ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
O34522 | MRMRHKPWADDFLAENADIAISNPADYKGKWNTVFGNDNPIHIEVGTGKGQFISGMAKQNPDINYIGIELFKSVIVTAVQKVKDSEAQNVKLLNIDADTLTDVFEPGEVKRVYLNFSDPWPKKRHEKRRLTYSHFLKKYEEVMGKGGSIHFKTDNRGLFEYSLKSFSEYGLLLTYVSLDLHNSNLEGNIMTEYEEKFSALGQPIYRAEVEWRT | Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 24504
Sequence Length: 213
Pathway: tRNA modification; N(7)-methylguanine-tRNA bi... |
Q8A0X7 | MGKNKLEKFADMASYPHVFEYPYSAVDNVPFDMKGKWHQEFFGNDHPIVLELGCGRGEYTVGLGRMFPDKNFIAVDIKGSRMWTGATESLQAGMKNVAFLRTNIEIIERFFAAGEVSEIWLTFSDPQMKKATKRLTSTYFMERYRKFLKPDGIIHLKTDSNFMFTYTKYMIEANQLPVEFITEDLYHSDLVDDILSIKTYYEQQWLDRGLNIKYIKFRLPQEGVLQEPDVEIELDPYRSYNRSKRSGLQTSK | Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 29494
Sequence Length: 252
Pathway: tRNA modification; N(7)-methylguanine-tRNA bi... |
A9KLV5 | MRLRNIPGSREYIAQNDYVVHDPEQKKGKWHEVFGNNNPIHIEIGMGKGQFITSLAMQNPNINYIGIEKYSSVLLRAIEKREEYEGDNLYFLRFDAESITDIFAPSEVDRIYLNFSDPWPKDRHSKRRLTSSEFLARYDQFLVKDGYVAFKTDNRDLFDFSLEQVTLSGWQLRDVTFDLHHSEYVEGNIMTEYEERFSSMGNPIHRLVAFREKE | Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 25288
Sequence Length: 214
Pathway: tRNA modification; N(7)-methylguanine-tRNA bi... |
Q88WZ9 | MRVRNKPWAPKLIAAHPELITEDPTQLKGRWQSRFAKPQPLQIEVGSGKGQFIIEMAKRHPEINYVAIEIQTSVIAIILKKLVEAPLPNLQLAHADGQAVTAFFEPHEVDRLYLNFSDPWPKSRHEKRRLTYKSFLSSYREVLKPNGQIEFKTDNRGLFEFSLTSMNNFGMQFEQVWLDLHAVATPEDNVETEYEQKFSAAGPIYKIIATFPAK | Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 24606
Sequence Length: 214
Pathway: tRNA modification; N(7)-methylguanine-tRNA bi... |
Q8F9Q1 | MVQDLEQKLWSIASGIPFSSDYFLQASPIRKLKKENLFSKVFETYFLELGSGWGEVAISMALQRPNTGFILMEKKFDRIRHTIREIEKHSLDNVKILCVNFNWFLEEVFEENLFSEILLNFPDPWPKKRHHKKRTVNSKFLESLKILLPEKGKFYFATDYGPYARKVIRLFRDSKAFSPEKVELKSERNEIPVSHFERKKREEGKRIYYIDRVLVQK | Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 25913
Sequence Length: 217
Pathway: tRNA modification; N(7)-methylguanine-tRNA bi... |
Q03WU9 | MHLRSKPWASDWLAEHSDIVIDQDRATAQIGQWQSLFDQEQPIHLEIGSGKGQFILGMALAHPEINYIGMEIQETAIAIAARKSFDQVGTLPNLRYIYGNGNGVETYFEKGEVSKVYLNFSDPWPKKRHESRRLTYKSFLKSYEAVLPEHGEVEFKTDNRHLFEYSMVSFMDYGMRWTPEDYTLDLHADEDKVQGNVETEYEQKFMAKGQPIYKIKAHF | Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 25462
Sequence Length: 219
Pathway: tRNA modification; N(7)-methylguanine-tRNA bi... |
P59721 | MSDSLHTPEEPRPGPGEQLAHAHDGSLRHTRAKGEPRFPDGPKADPAGSHFERRIRSFQPRRSRVTAGQADALQRLWPKWGLDIDGHALDLTELFGNTHPVVLEIGFGMGEATARMAAEDPDTGILAVDVHTPGQGNLLNLADQHGLTNIRVANGDAIILLREMLPPDSLDGLRVYFPDPWPKKRHHKRRLIQPEFLTLAATRLRPGALVHCATDWEPYAEQMLDVLTAHPDFENTQPTGGYAPRPGFRPLTRFEGQGLDKGHVVNDLLFRRVQPRDQHRDLPPSATEAD | Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 32245
Sequence Length: 290
Pathway: tRNA modification; N(7)-methylguanine-tRNA bi... |
Q9F305 | MSDSHHTPEAASASLRHVRAKGEPRFPDGPKADPAGSHFERRIRSFQPRRSRVTAGQADALQRLWPLWGLDIDGRRVVDLAELFGNARPVVLEIGFGMGETTARMAAADPDTNILAADVHTPGQGNLLGLAERQELPNIRVANGDAIILLREMLAPGSLAGLRVYFPDPWPKKRHHKRRLIQPEFLTLAATRLAPGAVVHCATDWEPYAEQMLDVLTAHPDFENTVPGGGFAPRPEHRPLTRFEGQGLDKGHVVNDLLFRRVQHKEPPPNG | Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 29912
Sequence Length: 271
Pathway: tRNA modification; N(7)-methylguanine-tRNA bi... |
Q28UF1 | MTEHPRLAKAWCAKVITLFPETFPGVLGASLTGKALQKGLWALEPIDLRTFGTGKHRQVDDTPAGGGAGLVLKPDVMARALDIAARGTPADRADWPIVYLSPRGKPFEQRDAERFASAKGITLVCGRFEGVDQRVIDAYGMEEICVGDAVLTGGEIAAQLVLDATTRLIPGVLGNADSTQEESFSDGLLEHPQYTKPADWRGHTIPPVLLSGDHGKVAEWRKAQAEALTQERRPDLWVKVAKPKKPR | Function: Specifically methylates guanosine-37 in various tRNAs.
Catalytic Activity: guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 26778
Sequence Length: 247
Subcellular Location: Cytoplasm
EC: 2.1.1.228
|
A6W7V0 | MRLDVVTIFGEYLQPLQLSLIGKAQAQGLLDVRVRDLREHTHDRHRTVDDTPYGGGAGLLMKPEPWGEALDAVLADPPEDADPRGPVLVVPSPVGEVFTQRAAVELAAEPWLVFACGRYEGIDARVVEHYRTRVRVREVSLGDYVLNGGEVAVLAITEAVARLLPGVIGNAASLTEESHAPEHDGLLEHPAYTKPASWRGLDVPAVLAGGNHAAVERWRRDEALRRTATRRPDVLARLDPERCDARDLAVLAELGWTPDGSGFRAGGDPVADSSDTNEP | Function: Specifically methylates guanosine-37 in various tRNAs.
Catalytic Activity: guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 30255
Sequence Length: 279
Subcellular Location: Cytoplasm
EC: 2.1.1.228
|
B2GFY4 | MRIDVLSIFPEYLEPLKLSLIGKAVTDGLLQLQVTDPREFATDRHRTVDDTPYGGGAGMVMKPEPWARALESVLRAGSDTTARSGSTAATSASAQQATRLGPDDDAAQPGDAGQGTAAPDYARTGGTPGAGRAASSRPVLVVPSPAGEVFTQEVAYELAEEEHLVFACGRYEGIDERFIEWARDEVRVRPLSLGDYVLNGGEVAVLAMVEAVTRLVPGVIGNPESLDEESHTGGLLEYPVYTKPAQWRERTVPDTLLSGHHGRIARWRRDQQLERTARRRPDMVLALDPATLDRADLAVLAAEGFTLRDGQWQRCSPAPS... | Function: Specifically methylates guanosine-37 in various tRNAs.
Catalytic Activity: guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 35752
Sequence Length: 331
Subcellular Location: Cytoplasm
EC: 2.1.1.228
|
Q1IMM4 | MKIDLITIFPEFFRGPLDHGIVSRAQKAGLVEITIRDLREFTHDRHRTVDDRPFGGGEGMVLKPEPIFECLEAMEIPPRGNRENVQVLVLSPQGRLFDQTMALELSKLDRLVLINGRYEGVDERVSEVLADGEISVGDFVLSGGELGSAIIVDAVTRLLPGALGNADSARQESFTAVAKEISEGPDSTCASGGLLDYPHYTRPAEFRGYVVPQVLQDGNHAEIQRWRRRRALEKTFKNRPDLLEGAELSKEDQKYLAQLRAGKD | Function: Specifically methylates guanosine-37 in various tRNAs.
Catalytic Activity: guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 29366
Sequence Length: 264
Subcellular Location: Cytoplasm
EC: 2.1.1.228
|
Q5FJK7 | MKINILTLFPDMFTPLQVSMLGRGLEDGKWDLNLVNFRDFTTDLHHHVDDTPYGGGAGMVLQIMPIKKALDSLPSTGKIIITAPQGKTFNEKMAQEWAKEDELTFICGHYEGFDQRVYDLADETVSIGDYVLTGGELPTMSMVDATVRLLPGILGNSASSVEESFSHGLLEYPQYTRPADFEGKKSARSFKPVVIIKRLLNGDTIRLLKATYLHRPDMLENRNLSDEEKKMLQEIKNEMNED | Function: Specifically methylates guanosine-37 in various tRNAs.
Catalytic Activity: guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 27258
Sequence Length: 242
Subcellular Location: Cytoplasm
EC: 2.1.1.228
|
B3WEU0 | MQIDVLSLFPNMFEPLRESMIGKAIERELLNFDVVDYRSYSHDKHHHVDDTPYGGGAGMLLKPEPLFEAMDGVNERHPGPKRVILMDPAGKKFNHQAARALSQEDHLVFICGHYEGYDERIRTLVTDEYSLGDYVLTGGELPAMVMIDAIVRLLPGVLGNDESAHTDSFENGLLEYPQYTRPPEYRGMKVPEVLQNGNHQLIARWRQKESLRRTYLRRPDLLKTITLDQTAQKLLREVKTEEATKAAEARLKNQS | Function: Specifically methylates guanosine-37 in various tRNAs.
