ids
stringlengths 6
10
| seqs
stringlengths 11
1.02k
| texts
stringlengths 108
11.1k
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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 biosynthesis.
EC: 2.1.1.33
|
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 biosynthesis.
EC: 2.1.1.33
|
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 biosynthesis.
EC: 2.1.1.33
|
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 biosynthesis.
EC: 2.1.1.33
|
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 biosynthesis.
EC: 2.1.1.33
|
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 biosynthesis.
EC: 2.1.1.33
|
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 biosynthesis.
EC: 2.1.1.33
|
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 biosynthesis.
EC: 2.1.1.33
|
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 | MRIDVLSIFPEYLEPLKLSLIGKAVTDGLLQLQVTDPREFATDRHRTVDDTPYGGGAGMVMKPEPWARALESVLRAGSDTTARSGSTAATSASAQQATRLGPDDDAAQPGDAGQGTAAPDYARTGGTPGAGRAASSRPVLVVPSPAGEVFTQEVAYELAEEEHLVFACGRYEGIDERFIEWARDEVRVRPLSLGDYVLNGGEVAVLAMVEAVTRLVPGVIGNPESLDEESHTGGLLEYPVYTKPAQWRERTVPDTLLSGHHGRIARWRRDQQLERTARRRPDMVLALDPATLDRADLAVLAAEGFTLRDGQWQRCSPAPSEQAPEGARDMA | 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 | MSSPTITVVGAGLAGSEAALAAAKLGVRVRLFEMRPQKMTPAHRTANFAELVCSTSLGGEGEMQSKGLLQAEMRSVGAAIVTSADASRVPAGNALAVDRDAFSAHVTEQVKNHPLIEVVEGEVETVPDGICVIASGPLTADALASDLRRLTGSERLSFYDAAAPVIDVDSIDMDIAWRAGRYDQSADYINCPFTKEEYLAFFEALETARSHTPHDWEKLEFFEGCMPIEEIARRGVDTPRFGPMSPKGLDDPKTGRWPYAVAQLRQEDAEGRMWSLVGFQTGLKWGDQKAVVQLIPGLHNADIVRYGVMHRNTYLNAPEVLDSTLQLRADPQKLVAGVLAGTEGYLESSATGWLAGTNAARLALGLEPLTPPAESMLGGLVRYLASANPKGFQPMNVNWALVPELPTEINEKTGKPKKLGKREKRPPLFRRGLGAFMAWAGQDAGVPVTPPAVPEHPQDELPAIR | 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 Length: 465
Subcellular Location: Cytoplasm
EC: 2.1.1.74
|
B1I258 | MSGGVIVVGAGLAGAEASWQLVRRGVPVVLYEMRPRKCTPAHKTGDFAELVCSNSLRAEALTNAVGLLKEEMRRLGSLIMACADAHRVPAGGALAVDRQLFAAAVTERLTSHRLVTVCREEITTIPTAELVILATGPLTSDALADELRRLTGQEHLYFFDAVAPIVTLESIDQDRVFRSSRYGRGDPAYLNCPMSREEYERFWEALVAAERATRHTFERETHFEGCLPVEVIAARGRETLLYGPLKPVGLVDPRTGERPYAVVQLRQDNRAGTLYNLVGFQTNLKWGEQRRVFSMIPGLEQAEFVRYGVMHRNTYINAPVLLSPNLMLKSRPGLFIAGQLSGVEGYVESAAAGLVAGLNAARLYKGLEPLVFPPETAHGALINYIVTADPANFQPMNVNFGLFPPLPGKRVRRRPERNLAHAQRALERLAAWLTEKGEG | 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 Length: 439
Subcellular Location: Cytoplasm
EC: 2.1.1.74
|
Q6ALS7 | MNNMNKVIIIGGGLAGSEAAWQAANRGCQVELVDMKPEKYSPAHSSPLLGELVCSNSLRSNDPTSAVGLMKREMRFFNSLIMDVADSTAVPAGKALAVDRDKFAEAITARLESHPNISISHREVTAVPEPADHPTIIATGPLTAEDFAESLAELTGRDRLAFYDAIAPILDSESLNMDIVYCKSRYDDGPGDYLNCPMNREEYERFISELASADYMPLKDFEDAKYFEGCLPVEVICSRGVDTLRFGPMKPVGLPDPRTGQDPYAVVQLRMENAEGSTYNMVGFQTKMTYPEQKRIFRMIPGMENVEFVRLGSIHRNTFICAPELLADTLQIKKRPDLLLAGQLSGVEGYIESAAMGLLAGINAARRAMGEELVSPPAEMALGAMVGHLTKSAAKNFQPSNVNFGLFPAWEKKVPKRFRGEKRAEASALALEVWNEKWQISEQV | 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 Length: 444
Subcellular Location: Cytoplasm
EC: 2.1.1.74
|
Q729K0 | MEDSLTTITTAAIIGAGLAGCECALRLARAGVRVTLFEMKPAAFSPAHSNPDLGELVCSNSLRSDDIASGVGLLKQEMRELGSIVMEAADATRVPAGKALAVDRDLFARHITAVIEAEPGITLERREVASLDDPALASADVVVIAAGPLASAGLSDSLAAVVGGQLYFYDAIAPIIAAESIDLSIVFSGSRYGEPGEEGDYLNCPMNRDEYDAFYEALLAAEKVPSRDFEKELHFEGCMPIEALAERGPRTLVFGPFKPVGFTDPRTGTRPYAIIQLRAENRNKTAFNIVGCQTKLKYAEQERVFRMIPGLAGAEFVRHGSVHRNTYVNAPRVLADDLSLRADKRVFLAGQITGVEGYVESAACGMWLGMVLAARIQGRELPTPPPQTALGALLMHLRTPVKNFQPSNANFGLMPELGLKVKKRERKPLYSARAREHFVRWLAEAGVTPVIEPLLPTAPDTTGAAGEETTQAES | 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 Length: 474
