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 | MSPTTPRSVEPSGLKPEQLPPSYFTWPGLLGRLGNGQELSEAQVRWAMNEIMEGNATDAQIAAFAFGIRVRGITAAELAAAAETMTSFATPVDFSDVPNCVDIVGTGGDGHHTVNISTMASFVVSAAGVPVVKHGNRAASSKCGGADMLEALGLDIERSPEDIRQDAHDTGFAFMFAKTYHPAMRFAGPVRSQLGAPTIFNLLGPMTNPAYPKFGLIGCAFKEFMPIMGGAFARQGSRVLVVRGMDGMDEISVCTPTEVVTVDAAGRTGEEVINPRNVGLDFYEDGSLVGGDAEYNADVAVRLMKGEISGAIKDAVLINAAGALTAVRGWEENGFQETLREQVQIAREALESGAALKQMEKIVGKEF | 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 1-diphosphate + anthranilate
Sequence Mass (Da): 38878
Sequence Length: 367
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 2/5.
EC: 2.4.2.18
|
Q3Z6G6 | MIKEAIGSLVLGKSLTLEQSASVMDEIMEGKTTPAQIGAFLTALRVKGETAEEIAGLANVMRAKSTRISTSTPVLDIVGIGGDGINTFNISTTAAFVISGAGIKVAKHGNRAASSMCGSADVLEALGIKIDLNAEQVKICIEQIGIGFMFAPVFHPAMKFVAPSRREIGIRTVFNILGPLTNPASAQYQLIGVPEIGLGDKIISALCHMDIKHALVVHGLDGMDEMSISGDSVIWELKDKEIIKFRHTVSPREMGLEQVSLQAVKGGAAEENALTLRAILSGAKGPKRDVVLLNAAAALMVADKIDTIAEGISLAAEIIDNGLALNKLESLIKLSQSLASG | 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 1-diphosphate + anthranilate
Sequence Mass (Da): 35748
Sequence Length: 341
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 2/5.
EC: 2.4.2.18
|
Q9RTJ5 | MQAQPIHARLMNGEVLSQDDATAFMREVMSGDMSGVRMAAALAALRVRGETPEEIAGFAQAMRESAVTVKVRPRDVLMDVVGTGGDGAHTFNISTTTAFVLAGAGVPIAKHGNRAASSRAGSADVLEALGVNLDASPEVIQEAIDTLGVGFMFARNYHPALRHAAPVRSDLAARTVFNILGPLSNPAGATHLVVGVFRADLTRTLAEALRHLGAKGATVVYGDGLDEFTVCGPNTVSGLRDGEIIDRTMHPEEFGVDLHPKTAIVGGSPAENAEITHALLTGGGTPAQKDIVALNAGAALRTAGRVGTIREGVEQAREVMKGGQGWEMLQKYGALTKR | 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 1-diphosphate + anthranilate
Sequence Mass (Da): 35288
Sequence Length: 338
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 2/5.
EC: 2.4.2.18
|
B1I3Z8 | MIREALQKLVGGEDLEQHEAEAVMAEIMDGEATSAQIGALLAGLRLKKETAAEIRGFARAMRARAEQVPTRHELVADTCGTGGDGAQTFNISTTAAFVVAGAGVPVAKHGNTAVSSRCGSADVLRHLGVNLDLTPAQMGACLDEVGIAFLFAPRLHRAMQHAAGPRKELGIRTVFNILGPLTNPVRPRVQVLGVFDAAVAELVADALAGLEVERAFVIHGAGRLDEVSLAGPAQVWEVRPGSVRAGILDPVDLGFERADVESLSGGSPADNARITLEILHGASGPRRDAVLLNAGLALLAAGRAGDAAGAVRLAAESLDSGAARERLTRLIEFTERCKHVEHDNRL | 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 1-diphosphate + anthranilate
Sequence Mass (Da): 36199
Sequence Length: 346
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 2/5.
EC: 2.4.2.18
|
Q24SK4 | MTYAIHESLTLLSQKQDLPEELTFTVVQDLLSGELTPAQIGGLLLGLSLKGETPEEIAAFAQALRGAGLKIKAPAGTLDTCGTGGDRSGTFNISTTAAFVIAGAGVPVAKHGNRFASGRCGSADVLEQLGISLKATPESSERHLQHIGMTFLFAQVYHPAMAKVAAERRELGIRTIFNLLGPLLNPAGAPYQLLGVSSPSLLPKMAKALQILGSKRAVVAVGEDGLDEVTLTGATQAILIDGGEIQPFIIRPEEYGLNLCSLQDLQGGTPAENGQITLRILQGKKGPQRDIVLLNAGTALYAANKAAGIREGIALAAESLDSGKALSILEKLKASA | 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 1-diphosphate + anthranilate
Sequence Mass (Da): 34950
Sequence Length: 336
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 2/5.