Catalytic Activity: guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 29142
Sequence Length: 255
Subcellular Location: Cytoplasm
EC: 2.1.1.228
|
Q9CFB7 | MRIDILSIFPEMFGPLNQSIVGKAQDKGILELHTHDFRENATNKQRHVDDMPYGGGQGMLLMPQPIFDTMDKIPQKPEKPARVILLDPAGKKFDQKMAEELSQEEQLIFICGHYEGYDERIKTLVTDEISLGDFVLTGGEVAATVMVDAVVRLIPGVLGKVASHEDDSFSSGLLEYPQYTRPEDFRGMKVPEVLMSGHHENIRKWRLKESLRKTLERRPDLLDKYEPNEEELKMLQLLRENVQDVVE | Function: Specifically methylates guanosine-37 in various tRNAs.
Catalytic Activity: guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 28245
Sequence Length: 247
Subcellular Location: Cytoplasm
EC: 2.1.1.228
|
Q8CQL4 | MKIDYLTLFPEMFEGVLNHSILKRAQDKGIINVNTINFRDYSINKHNQVDDYPFGGGQGMVLKPEPVFNAMEDINHNEHTRVILMCPQGRPFTQEIAQELSEAKHIVFICGHYEGYDERIRKHLVTDEISMGDYVLTGGELPAMTMTDAIVRLIPGVLGNQASHQDDSFSDGLLEFPQYTRPREYKNMSVPEVLLSGNHAHIDQWRHEQKLIRTYEKRPDLLEQYPLTEKDREILETYKKKLKND | Function: Specifically methylates guanosine-37 in various tRNAs.
Catalytic Activity: guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 28417
Sequence Length: 245
Subcellular Location: Cytoplasm
EC: 2.1.1.228
|
Q49X26 | MKIDFLTLFPEMFNGVLNQSILKRAQDKNMLTVNTVDFRHFAENKHNQVDDYPFGGGQGMVLKPEPIFNAMESIEKTDDTRVILMCPQGKPFTQAIANELSQSEHVVFICGHYEGYDERIREHLVTDEISMGDYVLTGGELPAMVMTDAIVRLLPGVLGNQQSHEDDSFQDGLLEFPQYTRPREYKGMSVPDVLLSGNHAHIDRWRHEQKILRTFVKRPDLLERYPMTVEEKDIVERYKKQLKKD | Function: Specifically methylates guanosine-37 in various tRNAs.
Catalytic Activity: guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 28330
Sequence Length: 245
Subcellular Location: Cytoplasm
EC: 2.1.1.228
|
P0A4P1 | MRLDVVTIFPEYLEPLNVSLVGKARARGQLGVHVHDLRDWTYDRHNTVDDTPYGGGPGMVMKTEPWGDALDSVLADGYETGCGEPALVVPTPSGRPFTQELAVHLSERPWLIFTPARYEGIDRRVVDEYATRMPVYEVSIGDYVLAGGEAAVLVVTEAVARLLPGVLGNAESHRDDSFAPGAMANLLEGPVHTKPPQWRGRGIPDVLLSGHHGKIARWRRDEALRRTTANRPDLIERCDPAAFDKKDREMLSILGWQPDPDGEPYGRFWRRTPGMEE | Function: Specifically methylates guanosine-37 in various tRNAs.
Catalytic Activity: guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 30828
Sequence Length: 277
Subcellular Location: Cytoplasm
EC: 2.1.1.228
|
B2FUB5 | MRFDVITLFPEFLAQSAGLGVVGRAQEKGLFSLHGWNPRDYAEGNYRRVDDRPFGGGPGMVMLIEPLQACLQAIRDADPTPARVIHLSPQGAPLTQAKVRELAALPRMVLLCGRYEGIDERFLEANVDEEISLGDYVLSGGELGAAVIIDAVARLQDGALNDAESAAQDSFEGDLGLLDCPHYSQPAQHPLGDVPDVLRSGNHAAIAAWRRQQSLVRTAQRRPDLLDEQALGKADRTLLEQGRQVQKQKADP | Function: Specifically methylates guanosine-37 in various tRNAs.
Catalytic Activity: guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 27452
Sequence Length: 252
Subcellular Location: Cytoplasm
EC: 2.1.1.228
|
Q9RXU7 | MSSPTITVVGAGLAGSEAALAAAKLGVRVRLFEMRPQKMTPAHRTANFAELVCSTSLGGEGEMQSKGLLQAEMRSVGAAIVTSADASRVPAGNALAVDRDAFSAHVTEQVKNHPLIEVVEGEVETVPDGICVIASGPLTADALASDLRRLTGSERLSFYDAAAPVIDVDSIDMDIAWRAGRYDQSADYINCPFTKEEYLAFFEALETARSHTPHDWEKLEFFEGCMPIEEIARRGVDTPRFGPMSPKGLDDPKTGRWPYAVAQLRQEDAEGRMWSLVGFQTGLKWGDQKAVVQLIPGLHNADIVRYGVMHRNTYLNAPEV... | Function: Catalyzes the folate-dependent formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNAs.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + H(+) + NADH + uridine(54) in tRNA = (6S)-5,6,7,8-tetrahydrofolate + 5-methyluridine(54) in tRNA + NAD(+)
Sequence Mass (Da): 50170
Sequence Len... |
B1I258 | MSGGVIVVGAGLAGAEASWQLVRRGVPVVLYEMRPRKCTPAHKTGDFAELVCSNSLRAEALTNAVGLLKEEMRRLGSLIMACADAHRVPAGGALAVDRQLFAAAVTERLTSHRLVTVCREEITTIPTAELVILATGPLTSDALADELRRLTGQEHLYFFDAVAPIVTLESIDQDRVFRSSRYGRGDPAYLNCPMSREEYERFWEALVAAERATRHTFERETHFEGCLPVEVIAARGRETLLYGPLKPVGLVDPRTGERPYAVVQLRQDNRAGTLYNLVGFQTNLKWGEQRRVFSMIPGLEQAEFVRYGVMHRNTYINAPV... | Function: Catalyzes the folate-dependent formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNAs.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + H(+) + NADH + uridine(54) in tRNA = (6S)-5,6,7,8-tetrahydrofolate + 5-methyluridine(54) in tRNA + NAD(+)
Sequence Mass (Da): 48337
Sequence Len... |
Q6ALS7 | MNNMNKVIIIGGGLAGSEAAWQAANRGCQVELVDMKPEKYSPAHSSPLLGELVCSNSLRSNDPTSAVGLMKREMRFFNSLIMDVADSTAVPAGKALAVDRDKFAEAITARLESHPNISISHREVTAVPEPADHPTIIATGPLTAEDFAESLAELTGRDRLAFYDAIAPILDSESLNMDIVYCKSRYDDGPGDYLNCPMNREEYERFISELASADYMPLKDFEDAKYFEGCLPVEVICSRGVDTLRFGPMKPVGLPDPRTGQDPYAVVQLRMENAEGSTYNMVGFQTKMTYPEQKRIFRMIPGMENVEFVRLGSIHRNTFI... | Function: Catalyzes the folate-dependent formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNAs.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + H(+) + NADH + uridine(54) in tRNA = (6S)-5,6,7,8-tetrahydrofolate + 5-methyluridine(54) in tRNA + NAD(+)
Sequence Mass (Da): 48848
Sequence Len... |
Q729K0 | MEDSLTTITTAAIIGAGLAGCECALRLARAGVRVTLFEMKPAAFSPAHSNPDLGELVCSNSLRSDDIASGVGLLKQEMRELGSIVMEAADATRVPAGKALAVDRDLFARHITAVIEAEPGITLERREVASLDDPALASADVVVIAAGPLASAGLSDSLAAVVGGQLYFYDAIAPIIAAESIDLSIVFSGSRYGEPGEEGDYLNCPMNRDEYDAFYEALLAAEKVPSRDFEKELHFEGCMPIEALAERGPRTLVFGPFKPVGFTDPRTGTRPYAIIQLRAENRNKTAFNIVGCQTKLKYAEQERVFRMIPGLAGAEFVRHG... | Function: Catalyzes the folate-dependent formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNAs.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + H(+) + NADH + uridine(54) in tRNA = (6S)-5,6,7,8-tetrahydrofolate + 5-methyluridine(54) in tRNA + NAD(+)
Sequence Mass (Da): 50947
Sequence Len... |
Q8REM9 | MEKEVIVVGAGLAGSEAAYQLAKRGIKVKLYEMKAKKKTPAHSKDYFSELVCSNSLGSDSLENASGLMKEELRILGSLLIEVADKNRVPAGQALAVDRDGFSEEVTKILKNTKNIEIIEEEFTEFPNDKIVIIASGPLTSDKLFQKISEITGEESLYFYDAAAPIVTFESIDMNKAYFQSRYGKGDGEYINCPMNKEEYYNFYNELIKAERAELKNFEKEKLFDACMPIEKIAMSGEKTMTFGPLKPKGLINPKTEKMDYAVVQLRQDDKEGKLYNIVGFQTNLKFGEQKRVFSMIPGLENAEFIRYGVMHRNTFINSTK... | Function: Catalyzes the folate-dependent formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNAs.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + H(+) + NADH + uridine(54) in tRNA = (6S)-5,6,7,8-tetrahydrofolate + 5-methyluridine(54) in tRNA + NAD(+)
Sequence Mass (Da): 49109
Sequence Len... |