Subcellular Location: Cytoplasm
EC: 2.1.1.74
|
Q8REM9 | MEKEVIVVGAGLAGSEAAYQLAKRGIKVKLYEMKAKKKTPAHSKDYFSELVCSNSLGSDSLENASGLMKEELRILGSLLIEVADKNRVPAGQALAVDRDGFSEEVTKILKNTKNIEIIEEEFTEFPNDKIVIIASGPLTSDKLFQKISEITGEESLYFYDAAAPIVTFESIDMNKAYFQSRYGKGDGEYINCPMNKEEYYNFYNELIKAERAELKNFEKEKLFDACMPIEKIAMSGEKTMTFGPLKPKGLINPKTEKMDYAVVQLRQDDKEGKLYNIVGFQTNLKFGEQKRVFSMIPGLENAEFIRYGVMHRNTFINSTKLLDKTLKLKNKDNIYFAGQITGGEGYVTAIATGMYVAMNVANRLENKEEFILEDISEIGAIVNYITEEKKKFQPMGANFGIIRSLDENIRDKKEKYRKLSERAIEYLKNSIKGV | 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 Length: 434
Subcellular Location: Cytoplasm
EC: 2.1.1.74
|
Q39X89 | MTDAITIIGGGLAGCEAVWQAAERGVRVTLHEMKPHAFSPAHHLAGLAELVCSNSLRGESLENAVGLLKEELRRAGSLIMAAADATRVPAGGALAVDRELFSAFVTERIENHPLVDLMRGEVADIPSEDIVIVATGPLTSDGLAERIRAITGPNLYFYDAIAPIVTAESLDMTKVFRASRYGKGDGDDYLNCPLNQEEYEGFVDAILAAEKVPARDFEKVVHFEGCMPVEEMAERGRETLRFGPLKPVGLADPRTGEEPHAVVQLRAENREGTMFNLVGFQTKLTYPEQRRIFRMIPGLENAEFVRLGSMHRNTFINAPALLAPTFQLKGDARILFAGQITGVEGYVESAGSGFLAGVNAARLVRGEEPVVPPLATALGALVTHITNADVKHFQPMNVNYGLFPPLEGKVKKKERRGKLAERALAELDRWIGTV | 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 Length: 434
Subcellular Location: Cytoplasm
EC: 2.1.1.74
|
Q74A44 | MTGAVTIIGGGLAGCEAAWQIAGRGVRVVLREMKPQRYSPAHHLSGLAELVCSNSLRGESLENAVGLLKEELRRAGSLIMAAADATRVPAGGALAVDRELFSSYVTERIEGHPLIELVREEVTELPAEGVLVIASGPLTSDALAERLKQITGDSLYFYDAIAPIVAADSLDSDKVFRASRYGKGDGDDYLNCPLSEEEYERFVDAVLAAEKVPARDFEKVVHFEGCMPVEEMAERGRETLRFGPLKPVGLTDPRTGREPHAVVQLRAENREGTLFNLVGFQTKLTWPEQRRVFRMIPGLESAEFVRLGSMHRNTFINAPTLLEPTFRLKGDPRTFFAGQITGVEGYVESAGSGFLAGINSARLVRGEDPAVPPPVTALGALVAHITTAPARHFQPMNVNYGLFPPLEGKVKKKDRRGRLAERALAELDHWLATV | 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 Length: 434
Subcellular Location: Cytoplasm
EC: 2.1.1.74
|
Q5NPP5 | MQPVNIIGGGLAGSEAAWQLASRQIPVRLFEMRGREKTPAHSTDKLAELVCSNSFRSDDPNSNAVGVLHAEMRKMGSLIMMIADQHRVPAGSALAVDREGFAEAVTNRLQNHPLIEIHRERIDHIPDETTIIASGPLTSDSLANAITELTGRDALSFFDAIAPIVYRDSIDMDIAWFQSRWDKGDGHDYINCPLNKEEYLAFHAALLAGEKGDFHEWEKDTPYFEGCMPIEVMADRGIDTLRFGPMKPVGLDDPRTGRWPYGAVQLRQDNALGTLWNMVGFQTKLKYAEQIRIFRMIPGLEKAEFARLGGMHRNSFIRSPVLLDEYLRLKKQTNIRFAGQITGCEGYIESASIGLLAGIFTAADKLDKKVSSPPVESALGALLGHITKNADPDHYQPMNINFGLFPPISEKHPKKQRKAMMAERARKALDQWISEEAFLKSSILEQ | 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 Length: 446
Subcellular Location: Cytoplasm
EC: 2.1.1.74
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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 Length: 211
EC: 2.1.1.34
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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: Cytoplasm
EC: 2.1.1.223
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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: Cytoplasm
EC: 2.1.1.223
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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: Cytoplasm
EC: 2.1.1.223
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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: Cytoplasm
EC: 2.1.1.223
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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: Cytoplasm
EC: 2.1.1.223
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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: Cytoplasm
EC: 2.1.1.223
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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: Cytoplasm
EC: 2.1.1.223