EC: 2.4.2.18
|
A8ZZX1 | MFSQTLSKIINRKDLSREEMDRIFSDIFSGNLTDAQIGAFMAALATKGETFEELAGAAEAMRRKATRIQAASPVVVDTCGTGGDGAHTFNISTTSAFVVAGAGICVAKHGNRSVSSKCGSADVLEALGVKLDTQPEVAEEAVNEIGIGFLFAPLFHGAMKYAIVPRKELGVRTIFNMLGPLTNPAAANCQVLGVFAPQLTEMFADALNLLGARRAFVVHGHDGLDEISVCASTRVSELNDGRVQTYDISPEHFFEDRARPEDMAGGTPSENAQITRHILSGKEKGPRRNVVVVNAGAALVAAGKAEDLKAGVALAGQIIDSGKAHEKLEQLIEFTKSNG | 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 1-diphosphate + anthranilate
Sequence Mass (Da): 35858
Sequence Length: 339
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 2/5.
EC: 2.4.2.18
|
Q6AMS5 | MAVTLGKNNMNIRQAIARVVTGADLSESEMMASMEEVMSGQASPAQIASFITALRMKGEAVEEIVGAVRVMRDKATFIDCGLGPDDILMDIVGTGGDGADTFNVSTTTSFVVAAAGVAVAKHGNRAVSSRCGSADVLEALGVDLSLDPATVARSVQEIGIGFLFAPLLHAAMKHAIVPRREMGIRTIFNILGPLTNPAGANVQLIGVFERSLTTVLAEVLLRLGERRSLVVWGEGNMDEMTVTGTSYIADAHDGRVTSYAVEPEDVGLARAAVADISGGRTPEESAQQVRAVLAGEKGARLDMVLLNAGAALLAAGRVETIVEGVVMARDVVESGAALKKLGQLVAFR | 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 1-diphosphate + anthranilate
Sequence Mass (Da): 36258
Sequence Length: 348
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 2/5.
EC: 2.4.2.18
|
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 (Da): 4460
Sequence Length: 39
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 2/5.
EC: 2.4.2.18
|
A1ALX3 | MIKKAIARIVEQKDLTEGEMIEVMGQIMTGEATPAQIGAFITALRMKGETIDEITGAARVMREHATRIRAGKDLLDIDRDDINIDRETILDVVGTGGDGTNTFNVSTTVAFVVSACGVKVAKHGNRSVSSLCGSADVLEKLGVNLDITPETVEQCITKIGIGFLFAPALHGAMRYAIGPRREIGIRTIFNILGPLTNPAGADCQVMGVYRPGLVEKLAGVLHRLGCRHGFVVHGMDGMDEITTTTETLIAEVTTSGVSICTIHPEELGFSRCSMDELRGGDATANADIVRSVLQGVAGPRRDIVLINAAYALVAADRAATPEQAIALAAEAIDSGRAMEQLRKLIQITKD | 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 1-diphosphate + anthranilate
Sequence Mass (Da): 37249
Sequence Length: 350
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 2/5.
EC: 2.4.2.18
|
A5D1S5 | MIKNAIKKVVSGQHLSEEEAGAVMEQIMEGGASPAQIASLLTAMRLKGETVDEITGFARVMRQKSTRVKSKHPVLVDTCGTGGDGAGTFNISTAAAFVVAGAGVPVAKHGNRSVSSRCGSADVLEELGVRVDLDREAVEECLNMVGMAFLFAPLLHRSMGYVAGPRREIGIRTVFNILGPLTNPAGANAQVLGVYSPFLAEMLAKVLARLGVSRAFVVHGAGGLDEISLAGPSILCEVRNGSVRRGLLDPARFGFRYAPVSVLAGGTPRENAAIALKILEGERGARRDVVVLNAALGLVAGGKARNIAEGLEIAALSIDSGLAVAKLRELVEFTGNLSCGEAAVR | 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 1-diphosphate + anthranilate
Sequence Mass (Da): 35864
Sequence Length: 345
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 2/5.