Q39X89 | MTDAITIIGGGLAGCEAVWQAAERGVRVTLHEMKPHAFSPAHHLAGLAELVCSNSLRGESLENAVGLLKEELRRAGSLIMAAADATRVPAGGALAVDRELFSAFVTERIENHPLVDLMRGEVADIPSEDIVIVATGPLTSDGLAERIRAITGPNLYFYDAIAPIVTAESLDMTKVFRASRYGKGDGDDYLNCPLNQEEYEGFVDAILAAEKVPARDFEKVVHFEGCMPVEEMAERGRETLRFGPLKPVGLADPRTGEEPHAVVQLRAENREGTMFNLVGFQTKLTYPEQRRIFRMIPGLENAEFVRLGSMHRNTFINAPA... | Function: Catalyzes the folate-dependent formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNAs.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + H(+) + NADH + uridine(54) in tRNA = (6S)-5,6,7,8-tetrahydrofolate + 5-methyluridine(54) in tRNA + NAD(+)
Sequence Mass (Da): 47144
Sequence Len... |
Q74A44 | MTGAVTIIGGGLAGCEAAWQIAGRGVRVVLREMKPQRYSPAHHLSGLAELVCSNSLRGESLENAVGLLKEELRRAGSLIMAAADATRVPAGGALAVDRELFSSYVTERIEGHPLIELVREEVTELPAEGVLVIASGPLTSDALAERLKQITGDSLYFYDAIAPIVAADSLDSDKVFRASRYGKGDGDDYLNCPLSEEEYERFVDAVLAAEKVPARDFEKVVHFEGCMPVEEMAERGRETLRFGPLKPVGLTDPRTGREPHAVVQLRAENREGTLFNLVGFQTKLTWPEQRRVFRMIPGLESAEFVRLGSMHRNTFINAPT... | Function: Catalyzes the folate-dependent formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNAs.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + H(+) + NADH + uridine(54) in tRNA = (6S)-5,6,7,8-tetrahydrofolate + 5-methyluridine(54) in tRNA + NAD(+)
Sequence Mass (Da): 47290
Sequence Len... |
Q5NPP5 | MQPVNIIGGGLAGSEAAWQLASRQIPVRLFEMRGREKTPAHSTDKLAELVCSNSFRSDDPNSNAVGVLHAEMRKMGSLIMMIADQHRVPAGSALAVDREGFAEAVTNRLQNHPLIEIHRERIDHIPDETTIIASGPLTSDSLANAITELTGRDALSFFDAIAPIVYRDSIDMDIAWFQSRWDKGDGHDYINCPLNKEEYLAFHAALLAGEKGDFHEWEKDTPYFEGCMPIEVMADRGIDTLRFGPMKPVGLDDPRTGRWPYGAVQLRQDNALGTLWNMVGFQTKLKYAEQIRIFRMIPGLEKAEFARLGGMHRNSFIRSP... | Function: Catalyzes the folate-dependent formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNAs.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + H(+) + NADH + uridine(54) in tRNA = (6S)-5,6,7,8-tetrahydrofolate + 5-methyluridine(54) in tRNA + NAD(+)
Sequence Mass (Da): 49770
Sequence Len... |
O67577 | MVMEYLVLEKRLKRLREVLEKRQKDLIVFADNVKNEHNFSAIVRTCDAVGVLYLYYYHAEGKKAKINEGITQGSHKWVFIEKVDNPVQKLLEFKNRGFQIVATWLSKESVNFREVDYTKPTVLVVGNELQGVSPEIVEIADKKIVIPMYGMAQSLNVSVATGIILYEAQRQREEKGMYSRPSLSEEEIQKILKKWAYEDVIKERKRTLSTS | Function: Catalyzes the 2'-O methylation of guanosine at position 18 in tRNA. Type II methylase, which methylates only a subset of tRNA species.
Catalytic Activity: guanosine(18) in tRNA + S-adenosyl-L-methionine = 2'-O-methylguanosine(18) in tRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 24488
Sequence Le... |
C6X2D2 | MKPFRFKKFTVQQHKEVFRVGTDGVLLGALADVSDAKNILEVGTGTGLVALMTAQRNPTSNITAIDVNPVAAELAAKNFLESHFGHRMRAMHCDYKTFGTQKKFDLIISNPPYFETNPSEKDATARQQRELSFKTLISKTAEILATEGRFCVIIPFPAGPTFEKTCEENKLFLLRRITVYGNANVEPKRLILEFSSNKNISVSEEIFVTEKAPRVYSEQYLKATADFHEFE | Function: Specifically methylates the adenine in position 37 of tRNA(1)(Val) (anticodon cmo5UAC).
Catalytic Activity: adenosine(37) in tRNA1(Val) + S-adenosyl-L-methionine = H(+) + N(6)-methyladenosine(37) in tRNA1(Val) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 26032
Sequence Length: 231
Subcellular Location: Cyt... |
A5FKD7 | MFQFKQFSVKQDKTAMKVGTDGVLLGSWAPVFHNPFSILDIGAGTGIIALMLAQRTHAEQIDALEIDEDAYEQAVENFEASPWGDRLFCFHAGLDEFIEEPEDEYDLIVSNPPFYAEDYKTNDEQRDLARFQDAMPFEEIVEAADLLLSENGILAVIIPFKEEAKFTALAKDFELYPIKITRVKGTPKSEIKRSLLAFSRNEVSEIEIDELVIEIDRHIYTPEYIDLTKEFYLKM | Function: Specifically methylates the adenine in position 37 of tRNA(1)(Val) (anticodon cmo5UAC).
Catalytic Activity: adenosine(37) in tRNA1(Val) + S-adenosyl-L-methionine = H(+) + N(6)-methyladenosine(37) in tRNA1(Val) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 26917
Sequence Length: 235
Subcellular Location: Cyt... |
A6GWI6 | MFSFKQFSVQQDKTAMKVGTDGVLLGAWTPINHNPISILDIGAGTGLIALMLAQRTSAVQIDALEIDEEAYEQATDNFENSPWSDRLFCYHAGLDEFVEEPEDEYDLIVCNPPFYAENYKTNSEQRDLARFSDAMPFEELIEAADLLLSENGILSVIIPYKEEEKFVTLANEFELYPIKITRVKGTPTSETKRSLLVFSRNKQNCEQDILVIETDRHVYTKEYIALTKGFYLKM | Function: Specifically methylates the adenine in position 37 of tRNA(1)(Val) (anticodon cmo5UAC).
Catalytic Activity: adenosine(37) in tRNA1(Val) + S-adenosyl-L-methionine = H(+) + N(6)-methyladenosine(37) in tRNA1(Val) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 26705
Sequence Length: 234
Subcellular Location: Cyt... |
Q4QNC1 | MSGFTFKQFHINQDSCAMKVGTDGILLGAWADVKHCKNILDMGSGTGLLTLMLAQRTEENCQIQAVELDPIAAKQAQENINNSVWKNRIQLTQADIQHFLQTTEQTFDLIVANPPYFEQGIACKNEERELARYTKQSHLNWLEWAATRLSENGKISFVLPYDAGKTLTKSTALFCIKQTNVITKIGKTPQRMLLTFAKQPEVLMQDQLVIYDADNQYTEAFIELTKDFYLKF | Function: Specifically methylates the adenine in position 37 of tRNA(1)(Val) (anticodon cmo5UAC).
Catalytic Activity: adenosine(37) in tRNA1(Val) + S-adenosyl-L-methionine = H(+) + N(6)-methyladenosine(37) in tRNA1(Val) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 26408
Sequence Length: 232
Subcellular Location: Cyt... |
A6LD46 | MANPYFQFKKFTVWHDKCAMKVGTDGVLLGAWASTERCQRILDVGTGTGLIALMLAQRSTAILDAIDIDSDACLQAQENIAKSPFANRIQVYQTSLSEYMPDENIKYDLIVSNPPYFIDSLKCPDTKRNLARHTDTLSLPDLLRDSRKLLAPEGNIALVLPFEQRESLIDIAREESLSPSREAHVSPIPDAPPKRLLIELSATPVAKPKSSHLTLEIERHRYSEEFTAIAKDFYLKM | Function: Specifically methylates the adenine in position 37 of tRNA(1)(Val) (anticodon cmo5UAC).
Catalytic Activity: adenosine(37) in tRNA1(Val) + S-adenosyl-L-methionine = H(+) + N(6)-methyladenosine(37) in tRNA1(Val) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 26633
Sequence Length: 237
Subcellular Location: Cyt... |
C6DC08 | MSHQADNKLTLRRDGFTFKQFFVAHDRCAMKVGTDGILLGAWAPLSSVTRILDIGSGSGLLALMLAQRSDTHVRIDAVELDSAASQQAKENISASPWADRIAVYAEDIIDFADTRSADYSLIISNPPYFPPGIACGSAEREQARYTTLLTHETLLRCAHQLLMPDGLFCVVLPIQVAENFIPLAQQHNWYVHQQLRVSEQEDKPAHRVLLALSRQKKECVNASLAIRDEERRYSTAFQQLTKDFYLFM | Function: Specifically methylates the adenine in position 37 of tRNA(1)(Val) (anticodon cmo5UAC).
Catalytic Activity: adenosine(37) in tRNA1(Val) + S-adenosyl-L-methionine = H(+) + N(6)-methyladenosine(37) in tRNA1(Val) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 27882
Sequence Length: 248
Subcellular Location: Cyt... |
C6Y2G0 | MKNAFRFKQFEIDQTGCAMRINTDGVLLGAVAGKNEAANILDIGTGTGVIALMLAQRFPNALVDAVEIDEQAALTATKNALNAPFSGRLKVLHSAIEDYLPEKYYDLIVSNPPYFVNDLKNPEHRKGVARHTDAHFFEQLLERVAAMLSRDGRFWFILPLKQAQNIVDMAKFYGLGMAVVLHIHSDENKPEIRQIVCLDYSGQPAHHHNLYIYAGKGLYTDAYKVLLKDFFLAF | Function: Specifically methylates the adenine in position 37 of tRNA(1)(Val) (anticodon cmo5UAC).