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B8M9K4 | MAPNFPPIEEALPLHHDLFYDGKWQTPITDSRRETLNPSTGQVIGKIADASTTDVDKAVEAAHKAFLSWKKTTMAERQGYMRRAAAILREHAAELALVESYNTGNPVAAMVIDAERAANALDYFAGLIPMLRGEVLPGPFPTEDYLHYTVREPMGVVARFVASNHPFMFAGARMASVIAGGNTVIIKPPEQAPLSCLRLAELLENVFPPGVVNILPGGAECGQALTCHPLVRKVSLIGSVATGKIIMRNAGSLMKQTSMELGGKNALIAFPDADIDHLVRSVAAGMNFTWAGQSCGSTSRVFLHDSIHDEVLARVVEVVRKGFRPGLATDPTTTMGSLISKAAQDRVLNYIASAREEGARLVTGGGMFDDLAGTPVEGGFFVQPTIFADVTPDMKIAREEIFGPVMSVLRWSDESELIRIVNSTNYGLTGSIFTKDLATAQRMIRQVEAGFVWVNDVCKHFLNVPYGGIKDSGIGRDECIDELFAYTNIKSVNINLGGATHLGSRLSQAGQISNT | 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 monooxygenase tropB to yield a dearomatized hydroxycyclohexadione . The 2-oxoglutarate-dependent dioxygenase tropC then performs the oxidative ring expansion to provide the first tropolone metabolite stipitaldehyde . Trop D converts stipitaldehyde into stipitacetal which is in turn converted to stipitalide by the short-chain dehydrogenase/reductase tropE . The next steps involve tropF, tropG, tropH, tropI and tropJ to form successive tropolone maleic anhydrides including stipitaldehydic, stipitatonic and stipitatic acids .
Catalytic Activity: an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH
Sequence Mass (Da): 55559
Sequence Length: 515
Pathway: Secondary metabolite biosynthesis.
EC: 1.2.1.3
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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 monooxygenase tropB to yield a dearomatized hydroxycyclohexadione . The 2-oxoglutarate-dependent dioxygenase tropC then performs the oxidative ring expansion to provide the first tropolone metabolite stipitaldehyde . Trop D converts stipitaldehyde into stipitacetal which is in turn converted to stipitalide by the short-chain dehydrogenase/reductase tropE . The next steps involve tropF, tropG, tropH, tropI and tropJ to form successive tropolone maleic anhydrides including stipitaldehydic, stipitatonic and stipitatic acids .
Sequence Mass (Da): 28201
Sequence Length: 254
Pathway: Secondary metabolite biosynthesis.
EC: 3.1.1.-
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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 substrate for the FAD-dependent monooxygenase tropB to yield a dearomatized hydroxycyclohexadione . The 2-oxoglutarate-dependent dioxygenase tropC then performs the oxidative ring expansion to provide the first tropolone metabolite stipitaldehyde . Trop D converts stipitaldehyde into stipitacetal which is in turn converted to stipitalide by the short-chain dehydrogenase/reductase tropE . The next steps involve tropF, tropG, tropH, tropI and tropJ to form successive tropolone maleic anhydrides including stipitaldehydic, stipitatonic and stipitatic acids .
Sequence Mass (Da): 29391
Sequence Length: 266
Pathway: Secondary metabolite biosynthesis.
EC: 1.-.-.-
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Q8L7L8 | MVSHKCVEEFGYASYLVPSNARAPRSARKRRSIEKRISKEDDNMCAIDLLATVAGHLSFESGSSLMSIDKLIEDHRVKEEFPEEEKPLMPVALSPYRGSLSPCGFSSVINGKVENEVDGFSYSGGSDACQVGNFSQDVKPDIDGDAVVLDARPNVVVSLGSSSRTEVPSIGNCVSHGVRDDVNLFSRDDDENFSKYIHPRVTKHSPRTVPRIGDRRIRKILASRHWKGGSRHSDTKPWRNYYLHQQRSYPIKKRKNFDHISDSVTDDYRMRTKMHRGSRKGQGASFVASDSHVKLRIKSFRVPELFIEIPETATVGSLKRMVMEAVSTLLSDGHRVGLMVQGKKVRDDNKTLHQTGISQDNSHLDSLDFSLEPSSEMPQLLTSHPLGHACEELLPVCQATKIDNVLESDHHDSALFPSDSLGNNNVTEDSKAMISVALNELSSQSQPPSRKSRRSEQQQQQAAQRRIRRPFSVAEVEALVQAVEKLGTGRWRDVKLCAFEDADHRTYVDLKDKWKTLVHTAKISPQQRRGEPVPQELLNRVLNAHGYWTQQQMQQLQQNVNKLEQETQSQTTEGLLLL | 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.