EC: 2.4.2.18
|
Q4FM53 | MRVFIDKLKDKQDLSFAESKNAFEILMNGKASDDEIFDFLTLLSSKGESSDEIAGGVFVLRDKSKRVNVDDCIDTCGTGGDGMNTLNISTASALLLSSMGIKVAKHGNKAVSSKCGSGDVLEALNIKIDLEPKDIEEQIKKNNFGFMFAPNYHSAMRFVGPTRKKIGKRTIFNMIGPLSSPALVDRQVIGVFDKKLLKIFANALNNLDIKFAWIVNSEDGLDEISPYSKTNVVQLKDGKISEMLIDPIKLNIGANKFENLLGDDAKFNANKMLDIFKGEDNDFSKAVCLNAAAGLIVSEKYTIFIDAYNEARTHILSGKTYNDLKEIQNV | 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 1-diphosphate + anthranilate
Sequence Mass (Da): 36315
Sequence Length: 330
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 2/5.
EC: 2.4.2.18
|
C0QR68 | MIKEYIRKITEGKDLSADEMKDLFNILMEGQATDAQIGAVLIGLKMKGESVEEISSAAQIMREKAVKVPVKDRSRLIDTCGTGGDKVDTFNVSTITAFVIAGAGVKVAKHGNRSVSSKCGSADIMEALGVKIDLSPEQAAEAIDRIGLGFLFAPVYHPAMKNVIRQRREIGVRTIFNILGPLSNPAGAKYQLLGVYDKDLVEPVARVLSLLGIERAYVVHGMEGLDEVSITTDTMVAEVDGGDISVYSVKPEDFGIERASLDDIRGGDLDFNLQIALDILEGKDRSRKTDFVSLNAGFAFHAVGVVDSVKEGIELAKETIYSKKAYEILEKLREYSKGG | 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 1-diphosphate + anthranilate
Sequence Mass (Da): 36733
Sequence Length: 339
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 2/5.
EC: 2.4.2.18
|
A9BHQ6 | MFNYYLQKVVKGENLSLDEMEQAMEMIMEGKVTHSQLSGFLVALHMKGETVEEITASAKVMKEKATPISIESGELMDTCGTGGDAKGTFNISTAVAFILAAAGVVVAKHGNRSVSSKSGSADVLESLGINISLPPSSVERCLKEINIAFLFAQDFHKATKHAAVPRKELGIRTIFNVLGPLTNPANIKYQLMGIYDPKLVYPIAEVLNNLGVKRAMVVHGSEGIDEFSLSGKNKVAFLNEGKIEKLEISPEDLGLEKYSIQEIQGGSAEENKRIILNIFNGEMGPKRDVVVLNTAAGLYVANKVNSLEEGINFAQEIIDSGKAMKKLEEMVEFTNFLSLQAKTS | 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 1-diphosphate + anthranilate
Sequence Mass (Da): 37333
Sequence Length: 344
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 2/5.
EC: 2.4.2.18
|
Q7N488 | MQAIFNKLFNAQTLTQQESQQLFAAIIQGELSEPQLAAVLISMKLRGEQPQEIAGAAQALLANALPFPRPDYTFCDIVGTGGDGANSINISTASAFVASACQIKIAKHGNRSVSSQSGSSDLLAAFGIALDISAECARSALDEIGICFLFAPHYHLGFCHAMPVRQQLKTRTIFNILGPLINPARPPLALIGVYSPELVEPIARTLLVLGYQRAAVVHSGGMDEVALHAPTKVAEINDGEIIHYQLNAEDFGLQRHPMSALKGGSPVDNHEMLSLLLQGRGKKAHADAVAANVALLMKIHGQEDLRHNTQQALETIHSGRAYERVIALATRS | 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 1-diphosphate + anthranilate
Sequence Mass (Da): 35577
Sequence Length: 332
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 2/5.