Catalytic Activity: adenosine(37) in tRNA1(Val) + S-adenosyl-L-methionine = H(+) + N(6)-methyladenosine(37) in tRNA1(Val) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 26257
Sequence Length: 234
Subcellular Location: Cyt... |
B8M9K4 | MAPNFPPIEEALPLHHDLFYDGKWQTPITDSRRETLNPSTGQVIGKIADASTTDVDKAVEAAHKAFLSWKKTTMAERQGYMRRAAAILREHAAELALVESYNTGNPVAAMVIDAERAANALDYFAGLIPMLRGEVLPGPFPTEDYLHYTVREPMGVVARFVASNHPFMFAGARMASVIAGGNTVIIKPPEQAPLSCLRLAELLENVFPPGVVNILPGGAECGQALTCHPLVRKVSLIGSVATGKIIMRNAGSLMKQTSMELGGKNALIAFPDADIDHLVRSVAAGMNFTWAGQSCGSTSRVFLHDSIHDEVLARVVEVVR... | Function: Aldehyde dehydrogenase; part of the gene cluster that mediates the biosynthesis of the tropolone class of fungal maleic anhydrides . The pathway begins with the synthesis of 3-methylorcinaldehyde by the non-reducing polyketide synthase (PKS) tropA . 3-methylorcinaldehyde is the substrate for the FAD-dependent... |
B8M9K0 | MASLPSQSCCYQGFRHSGAPKGTLSMVKDIEVYTSYPPDKSTEYGVLILTDIVGHRFSNAQIIADQFAENGYFVMMPDLFLGDAVPLNKPGEFDMGKWRSGAYHPQGKNHLPETVDPIVEVCLSEMRSKYQCKKIGAVGYCFGGKYVVRHLIPGKMDVGYTAHPSHIDESELKGIKGPLAIAAAAKDNIFPAEKRHVSEEILQEVGFPYQINLYSGVSHGFGVRGDMNAGEVRYAMRSAFVQAVEWFNEYMKEK | Function: Hydrolase; part of the gene cluster that mediates the biosynthesis of the tropolone class of fungal maleic anhydrides . The pathway begins with the synthesis of 3-methylorcinaldehyde by the non-reducing polyketide synthase (PKS) tropA . 3-methylorcinaldehyde is the substrate for the FAD-dependent monooxygenas... |
B8M9J5 | MNLPASIPVRTFISGCHILHRHHVLDAYGHLSVRNPERSDTFFMSRDLAPGLISSSVDLVEYFVHDASPVNPASPAGYIERFIHSEIYQKYPEVQSVVHSHASTVLPYTITGVNLRPCVHMSGFLGASVPNFDVAKFYKEDDKCDLLIRNKDLGAHLAECFSAPESDSESTRSVVLMRGHGFTAVGGSIPESVYRAIYTVENAKIQTVSMTLSAAAAKGDGPHSGIYFLPEHEIRGTKELTQRSVMRSWKLWVREVETGGLYTNLA | Cofactor: Binds 1 zinc ion per subunit.
Function: Decarboxylase; part of the gene cluster that mediates the biosynthesis of the tropolone class of fungal maleic anhydrides . The pathway begins with the synthesis of 3-methylorcinaldehyde by the non-reducing polyketide synthase (PKS) tropA . 3-methylorcinaldehyde is the ... |
Q8L7L8 | MVSHKCVEEFGYASYLVPSNARAPRSARKRRSIEKRISKEDDNMCAIDLLATVAGHLSFESGSSLMSIDKLIEDHRVKEEFPEEEKPLMPVALSPYRGSLSPCGFSSVINGKVENEVDGFSYSGGSDACQVGNFSQDVKPDIDGDAVVLDARPNVVVSLGSSSRTEVPSIGNCVSHGVRDDVNLFSRDDDENFSKYIHPRVTKHSPRTVPRIGDRRIRKILASRHWKGGSRHSDTKPWRNYYLHQQRSYPIKKRKNFDHISDSVTDDYRMRTKMHRGSRKGQGASFVASDSHVKLRIKSFRVPELFIEIPETATVGSLKR... | Function: Binds specifically to the plant telomeric double-stranded DNA sequences 5'-GGTTTAG-3'. At least 4 repeats of telomeric sequences are required for binding. Induces DNA bending.
Sequence Mass (Da): 65036
Sequence Length: 578
Domain: A N-terminal domain (80-269) is responsible for the interaction with KU70.
Subc... |
A9WFI5 | MSRIAETFARLRAAGRIALMPYLTVGFPERTSTLELVPALEAAGASLFELGIPFSDPLADGTTIQRATQRALENGITIADCIATVAELRARRVAAPLLLMGYYNPLLRYGLERACAALAAAGGDGWIIPDLPLEEADDLRQLAAAHQLDLIMFIAPTTPPARISQITAQASGFLYIVSLTGVTGARQTLAGNLTDLIANVRQQTNLPLVVGFGISQPAHIAEVARIADGAIVGSALIDRLERLPPEDRVSGAAAYIRELLSAVARP | Function: The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
Catalytic Activity: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan
Sequence Mass (Da): 28173
Sequence Length: 266
Pathway: ... |
Q822W2 | MNRIETAFKNTKPFIGYLTGGDGGFDYSVACAHALIRGGVDILEIGFPFSDPVADGPIIQKAHTRALEEKTDSTTILEIAKALRETSNIPLVLFSYYNPLLQKGPQYLHQLKAAGFDAVLIVDLPIPQHANESEPFFQALIEAKLFPIVLATPSTREERLLQIRKLAKGFLYYVSQKGTTGIRSKLSDDFSTQIARLRCYFQIPIVAGFGIANRASAAAALKHADGIVVGSAFVEKLEKKISPEELTTFAQSIDPRQ | Function: The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
Catalytic Activity: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan
Sequence Mass (Da): 28197
Sequence Length: 257
Pathway: ... |
Q8KEZ7 | MKENRITRLVKQDKKLLIAYYMPEFPVPGATLPVLEALQESGVDLIELGMPYSDPIGDGSVIQDAAHKAISHGVHVGSIFELVRRARNGEGCKKITTPILLMGYCNPLIAYGGDCFMADAVKAGVDGLLIPDLPPEESEDFLERAKHFGLSVIYLISPVTPPDRIELIDSMSTDFSYCLAVNATTGTGKLDVAGMDEKIAEYLKRVRQHTKKKFVVGFGIKDRERVRKMWELADGAVVGSALLQHVATAKTPEETAELAAGFWKSLR | Function: The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
Catalytic Activity: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan
Sequence Mass (Da): 29260
Sequence Length: 267
Pathway: ... |
O84173 | MSKLTQVFKQTKLCIGYLTAGDGGTSYTIEAAKALIQGGVDILELGFPFSDPVADNPEIQVSHDRALAENLTSETLLEIVEGIRAFNQEVPLILYSYYNPLLQRDLDYLRRLKDAGINGVCVIDLPAPLSHGEKSPFFEDLLAVGLDPILLISAGTTPERMSLIQEYARGFLYYIPCQATRDSEVGIKEEFRKVREHFDLPIVDRRDICDKKEAAHVLNYSDGFIVKTAFVHQTTMDSSVETLTALAQTVIPG | Function: The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
Catalytic Activity: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan
Sequence Mass (Da): 28056
Sequence Length: 253
Pathway: ... |
Q4FND0 | MSLINLAFKKVKTEKRPALLTYTVAGDSTKKKSLEILKSIAKYADICEIGFPHNTPIADGGQIQSSAYRALKNGIKIKDVFSIVKNFKKSKQSKPVILMGYYNMIYQYGDNNFINICKKVGVDGLIVVDLPYPENKEFAKKCKKKDISFIQLVSPTTSLDRMKKIIRDSHDMVYYISMLSTTGGKLKVSPKKILERYGKIKKLNKNKNIVIGFGITEKTIASLRKADGLVVGSALCKEISNSIKKRQNPVTNVTNIVLKLRKKIS | Function: The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
Catalytic Activity: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan
Sequence Mass (Da): 29700
Sequence Length: 265
Pathway: ... |
A9BHQ2 | MSKISEVFKNSKALITYVTAGDPNLEVTKEIILELNKDGVDIIEVGIPFSDPLADGPIIQKASQKALKNGVTLKKIFETLNEIKEEVTCPLVLMGYYNSILNYGIDNFITEAVNTGISGVIIPDLPFDEEEEFYAKIKENGIDPILLVAPNTSEERLKEISKVCSGFLYCVSIMGVTGDSQAPMEHLKEYSQRVRKYVNIPLAIGFGIDSPTKAKNIIEYFDGIIVGSALIKIIDENSDDKGKLLKEIKRFTKSLKVW | Function: The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
Catalytic Activity: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan
Sequence Mass (Da): 28626
Sequence Length: 258
Pathway: ... |
P51382 | MIINIHINFFMTTISSVFKKLDKQCALIPFITAGDPDLVSTSKALKILDQHGADIIELGLPYSDPLADGPIIQAASSRALKQSINLNNILDMVNITSSNIVAPIVLFTYYNPVLNLGINNFISAISRAGIKGLLIPDLPIEESDYIISVCKLFNIELIFLLSPTSSIERINKIVEQAPGCIYLVSTTGVTGQKPELTGKLKRLTETIKKMTQKPIILGFGISTAEQIKEIKGWNINGIVIGSAFVKRLSSDFPEEGLRKIKDFCTTAKSIIIS | Function: The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
Catalytic Activity: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan
Sequence Mass (Da): 29835
Sequence Length: 273
Pathway: ... |
Q9Y8T5 | MVSVPLRWYNIAADLPEPLPPLRDPEGLREESRIALLSRILPSRLIEDEYILARWVDIPGEVRKALARIGRPTPLIRAEGLEKVLGVKGRVRIYYKSEAVLPTGSHKINTAIAQAYYAKLDGAKEIVTETGAGQWGLAASTAAALMGLKATVFMTASSFKSKIQRRLLMEAQGARVISSPSKLTDTGREALEEYGSTHPGSLGLAIAEAVEYTLESGDRRYLPGSVLEAVLMHQTVIGLEALDQLPEEPDVVVACVGGGSNFGGFTYPMIGARLRGEGFEKTRFIAAESTAAPKLTRGEYRYDGLDSSLILPLAKMYTLG... | Function: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
Catalytic Activity: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan
Sequence Mass (Da): 45992