Subcellular Location: Nucleus
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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: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5.
EC: 4.2.1.20
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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: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5.
EC: 4.2.1.20
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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: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5.
EC: 4.2.1.20
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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: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5.
EC: 4.2.1.20
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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: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5.
EC: 4.2.1.20
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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: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5.
EC: 4.2.1.20
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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: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5.
Subcellular Location: Plastid
EC: 4.2.1.20
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Q9Y8T5 | MVSVPLRWYNIAADLPEPLPPLRDPEGLREESRIALLSRILPSRLIEDEYILARWVDIPGEVRKALARIGRPTPLIRAEGLEKVLGVKGRVRIYYKSEAVLPTGSHKINTAIAQAYYAKLDGAKEIVTETGAGQWGLAASTAAALMGLKATVFMTASSFKSKIQRRLLMEAQGARVISSPSKLTDTGREALEEYGSTHPGSLGLAIAEAVEYTLESGDRRYLPGSVLEAVLMHQTVIGLEALDQLPEEPDVVVACVGGGSNFGGFTYPMIGARLRGEGFEKTRFIAAESTAAPKLTRGEYRYDGLDSSLILPLAKMYTLGHRYTPPPSHAAGLRYHGVSPSLSILRRLGLVEAEAIPQEEALASILLMARSEGVVPAPESSHAVALAARIARKLPDGSVVAFNLSGHGLLDLDALQKALEIRGASMW | 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-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5.
EC: 4.2.1.20
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O66923 | MYNYPDERGYFGPFGGKFVPETLMYALEELEEKYRELKSDPEFQKELDYYLREYAGRPTPLYFAEKLTKYVGGAKIYLKREDLLHTGAHKINNTIGQCLLTKRMGKKRVIAETGAGQHGVATATASALFGLECVVYMGEEDAERQALNVFRMKLLGAKVEIVKSGSRTLKDAINEALRDWVTNVESTHYVIGSVVGPHPFPMIVRDFQSVIGRETKEQILQKEGRLPDAIVACVGGGSNAMGIFYPFVEDKGVQLIGVEAGGYGLETGQHAASICGGSVGILHGMKSYFLQDEEGQIQPTHSISAGLDYPGVGPEHALFHEIKRAKYTTATDEEALEGFKLLARTEGIIPALESAHAVIKAVEVARELGKDGIVVINLSGRGDKDMAHVMKHLSLEG | 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-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5.
EC: 4.2.1.20
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P14671 | MAASGTSATFRASVSSAPSSSSQLTHLKSPFKAVKYTPLPSSRSKSSSFSVSCTIAKDPPVLMAAGSDPALWQRPDSFGRFGKFGGKYVPETLMHALSELESAFYALATDDDFQRELAGILKDYVGRESPLYFAERLTEHYRRENGEGPLIYLKREDLNHTGAHKINNAVAQALLAKRLGKKRIIAETGAGQHGVATATVCARFGLECIIYMGAQDMERQALNVFRMRLLGAEVRGVHSGTATLKDATSEAIRDWVTNVETTHYILGSVAGPHPYPMMVRDFHAVIGKETRKQALEKWGGKPDVLVACVGGGSNAMGLFHEFVNDTEVRMIGVEAAGFGLDSGKHAATLTKGDVGVLHGAMSYLLQDDDGQIIEPHSISAGLDYPGVGPEHSFFKDMGRAEYYSITDEEALEAFKRVSRLEGIIPALETSHALAYLEKLCPTLSDGTRVVLNFSGRGDKDVQTVAKYLDV | 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-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5.
Subcellular Location: Plastid
EC: 4.2.1.20
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Q8TLP3 | MTETKVSEFQLKGKYGKYGGQYVPEVLMPALEELDVGYEKYKNDPESLAELDHYLRDFAGRETPLYFARNLSKKYGTKVYLKREDLVHGGAHKLNNALGQALLAKFMGKTRLIAETGAGQHGTATAMVGATLGFETIVYMGAKDIKRQQMNAYRMELMGTEVRAVETGSKTLKDAINEAMRDWVTNIENTHYLIGSVVGPHPYPMIVRDFQSVIGKEVKEQAMEKEGRLPDSIIACAGGGSNAMGTFHPFIEDREVKLIAVEAGGKGLKCTEKAALHSASLCIGEEGILHGARTKILQDKNGQILESESVSAGLDYSGVGPELAYLSESGRVTARYVTDDEALDAFNELSRLEGIIPALESSHALAYLKKAAESGELGEFVVVNLSGRGDKDLETVLSLRRGV | 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-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5.