EC: 2.4.2.18
|
Q5V448 | MQSVETDRTTFTDLAADAHPAARVPVEVRVDVDDPFLAYRRARDETGGVYLATTGGQSGWGYFGTAPADFREVDPRAGGTLAALTEFLDGERLVRGDCDVPYPCGAVGWLSYDVARELESLPDSADADRALPNLQVARYDRFAAWEEPRGESVTLRVTACPRVDDFETPELAYEFGKQHALDLARAAAQGDPSVEDPPVETDEATFESDCTRESFADRVQTVKQYIRDGDTFQANVSQRLRAPAAVHPVEAFDALRTVNPAPYSALLEFPGVDLVSASPELLLHRDGDRIETEPIAGTRPRGETPDADDRLETDLLDDEKERAEHAMLVDLERNDLGKVSKFGSVEVSDYRRVDRYSEVMHLVSVVEGRLRDGASLQDAIAAVFPGGTITGAPKPRTMEIIDEVEATRRGPYTGSIGLFGFDGRATLNIVIRTLVRYAEEYHLRVGAGVVHDSDPDREYQETLDKGRALVNAVDEALGRRVDLAMEDQQ | 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 | MTLDISREEFVEHAKADRPVVVRTAAELDVDVEPLTAYAALTGRTSDVAANDYTFLLESAEKVASSDPDGAFAPETDDRHARFSFVGYDPRAVVTVTGDESEVEAFDDRYADLVTTDGGDVVDDLRAAMPDVALRNFPAMDRQHLEGGLVGFLSYDAVYDLWLDEVGLDRPDSRFPDAQFVLTTSTVRFDHVEDTVSLVFTPVVRQGEDAGERYGELVAEAERVEAVLSDLSPLSTGGFRREDEVAGPRDEYEDAVERAKEYVLSGDIYQGVISRTRELYGDVDPLGFYEALRAVNPSPYMYLLGYDDLTIVGASPETLVSVAGDHVVSNPIAGTCPRGNSPVEDRRLAGEMLADGKERAEHTMLVDLARNDVRRVAEAGSVRVPEFMNVLKYSHVQHIESTVTGRLAEDKDAFDAARATFPAGTLSGAPKIRAMEIIDELERSPRGPYGGGVGYFDWDGDTDFAIVIRSATVEDEGDRDRITVQAGAGIVADSDPESEYVETEQKMDGVLTALEEIEGEPVDVAERAAGHEEVTR | 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 | MTEIRFSTDKESFIETARAAADGTRVPVEARVTVADPFEAYRRARDENTDGFYLETTGGQSGWGYFGIEPIERVEVSAGATPAQDGGSPSLEAIDDLLDREHLERGDCTVPYPCGAFGWLSYDVARELEDIPETTVSDGLPRLQFGVFDCIAAWEEPHDGNVEIHVTACPTVDGSPESAFERGRTMARELAQDAIHGEKHVQSQPTAASQATFESECGEAAFADRVRQIKQYVRDGDTFQTNVSHRLTAPAAVHPVDTFDAVRRVNPAPYSALLEFPGVDLVSASPELLLDVDGDQLLTEPIAGTRPRGATPSEDEDLEVDLCSDEKERAEHAMLVDLERNDLGKVSEYGSVDVAEYRRVDRYSEVMHLVSLIEGELRDAVSIADAVAAVFPGGTITGAPKPRTMEIIDEVERTRRGPYTGSIGMFGFDDRATLNITIRTLVHYDDEYRLRVGSGIVHDSVPEAEYRETLDKARALVTAVDEALGEQGSFAVESETEPMEGMR | 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 | MFYPTLDEVKIMAKDYNIIPVTMEVYADMETPISLFKRFEESSCCFLLESVEGGEKWARYSIIGKNPFLVVESYKNKTIIRERNGSQREVEGNPVEIIKGIMGKFKGANLPNLPRFNGGAVGYFGYDLIRHYENLPNVPEDDMGLPECHFMFTDEVLVYDHLKQKIHIIVNLHVNGNIERAYISAVDRIKTIHREILDTRWKTADNSVLSYNKKKNELAVTSNISKEDFCRNVLKAKQYIRDGDIFQVVLSQRLCVETNENPFNIYRALRVINPSPYMYYLKFGGYRIIGSSPEMLVRVENGIVETCPIAGTRKRGRTKEEDEALEKELLSDEKEIAEHVMLVDLGRNDIGRVSKFGTVAVKNLMHIERYSHVMHVVTNVQGEIREDKTPFDALMSILPAGTLSGAPKVRAMEIIDELETVKRGPYGGAIGYLSFNGNLDSCITIRTIILKDGKAYVQAGAGIVADSVPEREYEECYNKAMALLKAIEEAGEIR | 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 amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly from chorismate and high concentrations of ammonia (By similarity).
Catalytic Activity: chorismate + L-glutamine = anthranilate + H(+) + L-glutamate + pyruvate
Sequence Mass (Da): 56020
Sequence Length: 494
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 1/5.
EC: 4.1.3.27
|
Q9Y8T0 | MPSPPEPPLHWRDCRLEPILGFPRPRELAKSLEVQGEEWIALLESGGGLQHRSRYSFLAWGRRKSSETDAIRAYEELERLADDKCRALPCRSPTFFLVSYEAVVGEEPWLSRLVGRHEWPGMTAFSPEYVVVYDHAGGRVSVCPGDTPLPAPASRKESFSAEGPTYETSRKGFEAMVADALERIRAGEAFQVVLSRVERYRVWGSLFSAYERLADANPSPYLYYARLGGRVIIGSSPELLVKLEAGRVETHPIAGTRPRGSTPIEDIELEVELLNDEKERAEHVMLVDLARNDITRVSIPGTVQVTSFMDIERYETVMHIVSRVEGVTRPSTTFVEALKALHPAGTVSGAPKPRAMEIIAELEEEARGPYAGAIGVAGSSAGEAAIVLRSAWLLDDGETLEARAGAGIVYDSKPEREYMETVQKLGSLKRALGVDMCG | 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 amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly from chorismate and high concentrations of ammonia (By similarity).