Sequence Length: 427
Pathway: Amino-acid biosynthesis; L-tryptop... |
O66923 | MYNYPDERGYFGPFGGKFVPETLMYALEELEEKYRELKSDPEFQKELDYYLREYAGRPTPLYFAEKLTKYVGGAKIYLKREDLLHTGAHKINNTIGQCLLTKRMGKKRVIAETGAGQHGVATATASALFGLECVVYMGEEDAERQALNVFRMKLLGAKVEIVKSGSRTLKDAINEALRDWVTNVESTHYVIGSVVGPHPFPMIVRDFQSVIGRETKEQILQKEGRLPDAIVACVGGGSNAMGIFYPFVEDKGVQLIGVEAGGYGLETGQHAASICGGSVGILHGMKSYFLQDEEGQIQPTHSISAGLDYPGVGPEHALFH... | Function: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
Catalytic Activity: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan
Sequence Mass (Da): 43543
Sequence Length: 397
Pathway: Amino-acid biosynthesis; L-tryptop... |
P14671 | MAASGTSATFRASVSSAPSSSSQLTHLKSPFKAVKYTPLPSSRSKSSSFSVSCTIAKDPPVLMAAGSDPALWQRPDSFGRFGKFGGKYVPETLMHALSELESAFYALATDDDFQRELAGILKDYVGRESPLYFAERLTEHYRRENGEGPLIYLKREDLNHTGAHKINNAVAQALLAKRLGKKRIIAETGAGQHGVATATVCARFGLECIIYMGAQDMERQALNVFRMRLLGAEVRGVHSGTATLKDATSEAIRDWVTNVETTHYILGSVAGPHPYPMMVRDFHAVIGKETRKQALEKWGGKPDVLVACVGGGSNAMGLFH... | Function: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
Catalytic Activity: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan
Sequence Mass (Da): 50926
Sequence Length: 470
Pathway: Amino-acid biosynthesis; L-tryptop... |
Q8TLP3 | MTETKVSEFQLKGKYGKYGGQYVPEVLMPALEELDVGYEKYKNDPESLAELDHYLRDFAGRETPLYFARNLSKKYGTKVYLKREDLVHGGAHKLNNALGQALLAKFMGKTRLIAETGAGQHGTATAMVGATLGFETIVYMGAKDIKRQQMNAYRMELMGTEVRAVETGSKTLKDAINEAMRDWVTNIENTHYLIGSVVGPHPYPMIVRDFQSVIGKEVKEQAMEKEGRLPDSIIACAGGGSNAMGTFHPFIEDREVKLIAVEAGGKGLKCTEKAALHSASLCIGEEGILHGARTKILQDKNGQILESESVSAGLDYSGVG... | Function: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
Catalytic Activity: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan
Sequence Mass (Da): 43932
Sequence Length: 403
Pathway: Amino-acid biosynthesis; L-tryptop... |
Q9V1G8 | MWFGKFGGQYVPETLMEPLRELEKAYKRLKNDEEFNRQLDYYLRTWAGRPTPLYYAERLTKKVGGAKIYLKREDLLHGGAHKTNNAIGQALLAKFMGKTRLIAETGAGQHGVATAMAGALLGMKVDIYMGAEDVERQKMNVFRMKLLGANVIPVHTGSKTLKDAINEALRDWVATFEYSHYLIGSVVGPHPYPIIVRDFQSVIGREAREQILEAEGDLPDVIVACVGGGSNAMGIFYPFVKDKSVRLIGVEAGGKGIESGKHSASLNAGEIGVFHGMLSYFLQDEEGQIRTTHSIAPGLDYPGVGPEHAYLKESGRAEYV... | Function: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
Catalytic Activity: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan
Sequence Mass (Da): 42624
Sequence Length: 388
Pathway: Amino-acid biosynthesis; L-tryptop... |
P50383 | MVKEDEILPKYWYNIIPDLPKPLPPPRDPQGAYFSRIDLLRSILPKEVLRQQFTIERYIKIPEEVRDRYLSIGRPTPLFRAKRLEEYLKTPARIYFKYEGATPTGSHKINTAIPQAYFAKEEGIEHVVTETGAGQWGTAVALAASMYNMKSTIFMVKVSYEQKPMRRSIMQLYGANVYASPTNLTEYGRKILETNPQHPGSLGIAMSEAIEYALKNEFRYLVGSVLDVVLLHQSVIGQETITQLDLLGEDADILIGCVGGGSNFGGFTYPFIGNKKGKRYIAVSSAEIPKFSKGEYKYDFPDSAGLLPLVKMITLGKDYV... | Function: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
Catalytic Activity: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan
Sequence Mass (Da): 47707
Sequence Length: 425
Pathway: Amino-acid biosynthesis; L-tryptop... |
Q8RGH8 | MTTENKKGYFGEFGGSYVPEVVQKALDKLEEAYNKYKDDEEFLKEYHHYLKNYSGRETPLYFAESLTNYLGGAKIYLKREDLNHLGAHKLNNVIGQILLAKRMGKKKVIAETGAGQHGVATAAAAAKFGMQCDIYMGALDVERQRLNVFRMEILGATVHAVEKGERTLKEAVDAAFKAWINNINDTFYVLGSAVGPHPYPSMVKDFQRVISQEARRQILEKENRLPDMIIACVGGGSNAIGAFAEFIPDKEVKLIGVEAAGKGLNTDRHAATLTLGTVDVLDGMKTYALFNEDGSVKPVYSISPGLDYPGIGPEHAFLRD... | Function: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
Catalytic Activity: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan
Sequence Mass (Da): 43412
Sequence Length: 395
Pathway: Amino-acid biosynthesis; L-tryptop... |
B0R332 | MSTNTDDTTRTDGTFGDYGGQYVPEVLMPAVEELTDAYERYVLDNEDGFVDDFRQRIRSFGGRPTPLTHAPTLSQRHGVDVYLKREDLLHGGAHKLNNALGQVLLAKYMGKDRIVAETGAGQHGTATAMACAALEMPCEIYMGRTDVNRQRPNVFRMRLHDADVNPVTVGSGTLKEAINETMRDWATNVADTHYVIGSVVGPHPFPSMVRDFQAIISEELRAQSREQLGELPAAVIACAGGGSNTMGAFGAFVGSASLPGAPAGTHEPAPDVDLLAVEAGGSRLGVDDDAGYAPNSASLSTGTEGVLHGARTKLLQTETG... | Function: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
Catalytic Activity: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan
Sequence Mass (Da): 45451
Sequence Length: 430
Pathway: Amino-acid biosynthesis; L-tryptop... |
Q7VGA7 | MKKKIFTESKNGYFGEAKGGNHAFGGQYIPEILLPALKELEKAYHGVFVSKAYKKELKSLFKHFVGRPTPLIYAHNASKILKNDIYLKFEGLANTGAHKINNALGQVLLAKHMKKKRVIAETGAGQHGLATAAACARLGLECEIFMGEIDIARQRPNVFNMELFGAKVHSVSSGSKTLKDAVNEALREWSKRSDDSFYVLGSALGPYPYPDIVRDLQSVISKELKKQTKAYFSSLPDILVACVGGGSNAMGFFTHYLKEERVRLIGVEAGGIGDKEGENAIRINTINASEGIAQGYKSLFLQDKDGQLSDTHSISAGLDY... | Function: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
Catalytic Activity: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan
Sequence Mass (Da): 45883
Sequence Length: 420
Pathway: Amino-acid biosynthesis; L-tryptop... |
P56142 | MNKKAYFGEFGGSFVSELLVPALRELEQAFDACLKDEKFQKEYFRLLKDFVGRPSPLTLCQNIVSNPKVKLYLKREDLIHGGAHKTNQALGQALLAKKMGKTRIIAETGAGQHGVATAIACALLNLKCVVFMGSKDIKRQEMNVFRMHLLGAEVREVNSGSATLKDAVNEALRDWASSYKDTHYLLGTAAGPHPYPTMVKTFQKMIGDEVKSQILEKENRLPDYVIACVGGGSNAIGIFSAFLNDKEVKLIGVEPAGLGLETNKHGATLNKGRVGILHGNKTYLLQDDEGQIAESHSISAGLDYPGVGPEHSYLKESGRA... | Function: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
Catalytic Activity: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan
Sequence Mass (Da): 42684
Sequence Length: 393
Pathway: Amino-acid biosynthesis; L-tryptop... |
Q2FH64 | MNKQIQTEADELGFFGEYGGQYVPETLMPAIIELKKAYKEAKADPEFQRELEYYLSEYVGRATPLTYAASYTESLGGAKIYLKREDLNHTGAHKINNALGQALLAKRMGKKKLVAETGAGQHGVASATVAALFDMELVVFMGSEDIKRQQLNVFRMELLGAKVVAVEDGQGTLSDAVNKALQYWVSHVDDTHYLLGSALGPDPFPTIVRDFQSVIGKEIKSQILKKEGRLPDAIVACIGGGSNAIGTFYPFIKDDVALYGVEAAGQGDDTDKHALAIGKGSPGVLHGTKMYLIQDEDGQVQLAHSISAGLDYPGIGPEHS... | Function: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
Catalytic Activity: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan
Sequence Mass (Da): 43965
Sequence Length: 404
Pathway: Amino-acid biosynthesis; L-tryptop... |
Q3ABS1 | MFLEKIVQVRREKVRQAKNKIPFWEMRKMAEEQVSHRLPLSLRQALLRENAKGKVGVIAEIKKASPSKGVLREQLDPEEVAQVYAKSGAAAISVLTEEDYFLGSPEYLKAVRAVVSLPILRKDFILDPYQIYEAKVLGADAVLLITSLLASVELKEMIKITEGLGMEALVEAHSLEEVEKALTAGARLIGINNRDLRTFATNIDVSLKLAPVLKEAGVVMVSESGIRSKEDIKALMTAGYHGILIGEALVRAPDPGKALEVLLA | 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): 28978
Sequence Length: 264
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 4/5.
EC: 4.1.1.48
|
A9BHQ5 | MYLEKIVETKREEVAKLKEKKISLKDSFQKGKLTLIAEIKKASPSKGIISTNFDPQRQLELYIKGGADAISILTDEKYFQGSTNILKELRPKTNLPILRKDFIIDPIQIYQSLFLGANVILLIASILTKKEISNFLKISKDIGLEAIVEVHNHQELTKVLDTETEILGINNRDLSDFSLSLRNTEKLLEELEKLGKRRDFYVISESGIKEKSDIDYLRSLEVDGVLIGEALMKENDPVLKIGELFPEKRSNLQ | 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): 28803
Sequence Length: 253
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 4/5.