EC: 4.2.1.20
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Q9V1G8 | MWFGKFGGQYVPETLMEPLRELEKAYKRLKNDEEFNRQLDYYLRTWAGRPTPLYYAERLTKKVGGAKIYLKREDLLHGGAHKTNNAIGQALLAKFMGKTRLIAETGAGQHGVATAMAGALLGMKVDIYMGAEDVERQKMNVFRMKLLGANVIPVHTGSKTLKDAINEALRDWVATFEYSHYLIGSVVGPHPYPIIVRDFQSVIGREAREQILEAEGDLPDVIVACVGGGSNAMGIFYPFVKDKSVRLIGVEAGGKGIESGKHSASLNAGEIGVFHGMLSYFLQDEEGQIRTTHSIAPGLDYPGVGPEHAYLKESGRAEYVTVTDEEALRAFHELSRTEGIIPALESAHAVAYAIKLAREMSRDDVIIVNLSGRGDKDLDIVLKVSGNV | 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-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5.
EC: 4.2.1.20
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P50383 | MVKEDEILPKYWYNIIPDLPKPLPPPRDPQGAYFSRIDLLRSILPKEVLRQQFTIERYIKIPEEVRDRYLSIGRPTPLFRAKRLEEYLKTPARIYFKYEGATPTGSHKINTAIPQAYFAKEEGIEHVVTETGAGQWGTAVALAASMYNMKSTIFMVKVSYEQKPMRRSIMQLYGANVYASPTNLTEYGRKILETNPQHPGSLGIAMSEAIEYALKNEFRYLVGSVLDVVLLHQSVIGQETITQLDLLGEDADILIGCVGGGSNFGGFTYPFIGNKKGKRYIAVSSAEIPKFSKGEYKYDFPDSAGLLPLVKMITLGKDYVPPPIYAGGLRYHGVAPTLSLLTKEGIVEWREYNEREIFEAAKIFIENQGIVPAPESAHAIRAVVDEAIEARKNNERKVIVFNLSGHGLLDLSNYESMMKRLNGNG | 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-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5.
EC: 4.2.1.20
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Q8RGH8 | MTTENKKGYFGEFGGSYVPEVVQKALDKLEEAYNKYKDDEEFLKEYHHYLKNYSGRETPLYFAESLTNYLGGAKIYLKREDLNHLGAHKLNNVIGQILLAKRMGKKKVIAETGAGQHGVATAAAAAKFGMQCDIYMGALDVERQRLNVFRMEILGATVHAVEKGERTLKEAVDAAFKAWINNINDTFYVLGSAVGPHPYPSMVKDFQRVISQEARRQILEKENRLPDMIIACVGGGSNAIGAFAEFIPDKEVKLIGVEAAGKGLNTDRHAATLTLGTVDVLDGMKTYALFNEDGSVKPVYSISPGLDYPGIGPEHAFLRDSKRAEYVSATDDEAVNALLLLTKKEGIIPAIESSHALAEVIKRAPKLNKNKIIIVNISGRGDKDVAAIAEYLKNK | 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-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5.
EC: 4.2.1.20
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B0R332 | MSTNTDDTTRTDGTFGDYGGQYVPEVLMPAVEELTDAYERYVLDNEDGFVDDFRQRIRSFGGRPTPLTHAPTLSQRHGVDVYLKREDLLHGGAHKLNNALGQVLLAKYMGKDRIVAETGAGQHGTATAMACAALEMPCEIYMGRTDVNRQRPNVFRMRLHDADVNPVTVGSGTLKEAINETMRDWATNVADTHYVIGSVVGPHPFPSMVRDFQAIISEELRAQSREQLGELPAAVIACAGGGSNTMGAFGAFVGSASLPGAPAGTHEPAPDVDLLAVEAGGSRLGVDDDAGYAPNSASLSTGTEGVLHGARTKLLQTETGQIVESHSVSAGLDYAGVGPELAHLVDTGRITPTNVDDDAALAAFHRLSRDEGVIPALETSHAVAALDQYDGDGPVVVNVSGRGDKDLDTVIEASAANDIDAAPDMEVFEQ | 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-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5.
EC: 4.2.1.20
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Q7VGA7 | MKKKIFTESKNGYFGEAKGGNHAFGGQYIPEILLPALKELEKAYHGVFVSKAYKKELKSLFKHFVGRPTPLIYAHNASKILKNDIYLKFEGLANTGAHKINNALGQVLLAKHMKKKRVIAETGAGQHGLATAAACARLGLECEIFMGEIDIARQRPNVFNMELFGAKVHSVSSGSKTLKDAVNEALREWSKRSDDSFYVLGSALGPYPYPDIVRDLQSVISKELKKQTKAYFSSLPDILVACVGGGSNAMGFFTHYLKEERVRLIGVEAGGIGDKEGENAIRINTINASEGIAQGYKSLFLQDKDGQLSDTHSISAGLDYAGIGPQLAHLYEVGRVEFQSATDKEALEALSFFAQYEGIIPALESSHALAAVIRLCKDIKGKKIIANISGRGDKDIFITAKALTPEHWKTFLSEEIARIG | 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-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5.
