYGLEHAGLEQERRPLLLEPQGLKHEQTSDGLVLEFILPAG... | Function: Responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs.
Catalytic Activity: uridine(13) in tRNA = pseudouridine(13) in tRNA
Sequence Mass (Da): 41298
Sequence Length: 370
EC: 5.4.99.27
|
Q3A6I8 | MANYLTAKLPGIGGSIKTCPDDFLVEELPLYPTCGEGEHLYLEVEKRGMTTFELLKRLSRALQVNERAMGYAGLKDAQATTRQFISVTDCSAEQALALQLQDIRILSARRHRNKLRLGHLAGNRFTITIRDIDSDALEKARDILHVLQMTGVPNFFGEQRYGALGNSHLIGQAIVQKNFSQAAAHIIGDPDKIIHPEWRQGAILYAENRLEEAEQALPRRMRNERNLVRSLRQGRSAEKAVRRLPGKLLRLYLSAYQSHLFDRLVSMRLESLETLWTGDIAYKHDNGACFLVTDAALEQPRADRFEISPTAPLFGHKVMM... | Function: Responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs.
Catalytic Activity: uridine(13) in tRNA = pseudouridine(13) in tRNA
Sequence Mass (Da): 44480
Sequence Length: 398
EC: 5.4.99.27
|
P30635 | MLLSTFKRHLPIRRLFSSNKFDLIVIGAGSGGLSCSKRAADLGANVALIDAVEPTPHGHSWGIGGTCANVGCIPKKLMHQAAIVGKELKHADKYGWNGIDQEKIKHDWNVLSKNVNDRVKANNWIYRVQLNQKKINYFNAYAEFVDKDKIVITGTDKNKTKNFLSAPNVVISTGLRPKYPNIPGAELGITSDDLFTLASVPGKTLIVGGGYVALECAGFLSAFNQNVEVLVRSIPLKGFDRDCVHFVMEHLKTTGVKVKEHVEVERVEAVGSKKKVTFTGNGGVEEYDTVIWAAGRVPNLKSLNLDNAGVRTDKRSGKIL... | Cofactor: Binds 1 FAD per subunit.
Function: Maintains high levels of reduced glutathione in the cytosol.
Catalytic Activity: 2 glutathione + NADP(+) = glutathione disulfide + H(+) + NADPH
Sequence Mass (Da): 55046
Sequence Length: 503
Subcellular Location: Cytoplasm
EC: 1.8.1.7
|
Q9NNW7 | MAAMAVALRGLGGRFRWRTQAVAGGVRGAARGAAAGQRDYDLLVVGGGSGGLACAKEAAQLGRKVAVVDYVEPSPQGTRWGLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEVAQPVPHDWRKMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVCGVAKGGKEILLSADHIIIATGGRPRYPTHIEGALEYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMRSIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDGQLQVTWEDSTTGKEDTGTFDTVLWAIGRVP... | Function: Involved in the control of reactive oxygen species levels and the regulation of mitochondrial redox homeostasis . Maintains thioredoxin in a reduced state. May play a role in redox-regulated cell signaling.
Catalytic Activity: [thioredoxin]-dithiol + NADP(+) = [thioredoxin]-disulfide + H(+) + NADPH
Sequence M... |
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