EC: 4.1.1.48
|
P24920 | MGNILEEIAAQRRLDVAAAKQVVSTDDLAKKIEHTESVYGPALPVLERLNAPAEQVQAYANAGASMISVLTEPKWFKGSLDDMMEAREVVEGMSQRPAILRKDFIIDVYQLLEARAYGADCVLLIVTLLSKEQLIELIDATHNLGMCALVEVNSVQELDIALAAKARLIGVNNRDLRTFKVDMNTTARVADAIRERGLSLGRDGVALFALSGIRSHTDVVKYEKCGARGILVGEYLMKSGDIATTVKDLLQNVTRHSESGEFALLPPLAKVCGITTVEYALAALRNGANMIGIIMAEHSPRYVEKEEAKAIAKAVREYGE... | Function: Bifunctional enzyme that catalyzes two sequential steps of tryptophan biosynthetic pathway.
Catalytic Activity: N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Sequence Mass (Da): 57375
Sequence Length: 531
Pathway: Amino-acid biosynthesis; L-tryptophan biosy... |
Q6L277 | MIVDDIYKNNDKKILIKRNMRSRGILSMRSSIMNFNLNKKIGIIAEFKRRSPSGFVNNENTDIFKYYDVIHNSIAGMSILTEERYFNGNQMDVVSVQRYNIPILIKDFVSNDEMIESSYMIGGDVILLIADFLERDKIEMLNRKIKSLGMEALIEFHDLKAFERITTDENVIIGYNRRNLKTLKIEDESFDAQDLIRSTGLLSVLESGITSENILKMPRYNAMLIGSSILSNDSVLKSAGMIKYDGFGYS | 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): 28644
Sequence Length: 250
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 4/5.
EC: 4.1.1.48
|
Q123F4 | MSDILDKIIAVKREEIAQAIKRKPLAVVREDAESRVLTRDFVGALRAKISAGKPAVIAEVKKASPSKGVLRADFIPADIAQSYAEHGAACLSVLTDRQFFQGSVDYLKQARASCALPVLRKDFMVDAYQVYEARVMGADCILLIVACLDDAQMKALEALAFSLDMAVLVEVHDEAELERALKLRTPLVGINNRNLKTFEVSLDNTLSLLGKVPADRLLVTESGISTPADVKRLREARVNAFLVGEAFMRAEDPGVALAQLFGLD | 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): 28767
Sequence Length: 264
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 4/5.
EC: 4.1.1.48
|
P59415 | MKIILNKIYQGDTLNISETYTLFKSIMLKKINNIELSAILIALKIRGESQNEILGAVKACLEHMITFPKPTYMFSDIVGTGGDNSNSINISTTSALVGSACGFKIAKHCNGNISSKTGSADILKKFGINIQISPEKSKKMLDELNICFLFAPQYHINFKVVTQVRKILRIKTIFNIIAPLLNPAMPKLTVMGVCNFKLMLPIAQVLKTLNYHHAIIVCSDNIDEVTLHSFTKIIELKNNNITSYILHPDDFGVKYCHKNDILGGNTEENYNIIKKILQGKGPSAVTETIAVNVAILFKIFGYSNLKKNTEYALKVIRSGK... | 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... |
Q2FKX5 | MIQDTIRKVVSMQDLAPDEARDLMTSIADGKVTDAQIGSILTALSMKGVTAHEITAFAHVLRDRAVQLKTDTSGTFVDTCGTGGDGAHTFNISTAAALVAAAAGVRVVKHGNRGVSSRSGSADVLEALGIPITLTPEEAAASVSSHNIAFLFAPGYHPAIGRVASARREIGFFSVFNILGPLLNPAGASARLIGVGDTRHIPSITGALANLGVSHAMVVHGDGTDEITITGETEVYELSGGTICRYTLTPEEFGIRRVSRETIAGGSPAENAEIIMDIFSGRKGPCRDIVLLNAAAAIYLGEKATCIYDGYRIAREVVDS... | 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... |
Q57686 | MITEALKKVIEFKDLDEKEAEAVMKDIMSGNAKPTQIAAILTALRMKGETIEEITAFAKIMREFSLKINPNVPKLLDTCGTGGDNLNTFNISTATAFVVSAYVPVAKHGNKAVSSKSGSADVLEALGVNLNVPIERVKESIEKIGIGFLFAPHFHPAMKFATPVRKELGIRTVFNVLGPLTNPANANYQLMGVYDEKLTEKLANVLKNLGLKGALVVHGSGMDEITTIGKTKISELRNGEIKSYYIEPEDFGIKKAKLEDIRGGDAEENAKIIGEIFEGEEVGAKRDIVVLNAAFALYIAEEAKDVEEGIKLAEKSIDEG... | 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... |
Q8TXJ5 | MSVLERIIRGSDLDREEARDLMCRIVGGELSDVEVAGILVALRCKGYTSEELVGFVDGMMEHAVKVDPDVERLVDTAGTGGDELDTFNASTLAGLTAAAAGVPVAKHGNRSVTSECGSADILEALGVNIEADPDTVKRCIEEVGFGFMFAPKFHPAMKNVMPVRRKLGIRTVFNVLGPLTNPARERVTGQVIGVYSENLLDLVAGALAELGVRRGLVVYGLDGVDELSVTCENEVVYVDDGEVTDRDTVAPEDVGLDRADPKDVAGADPETSAEEARKILGGELPVDHPKVQMTAFNAGAALYVGEAVDSLEKGIQRALD... | 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... |
A2STA7 | MIAECIKKVASHSDLSVYEAKGAMQDIMSGNATDGQIGAFLTALVMKGETSSEIAAFASVMRENAVQITPKRNGMLVDTCGTGGDGKNTFNISTAAAFTAAGAGVTVVKHGNRGATSKCGSADVLEALGIKIDISPERVCEIIDENGIGFMFAQSHHPAMKYAGKVRKEIGIRSFFNLIGPLSNPAGADAQLLGVYDSPLTEKIAEVLNILGTKRAMVVHGDGYDEITTTGITQVSEVNDGQVRSYSLDPSSFGFQKADAASLFGGDSQYNAHIIRSVLSGDEGPRRDIVILNAAAAIYLGERAGSIADGIKYAEKSIDS... | 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... |
B1M5Q2 | MDSFRPHLAKVAGGLALDRAEARAAFDDLLSGEVTPVQAGAFLTALKVRGESVEEIVGAAEAMRARMTRVAAPENAVDVVGTGGDHSGSVNVSTLAAIVVAACGVPVAKHGNRAATSRSGAADVLAALGVRLGLDPAAQARCLDEAGLCFLFAQAHHPAMRHVAAVRSELPVRTIFNLLGPLSNPAGVGYQLFGVAQAALAEPLTRVLAELGSRRVWTVHGSDGLDEITVTGPTQVVALDEGRLCHFTIDPREFGLALRAPEELRGGDPADNARSLEAVLAGARNAYRDIAVLNAGAALVVAGAAQALADGVAQAQDAVD... | 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... |
A5UMC1 | MIKEAILKVVNGNDLNAKEAYGAMDEIMSGESSEVQMSAYLTALSMKGETIEEITASTKAMRAHCVKLLNDEEVLEIVGTGGDGSNTFNISTTSSIVISAAGVPVAKHGNRSASSKCGAADVLEALGVNIYIEPEKSLKILKEINLCFLFAQNYHLAMKFVAGVRKELSIRTIFNILGPLTNPAGATMQVLGVYDESLVKPLCEVLKNVGVKSALSVYGQDGLDEISVSDKTSVCELRDGRLKCYEIAPEDFGMERCSKEDLVGGNPRENAEITLSILNGQKGPKRNAVVLNSAAALYVAGKADSIEDGVRLASEIIDSG... | 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... |
A4YHE2 | MDPKEVLKRLTEGVSLSQEEAKELADLIMEGSIPEPLVAGILVALKMKGETPDEIIGFVNSMRQHALKLDLRNTLDTAGTGGDGIGTINVSTATALAVSSVFPVAKHGNRAASSRSGSADFLESLGYNIQVPPEKAKDLLSRNNFVFLFAQLYHPSMKNVAPVRKVLGVRTIFNLLGPLTNPAGSERQVMGVYSLPFMRKLAEAALKLGYVKLVLVHGEPGLDEVSPQGKTYITEVTGSKVEEYTYDFSEIIGQPVPVSRLTTTDPLDSVRRVLMASMGRDEAVEKFIRINVSVALYTAGLVSDFKDGFELSEELVRKLP... | 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... |
A7NL64 | MPIRDQIIQIVRGHDLTEEQAAEAMEEIMTGVATPAQVAALLTALHLKGETDAEIAGMARVMRAKAIPVHFDGPLLDTCGTGGDSAGTFNISTTAAFIAAGAGATVAKHGNRAMSSVCGSADVLEGLGVTIDLDAAGVARCLEQAGIGFMFAQKFHPAMRFVGPVRREIGIRTIFNALGPLSNPAQARHQTLGVADPALAEKMARALYLLGAQHALVVHGHGGLDELTLSGPNLVIEVRAGHKPRRYEVSAGDLGLTPAPREALLGGDVSTNVAIVRAILSGEERGARRDVALLNAAAALVAADYAADLREGLQQARQSL... | 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... |
Q163Y0 | MSDALKPLIGAAADRALSRAEAEDAFRILFEGEATPSQIGGFLMALRTRGETVAEYAAAASVMRAKCNAVKAPAGAMDIVGTGGDGKGTLNISTATAFVVAGAGVVVAKHGNRNLSSKSGAADALSQMGLNVMVGPEVVERALAEAGIGFMMAPMHHPAIAHVMPTRAELGTRTIFNILGPLTNPAGVKRQLTGAFSRDLIRPMAQTLGALGSEKAWLVHGSDGTDELTITGVSWVAALGPDGSVTDMEIHPEDAGLPVHPFEAIVGGTPAQNAADFKALLAGEASAYRDAVLLNAAAALVVADAASTLQDGVEMAATSI... | 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... |
Q1AU89 | MLREALRKAAAGEPLSEGEAERALETIMEGGASPEATAALLTALRVRGESVQEIVGFARAMRRFAARVRAPEGVVDTCGTGGDAKGTINVSTAAAFVARGAGVVIAKHGNRAATSRAGSADVLEALGAAIELSPEQVSRCIEEAGIGFMFARTHHPAMRHVAPVRAELPFRTVFNLLGPLTNPAGARRQLVGVFSAGYVRPMAEALEGLGAERALVVHGRDGMDEITVTGPTLVAEVGGGGVEEYEISPEDFGLSRHAPDGLLGGDAHLNARILRDVLSGEERGASRDVIVLNAGAAIYVAGKAPSIEEGVRLAEGSLES... | 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... |
Q1GHJ3 | MSDALKPLIGLAADRALTRTEAETAFAALFNGEATPSQMGGLLMALRTRGETVDEYAAAAAVMRAKCNKVSAPADAMDIVGTGGDGKGTLNISTATAFVVAGAGVPVAKHGNRNLSSKSGAADALTEMGIQVMVGPKVVEKSLKEAGICFMMAPMHHPAIAHVMPTRQELGTRTIFNILGPLTNPADVKRQLTGAFSRDLIRPMAETLKQLGSEVAWLVHGSDGTDELTITGVSWVAGLSEDGNISEFEVHPEEAGLPEHPFEAIVGGTPAENAAAFRALLEGTPSAYRDAVLLNSAAALKVAGVVSSLKEGAERAAESI... | 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... |