EC: 4.2.1.20
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P56142 | MNKKAYFGEFGGSFVSELLVPALRELEQAFDACLKDEKFQKEYFRLLKDFVGRPSPLTLCQNIVSNPKVKLYLKREDLIHGGAHKTNQALGQALLAKKMGKTRIIAETGAGQHGVATAIACALLNLKCVVFMGSKDIKRQEMNVFRMHLLGAEVREVNSGSATLKDAVNEALRDWASSYKDTHYLLGTAAGPHPYPTMVKTFQKMIGDEVKSQILEKENRLPDYVIACVGGGSNAIGIFSAFLNDKEVKLIGVEPAGLGLETNKHGATLNKGRVGILHGNKTYLLQDDEGQIAESHSISAGLDYPGVGPEHSYLKESGRAVYESASDAEALEAFKLLCQKEGIIPALESSHALAYALKLAQKCEEESIIVVNLSGRGDKDLSTVYNALKGGLK | 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-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5.
EC: 4.2.1.20
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Q2FH64 | MNKQIQTEADELGFFGEYGGQYVPETLMPAIIELKKAYKEAKADPEFQRELEYYLSEYVGRATPLTYAASYTESLGGAKIYLKREDLNHTGAHKINNALGQALLAKRMGKKKLVAETGAGQHGVASATVAALFDMELVVFMGSEDIKRQQLNVFRMELLGAKVVAVEDGQGTLSDAVNKALQYWVSHVDDTHYLLGSALGPDPFPTIVRDFQSVIGKEIKSQILKKEGRLPDAIVACIGGGSNAIGTFYPFIKDDVALYGVEAAGQGDDTDKHALAIGKGSPGVLHGTKMYLIQDEDGQVQLAHSISAGLDYPGIGPEHSYYHDIGRVTFENASDTQAMNALINFTKHEGIIPAIESAHALSYVERLAPTMSKEDIIVVTISGRGDKDMETIRQYMVERGLAND | 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-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5.
EC: 4.2.1.20
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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
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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
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P24920 | MGNILEEIAAQRRLDVAAAKQVVSTDDLAKKIEHTESVYGPALPVLERLNAPAEQVQAYANAGASMISVLTEPKWFKGSLDDMMEAREVVEGMSQRPAILRKDFIIDVYQLLEARAYGADCVLLIVTLLSKEQLIELIDATHNLGMCALVEVNSVQELDIALAAKARLIGVNNRDLRTFKVDMNTTARVADAIRERGLSLGRDGVALFALSGIRSHTDVVKYEKCGARGILVGEYLMKSGDIATTVKDLLQNVTRHSESGEFALLPPLAKVCGITTVEYALAALRNGANMIGIIMAEHSPRYVEKEEAKAIAKAVREYGERTGPILSDILESHLDDKSDWFHRNVLALREACSRAPLVVGVFVNKTATEMNAAAEEIGLDLVQLHGDEGFEICKDIKYPTIRALHLPDTAQCDGVDAEAVLQQVSEGLANYILLDTTVKGQQGGTGVAFDWKIAAIFTQARLPCLMAGGLTPENVVKALSVGHPVGVDVSSGVEVKGSPGVKDLDKVAAFLKAVKDHLSVATLKIDEETEN | 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 biosynthesis; L-tryptophan from chorismate: step 3/5.
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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
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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
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P59415 | MKIILNKIYQGDTLNISETYTLFKSIMLKKINNIELSAILIALKIRGESQNEILGAVKACLEHMITFPKPTYMFSDIVGTGGDNSNSINISTTSALVGSACGFKIAKHCNGNISSKTGSADILKKFGINIQISPEKSKKMLDELNICFLFAPQYHINFKVVTQVRKILRIKTIFNIIAPLLNPAMPKLTVMGVCNFKLMLPIAQVLKTLNYHHAIIVCSDNIDEVTLHSFTKIIELKNNNITSYILHPDDFGVKYCHKNDILGGNTEENYNIIKKILQGKGPSAVTETIAVNVAILFKIFGYSNLKKNTEYALKVIRSGKVYEKIIQLSKF | 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): 36907
Sequence Length: 331
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 2/5.
EC: 2.4.2.18
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Q2FKX5 | MIQDTIRKVVSMQDLAPDEARDLMTSIADGKVTDAQIGSILTALSMKGVTAHEITAFAHVLRDRAVQLKTDTSGTFVDTCGTGGDGAHTFNISTAAALVAAAAGVRVVKHGNRGVSSRSGSADVLEALGIPITLTPEEAAASVSSHNIAFLFAPGYHPAIGRVASARREIGFFSVFNILGPLLNPAGASARLIGVGDTRHIPSITGALANLGVSHAMVVHGDGTDEITITGETEVYELSGGTICRYTLTPEEFGIRRVSRETIAGGSPAENAEIIMDIFSGRKGPCRDIVLLNAAAAIYLGEKATCIYDGYRIAREVVDSGQAYRLVMALRRTT | 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): 34995
Sequence Length: 334
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 2/5.