Catalytic Activity: chorismate + L-glutamine = anthranilate + H(+) + L-glutamate + pyruvate
Sequence Mass (Da): 48310
Sequence Length: 438
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 1/5.
EC: 4.1.3.27
|
O66849 | MNLNLSLEEVRKLSENYNVIPLYTELLVDTETPLSIFLKLKEKGQFNILLESAEGGEKWGRYSFIITGSSFYLRTRKDIGEIYERGKVNFFETKDPLSKIKEVVKKFIPYHDERLPRFWGGLVGYFAYDVVKFYEPVEDKNPDPIHTYDIYLVLTDVVVIHDNLTGKIKVVVPIFAQNGIEEEYERAKNLIRDTVKKLKERGTTFLNVVEKEPDFKNWRSNFTKEEFEDIVKKAKEYIAQGDVIQVVLSQRFRKRFKGNPDNIYRVLRFLNPSPYMYYLDFDQLKVIGSSPEILVRLEEGRIETRPIAGTRKRGRTEEEDKRLEEDLLSDEKERAEHLMLVDLARNDIGRVAKTGSVRVENFMRIERYSHVMHIVSDVVGELREGYDALDVLKATFPAGTVSGAPKVRAMQIIEELENERRGIYAGSVGYISFQGNMDMAIAIRTAVYRDRDIFVQAGAGIVADSVPEKEWEETVNKAKALMKAIEIAEESQEE | 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 amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly from chorismate and high concentrations of ammonia (By similarity).
Catalytic Activity: chorismate + L-glutamine = anthranilate + H(+) + L-glutamate + pyruvate
Sequence Mass (Da): 57087
Sequence Length: 494
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 1/5.
EC: 4.1.3.27
|
P32068 | MSSSMNVATMQALTFSRRLLPSVASRYLSSSSVTVTGYSGRSSAYAPSFRSIKCVSVSPEASIVSDTKKLADASKSTNLIPIYRCIFSDQLTPVLAYRCLVKEDDREAPSFLFESVEPGSQMSSVGRYSVVGAQPAMEIVAKENKVIVMDHNNETMTEEFVEDPMEIPRKISEKWNPDPQLVQDLPDAFCGGWVGFFSYDTVRYVEKRKLPFSKAPEDDRNLPDMHLGLYDDVVVFDHVEKKAYVIHWIRLDGSLPYEKAYSNGMQHLENLVAKLHDIEPPKLAAGNVNLQTRQFGPSLDNSNVTCEEYKEAVVKAKEHILAGDIFQIVLSQRFERRTFADPFEVYRALRVVNPSPYMGYLQARGCILVASSPEILTKVKQNKIVNRPLAGTSKRGKNEVEDKRLEKELLENEKQCAEHIMLVDLGRNDVGKVTKYGSVKVEKLMNIERYSHVMHISSTVTGELQDGLTCWDVLRAALPVGTVSGAPKVKAMELIDELEPTRRGPYSGGFGGVSFTGDMDIALSLRTIVFPTACQYNTMYSYKDANKRREWVAYLQAGAGVVADSDPQDEHCECQNKAAGLARAIDLAESAFVKK | 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 amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS to produce anthranilate. Plays an important regulatory role in auxin production via the tryptophan-dependent biosynthetic pathway.
Catalytic Activity: chorismate + L-glutamine = anthranilate + H(+) + L-glutamate + pyruvate
Sequence Mass (Da): 66312
Sequence Length: 595
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 1/5.
Subcellular Location: Plastid
EC: 4.1.3.27
|
O28669 | MQKHEYVNPVKLYSAIRDEKFPFILESAEKSGRARYTYISFNPLYTVRVGSRTRVDGEVISKISDPFDALNEIHVKGLLVGYVAYEAVKNYIGKKPQTPSVFGCYDGYFVYDHYLRKLFSVNVENADKIVERAKRVEVEQVRGNSEVLRAGSREKFEKMVERGKEQIFEGEVYQIVLSREYVVDTDLSPFQMYLNLRETNPSPYMFLLEFDRALIGSSPETMGRVEGNSFIINPIAGTARREAGREKEIAEKLLSDEKERAEHVMLVDLARNDVRKVCRAGSVRVSRFMEVVEYPSVLHIESEVVGELKAGVTHFDAMKATFPAGTVTGAPKLRAIELIDEIEGDCRGVYAGAVGYFSENVSDLAIAIRMIEFDGKARIRAGAGIVADSVPEREFFETENKIARVLRAVGL | 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 amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly from chorismate and high concentrations of ammonia (By similarity).