B8I0U9 | MIQEAIYQVINKQDLDLDKTIQVMEEIMEGRATNAQIGSFLTAMRMKGETIDEITACATVMRQKCKRIHPEKDVLDIVGTGGDEANTFNISTVSSFVVSAGGVPVAKHGGRSVSSKCGSADLLEALGINIALSAEQSAEILQKIGMCFMFAPTYHASMKYAAPVRKELSVRTIFNILGPLANPAGANMQLLGVYDENLVEPLARVLLNLGVKRAMVVHGHDGLDEVTLCNTTTICEVSNGNINSFFLSPEQLGFSRCLLKELVGGDPKKNASIALDILNGSKGPKRDIVVLNSALCLYMSYNQITLRDCVKMAEQLIDSG... | 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... |
P50384 | MNINEILKKLINKSDLEINEAEELAKAIIRGEVPEILVSAILVALRMKGESKNEIVGFARAMRELAIKIDVPNAIDTAGTGGDGLGTVNVSTASAILLSLVNPVAKHGNRAVSGKSGSADVLEALGYNIIVPPERAKELVNKTNFVFLFAQYYHPAMKNVANVRKTLGIRTIFNILGPLTNPANAKYQLMGVFSKDHLDLLSKSAYELDFNKIILVYGEPGIDEVSPIGNTFMKIVSKRGIEEVKLNVTDFGISPIPIEKLIVNSAEDSAIKIVRAFLGKDEHVAEFIKINTAVALFALDRVGDFREGYEYADHLIEKSL... | 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... |
Q2S1Z6 | MNTLLQTIADGDPLSRPEAEEAMATMMSGSARDEHIAALLMGLRTRGETLDELVGFTKTMREFAVSVETDDPQTIDLCGTGGDGASTFNISTTASFIAAGAGATVAKHGNRSVSSQSGSADVLEALGVQIDLEKEGVEHCLHEAGIAFLFAPFFHPAMRHVMPVRKALGVRTFFNILGPLCNPAGVTRQIVGAFDTSTAQTMVRILAELDADHVITLHADDGLDEVSISASTTLFEYDASDQNPVPRSHEVGPERHDLDRASISTLEGGTAQQNASILRNILSGEDQGPRRDVALLNAAYALHVSDQYADLDACLEAAAE... | 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... |
O60122 | MINTFNPEVRLAIHDLDKVGPAIPLENYEAALRAILTGKASPVETASFLASLHLTKAEEVPDILMQTVQILKSYSTPIANIEMVSPRFVDIVGTGGDGHNTFNVSTASAIVAAGAGLWVCKHGNKASTSASGSADLLMSFGCDLLNVTPKNIVSITEQCKFSFLFAPMCHPTLKNVAPIRKQLGLPTIFNLVGPLLNPIPTYARIIGVSKLSLGEVVAKTLLKLGAGRSLVVCGEEGLDEISPAGPTHTWLVRDGTITHEVYTPESFHLQSHPLSSVASGTPSANAILLEELLSNMLHANHPILDYVLMNTAALLHVAGM... | Catalytic Activity: diphosphate + N-(5-phospho-beta-D-ribosyl)anthranilate = 5-phospho-alpha-D-ribose 1-diphosphate + anthranilate
Sequence Mass (Da): 37556
Sequence Length: 354
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 2/5.
EC: 2.4.2.18
|
Q06128 | MEVHPISEFASPFEVFKCIERDFKVAGLLESIGGPQYKARYSVIAWSTNGYLKIHDDPVNILNGYLKDLKLADIPGLFKGGMIGYISYDAVRFWEKIRDLKPAAEDWPYAEFFTPDNIIIYDHNEGKVYVNADLSSVGGCGDIGEFKVSFYDESLNKNSYERIVSESLEYIRSGYIFQVVLSRFYRYIFSGDPLRIYYNLRRINPSPYMFYLKFDEKYLIGSSPELLFRVQDNIVETYPIAGTRPRGADQEEDLKLELELMNSEKDKAEHLMLVDLARNDLGKVCVPGTVKVPELMYVEKYSHVQHIVSKVIGTLKKKYN... | 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... |
P00898 | MQTPKPTLELLTCDAAYRENPTALFHQVCGDRPATLLLESADIDSKDDLKSLLLVDSALRITALGDTVTIQALSDNGASLLPLLDTALPAGVENDVLPAGRVLRFPPVSPLLDEDARLCSLSVFDAFRLLQGVVNIPTQEREAMFFGGLFAYDLVAGFEALPHLEAGNNCPDYCFYLAETLMVIDHQKKSTRIQASLFTASDREKQRLNARLAYLSQQLTQPAPPLPVTPVPDMRCECNQSDDAFGAVVRQLQKAIRAGEIFQVVPSRRFSLPCPSPLAAYYVLKKSNPSPYMFFMQDNDFTLFGASPESSLKYDAASRQ... | 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... |
P21690 | MFLFVETIRPQQRGESLLETVIKVVPGERFTPYGLALKLGARVVLESSSSKKGRDRYSLLLLQEAFRVAQEGTEVYFVKDGRRSKVKANHRDILDVLMYFARQHSDPGQDFPFPAGGVGYLSFEFCRYCDTIHLNPAKPDPLELPDALFLFGHVFLIYDHYTDLIYLVGLNYKEASIDLEAALAAVEARVNDGDWSALGSVGAPYDAEVLPQDYDPDETYKANVGAMRQEVIAGNLLQGVPSRRLLVKTEMPAIEAYRRLRSSNPSPYMFYLDFGDYQLFRASPELHVKVKGGTAEIRPIAGTRRRGATDAEDRALEAEL... | 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... |
Q9Z4W7 | MTTHAAEAPTTDPQGAPGSQKTPDATEAEEAARATVPHRAAAAALAREHDVVPLHQEFLDDSVSPVTAFAQLCGPDEAGFLLESVPVSGGVARYSYVGHRPVPLEPTGGDPLTALRSHLARSVAPVPGLPPFHGGVVGYLGYEAARHFEDLPLAAGPPPGLPESAFLAADDLVVFDHATRRVLLMTLYRPARESYDDAVARIVRLNRALRRAPAPAAFSGRPLAAATPADHGTQGWTANLTEAQFTERVARAREHIAAGDAFQIVLSRRLSRPLRARPTDLYRHLRATNPSPYMYHLSLGGGRHVIGASPELLVKAEGRT... | 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... |
P20170 | MISPGFSHFTELAQQGNFIPVYQEWVADLETPVSAWYKVCSSQPYNFLLESVEGGESIGRYSFLGCDPMWVLEARGDETTQVLRNGQTETFRGNPLDILSQCLESIRPVNLPQLPPGIGGLFGVWGYELIRWMEPRVPVYEPQPEDPPDGIWMQVDHLLIFDQVKRKIWAIAFADLRGENVDLETAYRNACQRVTKLVLQLQLPLPPEATALELLTKTQLEGKELNYSSNTEQEKFLEEVAIAKDYITAGDIFQVVLSQRLSTIYRDDPFKLYRSLRLINPSPYMAYYNFGHWQIIGSSPEVMVKADRQLDGKLMATVRP... | 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... |
Q9YGB3 | MPLKKLKPVDPLKLYSALRDFGMPFMLRSAEKDSRKARFTYISAEPEFVVEVGEGTEIDGERVSDERNPLRALKGLMGERVEGRRFMGGFVGYVSYDSVHSIIGGKIEEPSVFGYYPWTFIYDHSTGALSFFYLREAPFDPEALVERARREESRLEDGGSEVISTDAGMEEFVEIVRAGKEYIYSGDVFQVVLSREYRVRTDLDALEIYKRLVELNPSPYTFILEFEKTVVGASPETMGSVEGRTFKINPIAGTAPRGRTGEEDRELEKALLSDEKERAEHVMLVDLARNDVRRVSKPGSVRLTRFFDVLKYSHVQHIES... | 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... |
Q08653 | MGDSMHVLKLVSDLETPVSTFMKVSRGEEFAFLLESVELGSAFGRHSFIGIGKKDVLVFEKGILRTSNQQLDYTSSPLKAIKDWLEVYRYSVKHDELPSFRGGAVGFVSYDYISYIEKVKVKASVFPTFYFVVPEHLIIFDHLKNNVFIISDSPEELTSKVLSPFEEKPEKNVFVTEPESNFEREQFYKVVEKAKKYIVEGDIFQVVLSQAFTFKTTLDPFYIYRALRMINPSPYMFYLKFGDTVVLGSSPETMAKVEGDKATVKPIAGTRPRGRTVEEDLKLERELLNDEKEIAEHVMLVDLGRNDLGRVCKEGTVRVE... | 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... |
P05378 | MERIRPYRKTFLADLETPVTAYLKLAEKAPVSFLLESVERGRQSRFSIVGVGARRTFRLKDGVFTVNGERVETRDPLRALYERVYAPLERHPDLPPFFGGVVGYAAYDLVRYYERLPSLKPDDLGLPDLLFVEPEVVAVFDHLKNLLHLVAPGRDPEEAEARLFWAERRLKGPLPGVPGERAGGRARFQADFSREAYLEAVRRALDYIRAGDIFQVVLSLRLSSPLTVHPFALYRALRSVNPSPYMGYLDLGEVVLVSASPESLLRSDGRRVVTRPIAGTRPRGKDEEEDKRLAEELLRDEKEVAEHVMLLDLSRNDIGR... | 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... |
P22099 | MRLCTAGRLKQLQGGLVNKAIEIKKLGQLEVLKASVPYTQDPTRLFHTICENKTDSLLLESAEIDSKQNLKSLLIVDSAVRIVCYGHTVSFHALTENGKNLLTHVNQNVRGEVASQFDGETLTLEFIQPCDTIDEDSRLREASSFDALRLVQHSFDLSSQDKHAIFLGGLFAYDLVANFEPLGDAVATNQCPDYVFYVAETLLVVDHQTESCQLQATLFVDGSQKAALESRIEDIRAQCTSPKRLPDATQVANITAQPSVPDQDFCQIVRDLKEFVVKGDIFQVVPSRRFTLPCPSPLAAYKELKQSNPSPYMFYMQDEL... | 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... |
P00899 | MTASIKIQPDIDSLKQLQQQNDDSSINMYPVYAYLPSLDLTPHVAYLKLAQLNNPDRKESFLLESAKTNNELDRYSFIGISPRKTIKTGPTEGIETDPLEILEKEMSTFKVAENVPGLPKLSGGAIGYISYDCVRYFEPKTRRPLKDVLRLPEAYLMLCDTIIAFDNVFQRFQIIHNINTNETSLEEGYQAAAQIITDIVSKLTDDSSPIPYPEQPPIKLNQTFESNVGKEGYENHVSTLKKHIKKGDIIQGVPSQRVARPTSLHPFNIYRHLRTVNPSPYLFYIDCLDFQIIGASPELLCKSDSKNRVITHPIAGTVKR... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Catalytic Activity: chorismate + L-glutamine = anthranilate + H(+) + L-glutamate + pyruvate
Sequence Mass (Da): 56768
Sequence Length: 507
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 1/5.