EC: 2.4.2.18
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Q57686 | MITEALKKVIEFKDLDEKEAEAVMKDIMSGNAKPTQIAAILTALRMKGETIEEITAFAKIMREFSLKINPNVPKLLDTCGTGGDNLNTFNISTATAFVVSAYVPVAKHGNKAVSSKSGSADVLEALGVNLNVPIERVKESIEKIGIGFLFAPHFHPAMKFATPVRKELGIRTVFNVLGPLTNPANANYQLMGVYDEKLTEKLANVLKNLGLKGALVVHGSGMDEITTIGKTKISELRNGEIKSYYIEPEDFGIKKAKLEDIRGGDAEENAKIIGEIFEGEEVGAKRDIVVLNAAFALYIAEEAKDVEEGIKLAEKSIDEGKALKKLEDLIEFYREG | 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): 36630
Sequence Length: 336
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 2/5.
EC: 2.4.2.18
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Q8TXJ5 | MSVLERIIRGSDLDREEARDLMCRIVGGELSDVEVAGILVALRCKGYTSEELVGFVDGMMEHAVKVDPDVERLVDTAGTGGDELDTFNASTLAGLTAAAAGVPVAKHGNRSVTSECGSADILEALGVNIEADPDTVKRCIEEVGFGFMFAPKFHPAMKNVMPVRRKLGIRTVFNVLGPLTNPARERVTGQVIGVYSENLLDLVAGALAELGVRRGLVVYGLDGVDELSVTCENEVVYVDDGEVTDRDTVAPEDVGLDRADPKDVAGADPETSAEEARKILGGELPVDHPKVQMTAFNAGAALYVGEAVDSLEKGIQRALDVLEEGRALEVLEKVVDLSS | 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): 36019
Sequence Length: 339
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 2/5.
EC: 2.4.2.18
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A2STA7 | MIAECIKKVASHSDLSVYEAKGAMQDIMSGNATDGQIGAFLTALVMKGETSSEIAAFASVMRENAVQITPKRNGMLVDTCGTGGDGKNTFNISTAAAFTAAGAGVTVVKHGNRGATSKCGSADVLEALGIKIDISPERVCEIIDENGIGFMFAQSHHPAMKYAGKVRKEIGIRSFFNLIGPLSNPAGADAQLLGVYDSPLTEKIAEVLNILGTKRAMVVHGDGYDEITTTGITQVSEVNDGQVRSYSLDPSSFGFQKADAASLFGGDSQYNAHIIRSVLSGDEGPRRDIVILNAAAAIYLGERAGSIADGIKYAEKSIDSGLALEKLENLILLSGGKNDS | 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): 35571
Sequence Length: 340
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 2/5.
EC: 2.4.2.18
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B1M5Q2 | MDSFRPHLAKVAGGLALDRAEARAAFDDLLSGEVTPVQAGAFLTALKVRGESVEEIVGAAEAMRARMTRVAAPENAVDVVGTGGDHSGSVNVSTLAAIVVAACGVPVAKHGNRAATSRSGAADVLAALGVRLGLDPAAQARCLDEAGLCFLFAQAHHPAMRHVAAVRSELPVRTIFNLLGPLSNPAGVGYQLFGVAQAALAEPLTRVLAELGSRRVWTVHGSDGLDEITVTGPTQVVALDEGRLCHFTIDPREFGLALRAPEELRGGDPADNARSLEAVLAGARNAYRDIAVLNAGAALVVAGAAQALADGVAQAQDAVDSGAARATLARLVRASNDHSNGQEGR | 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): 35337
Sequence Length: 345
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 2/5.
EC: 2.4.2.18
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A5UMC1 | MIKEAILKVVNGNDLNAKEAYGAMDEIMSGESSEVQMSAYLTALSMKGETIEEITASTKAMRAHCVKLLNDEEVLEIVGTGGDGSNTFNISTTSSIVISAAGVPVAKHGNRSASSKCGAADVLEALGVNIYIEPEKSLKILKEINLCFLFAQNYHLAMKFVAGVRKELSIRTIFNILGPLTNPAGATMQVLGVYDESLVKPLCEVLKNVGVKSALSVYGQDGLDEISVSDKTSVCELRDGRLKCYEIAPEDFGMERCSKEDLVGGNPRENAEITLSILNGQKGPKRNAVVLNSAAALYVAGKADSIEDGVRLASEIIDSGRAKKQLEKFIEYTNS | 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): 35893
Sequence Length: 335
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 2/5.
EC: 2.4.2.18
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A4YHE2 | MDPKEVLKRLTEGVSLSQEEAKELADLIMEGSIPEPLVAGILVALKMKGETPDEIIGFVNSMRQHALKLDLRNTLDTAGTGGDGIGTINVSTATALAVSSVFPVAKHGNRAASSRSGSADFLESLGYNIQVPPEKAKDLLSRNNFVFLFAQLYHPSMKNVAPVRKVLGVRTIFNLLGPLTNPAGSERQVMGVYSLPFMRKLAEAALKLGYVKLVLVHGEPGLDEVSPQGKTYITEVTGSKVEEYTYDFSEIIGQPVPVSRLTTTDPLDSVRRVLMASMGRDEAVEKFIRINVSVALYTAGLVSDFKDGFELSEELVRKLPDRIETLVRDNGDPSKIKAIKGSL | 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): 37229
Sequence Length: 343
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 2/5.