Catalytic Activity: chorismate + L-glutamine = anthranilate + H(+) + L-glutamate + pyruvate
Sequence Mass (Da): 46346
Sequence Length: 411
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 1/5.
EC: 4.1.3.27
|
P50872 | MYPADLLASPDLLEPLRFQTRGGVTVTRRATALDPRTALDPVIDALDRRRGLLLSSGVEAPGRYRRHALGFTDPAVALTARGRTLRIDALNGRGQVLLPAVAEALRGLEALAGLEEAPSRVTASSASPAPLPGEERSRQPSVFSVLRAVLDLFAAPDDPLLGLYGAFAYDLAFQFEPIRQRLERPDDQRDLLLYLPDRLVALDPIAGLARLVAYEFITAAGSTEGLECGGRDHPYRPDTNAEAGCDHAPGDYQRVVESAKAAFRRGDLFEVVPGQTFAEPCADAPSSVFRRLRAANPAPYEAFVNLGRGEFLVAASPEMYVRVAGGRVETCPISGTVARGADALGDAAQVLRLLTSAKDAAELTMCTDVDRNDKARVCEPGSVRVIGRRMIELYSRLIHTVDHVEGRLRSGMDALDAFLTHSWAVTVTGAPKRWAMQFLEDTEQSPRRWYGGAFGRLGFDGGMDTGLTLRTIRMAEGVAYVRAGATLLSDSDPDAEDAECRLKAAAFRDAIRGTAAGAAPTLPAAPRGGEGRRVLLVDHDDSFVHTLADYLRQTGASVTTLRHSHARAALAERRPDLVVLSPGPGRPADFDVAGTIDAALALGLPVFGVCLGLQGMVERFGGALDVLPEPVHGKATEVRVLGGALFAGLPERLTVGRYHSLVARRDRLPADLTVTAETADGLVMAVEHRRLPLAAVQFHPESILSLDGGAGLALLGNVMDRLAAGALTDAAA | 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 | MGGNSQPHQEPRRVNNDPRAKQQKGNQVRRDRRDVHGWVVLDKPIGMTSTQAVAVLKRLFNAKRAGHAGTLDPLASGGLPIALGEATKTVPFVMDGRKRYQFTVCWGEERDTDDIEGRVTATSELRPTREAILALLPRFTGVIEQIPPRYSAIKIQGERAYDLARDGEVVELAPRPVEIHRLTLVDQPDNDRAVFEAECGKGTYVRALARDMGRILGTYGHICALRRTLVGPFGENDMIPLDQLEALCDRAASGEGSLADALLPVETALDDIPALAVTRADAARLHRGQAVLLRGRDAPTCSGTVYVTVAGRLLALAEVGNGEIIPKRVFNLTGLTASPGRNERN | 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 | MARRGKKKGRPISGWVIFDKPKGMGSTEAVSKIKWLFSAEKAGHAGTLDPLASGMLPIALGEATKTVPYAMDGTKVYRFTVTWGEERSTDDLEGQPTKTSDKRPSREEVEALLPDYTGVISQVPPQFSAIKIDGERAYDLAREGETVEIPAREVEIDRLEIVGFPDADRTEFEVECSKGTYVRSLARDMGRDLGCYGHISDLRRVEVAPFTDEDMVTLAKLEAVWPPLPPKDEDGNVIEPAPRRDFSALDALVIDTGAALDCLPQVPLSDDQAQRVRLGNPVILRGRDAPLEADEACVTTRGKLLAIGYIEHGQFKPKRVFTAG | 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 | MRPPRTTELDRPMTTAASQRPRVPRRLLDGVLLLDKPVGLSSNDALIRAKRLLLAKKAGHTGTLDPLASGLLPLCFGEATKFSQDLLEADKTYEATMRLGQRTATGDAEGEVIDTRPVECDRAAVEAALVRFTGEIVQVPPMYSALKRDGKPLYEYARAGQTVEREGRNVTILALALLACDLPDVTFRVTCSKGTYVRTLAEDIGEALGCGAHLTMLRRTGVGALTLEHAVTLDALSDADDASRDAWLQPVDALLSTFPLVRLDETSAKRFLHGQRLPLSALDPIDAAEGERVRVYDATRLLGVARKANGVLAPERLVVTAA | 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 | MLCLSLMRIFCSKCLEEQECPLPWELEKYEIWVKKEAETNEKWGEDPYNRPIERLLKYSVINLDKPSGPTSHQVVAWVRDIVGVKAGHGGTLDPKVTGVLPIAIGEATKVLQTLLIAGKEYVALMHLHKEVSEKDIIKVMSKFVGTIIQTPPLRSAVKKRPRKKKVYCIKIIEIDGKDVLFRVSTQGGVYIRKLIHDIGVKLGVGAHMQELRRIKSGPFHENNSVYLQDIVDSLYFWKEEGNEEYIRKVFLPVEEAVKHLKKIYILDSAVAAIVHGANLAVPGIAKLYSNIKKGDLVSIHTLKGELVAIGIALMDSKEMLEKKRGIAVDIERVFMKPGLYPKMWVSQG | 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 | MIEEIQKLNGFIVIDKPQGPTSHQVDYWVRQILGTEKVGHIGTLDPNVTGVLVMAIGKAVRLIDVVHEKPKEYVGVMRFHSDISEEEVREVFRKFTTRIYQLPPVRSAVSRKVRIKTIYELDMIEKKDKIVLFHVKCESGTYIRTLCTDIGYVSGKGGQMVDLRRISTGPFKEDIAITLQDLQAYVDLAKEGKDELFRSHFLDMTYAFIDYPKIVAKKSAVENIAHGSDLYVGGVKLIDGNFQKGDRVCVLSEDNELLGTGIARCDSSNLFMKVVDFDHIFVEAKHGKGDVVRDREKDVQRPGQQVHRNIRDAAHGPDSRTGRGRKETGPQIAPNRVRKLQNKTGVHRRPGSH | 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 | MELNKNLIIPFAKQAGLTSFASMSAVKKALSTKKVGHTGTLDLFADGLLVLLTGQLTRLADIISAEKKTYEAWVEFGTETDTLDPEGEPVLTAPLPSYKNLTESIPSFLGKILQRPPEFSAIKINGKRASDRIRSGEKIKIAEREIEIFKIELKGIITDSGLEFTEKDFTNINAELKIRYAHIVVECSKGTYIRSLVRDLARKASSCAYVRALRRTAVGNFKLEDAAGFDLLNNFSAAPENLFLKEKKILDAAAGKKFYKQKEIDFLEIMAKSIIFSPKTAENLKLPYLFLDRKYLNDFYNGKKIKFNWFLNTDEVLENITGLDLENKKTCVFCGDLWIGIIGLNKNCPKYETVIKN | 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 | MCRLSMPDAIVPFAKVSGLTSFAALAQVRRLLGVKKVGHTGTLDRFADGLLLLLVGGFTKLAPVMTRLEKSYEARIQFGVQTDTLDPEGAVVRCSLFPTFARVRAALPHFTGSIDQVPPEYSALKFGGVRASDRVRRGEAVCMKARRVFVFDLQVLGCEADLGEFKKTQAGRGAAIADLDLTRVRAVTLYVRCSAGFYVRALARDIAAACGSCAYVSHLRRTRIGPFDLAQAAGVSRLGSWTWGKERASCGAACFDVGAPPPPSSGGVATDSVSFGCEDLTVREIKQAVVSCDVDFANRIGLTACSVHAQYASRFLHGERIRACWFQSFGTRRPGERALVFSEGRCLGLIRKAANGFSYDAVFCTE | 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 | MLGKVERSEMYILFAMTQVLLVDKISGITSHTAVAKIRHLTGIKKIGHCGTLDPAACGLLIMGCGTATRLIRYMSNLDKRYIATITLGTQTTTDDSEGEIIYSAPKPSLDKITLESIGRAAEKLSGTIKQIPSAYSAIKVSGNRAYNLARQGIIPKLNAREVRVHWKFLGDFENNQVHVQITCSSGTYVRALARDMGKFLGVGGHLSYLKRLSIGPFHLHEIYREINKKEATMSERTPSGNTQGLTDNMAISESDKHDCTEPGINCTELGIKDTCTALREVHYTQGDTLSFTRLTALQALSRIYKPIEVSQKQADDLSCGRYISLGIDSKGPVCAVCKENLIAVIQPVSAGLWRPETVLSDNRKLNSNAAQDASGST | 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 | MPPASRTRVQRRPVHGVLLLDKPLALSSNQALQKAKWLLRAEKAGHTGTLDPLATGVLPLCFGAATKFSQLQLDAPKTYEAIALPGVTTSTGDAEGAVLQRCAVDPAQLAPERLSAVQRQFTGPISQLPPMHSALKKDGRALYTYARAGIALERAARAVVIHALELSLVQHAPAQTAIKIAVTCSKGCYIRTLAEDIGAALGCGAHLSALRRTDSGGIGIERCISLERLQALPEAERLACLQPPQSLLTRHLRVTLDSDNAARFLSGLPRRGAWPDAPAVAVFGADPPALLGVGHIAGGCLLPDRLLSALEIAQILASQPQRQDCGILEET | 