EC: 4.1.3.27
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Q8PRX4 | MRIKVCGIKRVEDAVMAAYCGADAIGLVVGRKHNSDDFIDKHLAQKIVRECPPYISPVLVTELDDAEEISGLVHETGVTSVQLHSDCTVDSIISLRKTFPNIKIIKNFHVIGPGVIHAMKPFESVVDAFILDTLDLANDKVGSTGLVHDWSISRKIVKEVSRPVILAGGLTPENVGEAIRVVNPYGVDASSGLKDSNGFKDEMKVINFVHRAKNDFFKVRNLSLEN | Catalytic Activity: N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Sequence Mass (Da): 24760
Sequence Length: 226
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5.
EC: 5.3.1.24
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B0CA72 | MRVKICGITQPDQGVAIATLGADALGFICVSQSPRYVTPQQIQVVTQALPTQTLKGEPLTRIGVFANAALDLIQQTVEVGQLTGVQLHGDESPEFCQQVKAKLPKVELIKAFRVRSAETLAQITPYEAIANTLLLDAYTPQALGGTGHTWDWTLLKTFTPKLPWFLAGGLTPDNVTPAITTLTPSGIDLSSGVEQSPGNKDLQKVKQLFQQVHTLVI | Catalytic Activity: N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Sequence Mass (Da): 23382
Sequence Length: 217
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5.
EC: 5.3.1.24
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A3DDS6 | MTCVKICGLRRKEDIDYVNLYKPQFAGFVFAESRRKVSKETARMLVKALLPQIKSVGIFVNEKKETVAEIVKYTGLDCVQLHGDETPEYVEKLKELLGRITEKRIEIWKAVRVKNKESLEIISEFDVDAFLLDAYVEGSYGGAGAVFDWQLAADVAAGHERIILAGGLNPENVKTAVAKVKPYGVDVSSGVETDGFKDAEKIRDFIMKVREADGGVLS | Catalytic Activity: N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Sequence Mass (Da): 24220
Sequence Length: 218
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5.
EC: 5.3.1.24
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P16923 | MRTRAKICGITRSQDVQAAVSAGADAIGLVFFPPSPRHVSIAQAQALLQHIPAYVQVVGLFVNATADQIKSVLDCVALDVLQLHGDETPEQCQEIALQCKRRWYKAIQVKPELDVVDEVQRYQAAGASAVLLDAWHPELKGGTGHQFDWSKFPKLDIPLILAGGLTPENVVDAIQTTHAFAVDVSGGVEAAKGIKDKQLIERFMQGVQCGSAK | Catalytic Activity: N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Sequence Mass (Da): 23005
Sequence Length: 213
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5.
EC: 5.3.1.24
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A5FZ94 | MARAKICGLRTRETWLAATDAGADWVGFVFFPRSPRFVTIEALKAIGADARVPRVGLFVDPEPAAIEAVLKVQDLEFLQIYAGAEACRAMRARFGAKVWRAVGVASAADLPRDDEGLDGFLIESKPPRGADRPGGNATAFDWAVMQGWRAPAPWLLAGGLTPANVAAAVRASGAAAVDVSSGVESAPGEKSVPLIRDFVAAAHAA | Catalytic Activity: N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Sequence Mass (Da): 21466
Sequence Length: 205
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5.
EC: 5.3.1.24
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B7J4T0 | MPMVRIKICGITNTEDARAAAAAGADAVGLVFYRSSPRALDAVRARKILAALPPFVTRVGLFVNAEAADVAATLQQCPLDVLQFHGDESPSLCRGFGRPYIKVLRVTAAQDLRPAVDAYHDAQGLLLDCAAPGVWGGSGRSFDWWRLPDLGKPLILAGGLHAENVAEAIAIARPYAVDVSSGVELSPGRKDHDKMARFVARVRGT | Catalytic Activity: N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Sequence Mass (Da): 21827
Sequence Length: 205
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5.
EC: 5.3.1.24
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Q2RIT8 | MVRVKICGIRDWEEARMVLDAGVDTLGFVFARSPRAIKPEAAREIITKLPPFTTTVGVFVNEPRYSLMEIASFCRLDVLQLHGDEPPEYCHGLSQRLIKAIRVRDAASLASLEAYREVQGFLLDAWVPGKAGGTGTTFNWELVRGAATGGKPVILAGGLTPENVGAAIQLVHPYAVDVSSGVEVDGRKNPARIAAFLEAVRKAEEHHVRPTASSCCTGLKGDF | Catalytic Activity: N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Sequence Mass (Da): 24112
Sequence Length: 223
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5.
EC: 5.3.1.24
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Q1CZH4 | MSVRVKVCGVTRLSDAVAAWEAGVDALGLNFYPKSPRYLDLPTAAALARTRPPLGTVLGVFVNAAPDTIRETVRACGLTAVQLHGDEPPEACSGYGVPVIKALRVTGPEDVVRARTYVGVGDVAGLLLDGAAPGYGGGGVGFDWSLVAGLAGSGVPVLVAGGLRPSNVAEAVRATRPYGVDVASGVESAPGIKDVEAVRAFVRAAKSINLWE | Catalytic Activity: N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Sequence Mass (Da): 21633
Sequence Length: 212
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5.
EC: 5.3.1.24
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Q9K0C6 | MRKIRTKICGITTPEDAAAAAAAGADAVGLVFFQGSSRAVDIARAKKITAALPPFVSVVALFVNESAQNIRRILAEVPIHIIQFHGDEDDAFCRQFHRPYIKAIRVQTASDIRNAATRFPDAQALLFDAYHPSEYGGTGNRFDWTLLAEYSGKPWVLAGGLTPENVGEAVRITGAESVDVSGGVEASKGKKDAAKVAAFIATANRLSR | Catalytic Activity: N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Sequence Mass (Da): 22242
Sequence Length: 208
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5.
EC: 5.3.1.24
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Q2Y7R3 | MSIRVKVCGITRVEDALAAVHLGANAVGFVFWEQSARYISPAEARGIVSTLPPFVTSVGVYVDPEAGWVDESISVAGLNLLQFHGSESPEFCQQFSLPYIKAVRVRPGLDLLQYASLYTGATGLLLDTYVEGEPGGTGEAFDWNLIPRNLPLPLILSGGLHAGNVTSAIQQAHPWAVDVSSGVEAAKGIKDSGKIAAFMRGVGISESL | Catalytic Activity: N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Sequence Mass (Da): 21998
Sequence Length: 208
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5.
EC: 5.3.1.24
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Q3JCB9 | MRTRVKFCGITRREDAIQAIRLGADAIGLVFYPESPRAVSPQQAYQIVRELPPFVTVVGLFVNAASCYLQQILDKVPIDILQFHGEESPEECGYYGRSYIKAIRMAEGVDLPSLARSYESASALLLDAYQAGVPGGTGRAFDWRRIPKNFSKAVILAGGLTPENIAQAVRQVRPYAVDVSGGVERIKGVKDAAKMAAFMRGVDSVN | Catalytic Activity: N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Sequence Mass (Da): 22482
Sequence Length: 206
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5.
EC: 5.3.1.24
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A6Q1S6 | MRVKICGITNLEDALVAIEAGADALGFVFYEKSPRYIHPQEAKIISKKLPPFVERVGLFVHEEPVKIDEICSYCNMSLAQIHFDVEESFFEKLQTKALPVVRAKCAEDILQFSDRYRLVDAYVPEFGGAGRRVALEWFENIDCSKIVLAGGLSPKNVSEVKRYGFYGVDVSSGVEARKGKKDPQKVREFIQKAKFE | Catalytic Activity: N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Sequence Mass (Da): 22142
Sequence Length: 196
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5.
EC: 5.3.1.24
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