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 | MSELHYLYGKPTGTADLRTVNSDFIVKEILPFSPSGEGEHHLVHIRKDGLNTVQVAEMLAKFAKVHPKEVTYAGQKDKNAITEQWFGIRIPGKETPAWIELNSDRLTVLSSSRHSKKLRIGALLGNRFILTLRNVTNVEDIISRIEKVSQIGVPNYFGEQRFGHDGKNLVLGRQMLAGKKVKDRNKRSMYLSAVRSHLFNTVVSYRLTHYGTRPLAGDCVMLAGSKSFFVTPEWDLVVLKRLIEKDIQLSAPLWGRGKMLPQGEAAEVETQAMADLTEDCYGLEHAGLEQERRPLLLEPQGLKHEQTSDGLVLEFILPAGCFATSLLRELVDYQDVKELQWQTTLTAETNVVTESNTAAANVSDNGESAS | 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 | MANYLTAKLPGIGGSIKTCPDDFLVEELPLYPTCGEGEHLYLEVEKRGMTTFELLKRLSRALQVNERAMGYAGLKDAQATTRQFISVTDCSAEQALALQLQDIRILSARRHRNKLRLGHLAGNRFTITIRDIDSDALEKARDILHVLQMTGVPNFFGEQRYGALGNSHLIGQAIVQKNFSQAAAHIIGDPDKIIHPEWRQGAILYAENRLEEAEQALPRRMRNERNLVRSLRQGRSAEKAVRRLPGKLLRLYLSAYQSHLFDRLVSMRLESLETLWTGDIAYKHDNGACFLVTDAALEQPRADRFEISPTAPLFGHKVMMAEAQAGILEQALLAKEGITPDDFRLGAGLSMPGERRPLRIPISETASNQQGNELELSFSLPKGSFATTVLHEVMKTDV | 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 | MLLSTFKRHLPIRRLFSSNKFDLIVIGAGSGGLSCSKRAADLGANVALIDAVEPTPHGHSWGIGGTCANVGCIPKKLMHQAAIVGKELKHADKYGWNGIDQEKIKHDWNVLSKNVNDRVKANNWIYRVQLNQKKINYFNAYAEFVDKDKIVITGTDKNKTKNFLSAPNVVISTGLRPKYPNIPGAELGITSDDLFTLASVPGKTLIVGGGYVALECAGFLSAFNQNVEVLVRSIPLKGFDRDCVHFVMEHLKTTGVKVKEHVEVERVEAVGSKKKVTFTGNGGVEEYDTVIWAAGRVPNLKSLNLDNAGVRTDKRSGKILADEFDRASCNGVYAVGDIVQDRQELTPLAIQSGKLLADRLFSNSKQIVRFDGVATTVFTPLELSTVGLTEEEAIQKHGEDSIEVFHSHFTPFEYVVPQNKDSGFCYVKAVCTRDESQKILGLHFVGPNAAEVIQGYAVAFRVGISMSDLQNTIAIHPCSSEEFVKLHITKRSGQDPRTQGCCG | 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 | MAAMAVALRGLGGRFRWRTQAVAGGVRGAARGAAAGQRDYDLLVVGGGSGGLACAKEAAQLGRKVAVVDYVEPSPQGTRWGLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEVAQPVPHDWRKMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVCGVAKGGKEILLSADHIIIATGGRPRYPTHIEGALEYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMRSIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDGQLQVTWEDSTTGKEDTGTFDTVLWAIGRVPDTRSLNLEKAGVDTSPDTQKILVDSREATSVPHIYAIGDVVEGRPELTPIAIMAGRLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSEEEAVARHGQEHVEVYHAHYKPLEFTVAGRDASQCYVKMVCLREPPQLVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSEEVVKLRISKRSGLDPTVTGCUG | 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 Mass (Da): 56507
Sequence Length: 524
Subcellular Location: Mitochondrion
EC: 1.8.1.9
|
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.