EC: 2.4.2.18
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A7NL64 | MPIRDQIIQIVRGHDLTEEQAAEAMEEIMTGVATPAQVAALLTALHLKGETDAEIAGMARVMRAKAIPVHFDGPLLDTCGTGGDSAGTFNISTTAAFIAAGAGATVAKHGNRAMSSVCGSADVLEGLGVTIDLDAAGVARCLEQAGIGFMFAQKFHPAMRFVGPVRREIGIRTIFNALGPLSNPAQARHQTLGVADPALAEKMARALYLLGAQHALVVHGHGGLDELTLSGPNLVIEVRAGHKPRRYEVSAGDLGLTPAPREALLGGDVSTNVAIVRAILSGEERGARRDVALLNAAAALVAADYAADLREGLQQARQSLESGAALARLERLITVSSINR | 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): 35360
Sequence Length: 340
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 2/5.
EC: 2.4.2.18
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Q163Y0 | MSDALKPLIGAAADRALSRAEAEDAFRILFEGEATPSQIGGFLMALRTRGETVAEYAAAASVMRAKCNAVKAPAGAMDIVGTGGDGKGTLNISTATAFVVAGAGVVVAKHGNRNLSSKSGAADALSQMGLNVMVGPEVVERALAEAGIGFMMAPMHHPAIAHVMPTRAELGTRTIFNILGPLTNPAGVKRQLTGAFSRDLIRPMAQTLGALGSEKAWLVHGSDGTDELTITGVSWVAALGPDGSVTDMEIHPEDAGLPVHPFEAIVGGTPAQNAADFKALLAGEASAYRDAVLLNAAAALVVADAASTLQDGVEMAATSIDSGAAARKIEAVAQITQAT | 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): 34388
Sequence Length: 339
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 2/5.
EC: 2.4.2.18
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Q1AU89 | MLREALRKAAAGEPLSEGEAERALETIMEGGASPEATAALLTALRVRGESVQEIVGFARAMRRFAARVRAPEGVVDTCGTGGDAKGTINVSTAAAFVARGAGVVIAKHGNRAATSRAGSADVLEALGAAIELSPEQVSRCIEEAGIGFMFARTHHPAMRHVAPVRAELPFRTVFNLLGPLTNPAGARRQLVGVFSAGYVRPMAEALEGLGAERALVVHGRDGMDEITVTGPTLVAEVGGGGVEEYEISPEDFGLSRHAPDGLLGGDAHLNARILRDVLSGEERGASRDVIVLNAGAAIYVAGKAPSIEEGVRLAEGSLESGAALAALERFVRVSRRLAGRGA | 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): 35379
Sequence Length: 342
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 2/5.
EC: 2.4.2.18
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Q1GHJ3 | MSDALKPLIGLAADRALTRTEAETAFAALFNGEATPSQMGGLLMALRTRGETVDEYAAAAAVMRAKCNKVSAPADAMDIVGTGGDGKGTLNISTATAFVVAGAGVPVAKHGNRNLSSKSGAADALTEMGIQVMVGPKVVEKSLKEAGICFMMAPMHHPAIAHVMPTRQELGTRTIFNILGPLTNPADVKRQLTGAFSRDLIRPMAETLKQLGSEVAWLVHGSDGTDELTITGVSWVAGLSEDGNISEFEVHPEEAGLPEHPFEAIVGGTPAENAAAFRALLEGTPSAYRDAVLLNSAAALKVAGVVSSLKEGAERAAESIDSGAALGKVTAVARITSEAS | 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): 34984
Sequence Length: 340
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 2/5.
EC: 2.4.2.18
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B8I0U9 | MIQEAIYQVINKQDLDLDKTIQVMEEIMEGRATNAQIGSFLTAMRMKGETIDEITACATVMRQKCKRIHPEKDVLDIVGTGGDEANTFNISTVSSFVVSAGGVPVAKHGGRSVSSKCGSADLLEALGINIALSAEQSAEILQKIGMCFMFAPTYHASMKYAAPVRKELSVRTIFNILGPLANPAGANMQLLGVYDENLVEPLARVLLNLGVKRAMVVHGHDGLDEVTLCNTTTICEVSNGNINSFFLSPEQLGFSRCLLKELVGGDPKKNASIALDILNGSKGPKRDIVVLNSALCLYMSYNQITLRDCVKMAEQLIDSGAAKAQLNKFIELSNSFNQEVK | 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): 36906
Sequence Length: 341
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 2/5.
EC: 2.4.2.18
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P50384 | MNINEILKKLINKSDLEINEAEELAKAIIRGEVPEILVSAILVALRMKGESKNEIVGFARAMRELAIKIDVPNAIDTAGTGGDGLGTVNVSTASAILLSLVNPVAKHGNRAVSGKSGSADVLEALGYNIIVPPERAKELVNKTNFVFLFAQYYHPAMKNVANVRKTLGIRTIFNILGPLTNPANAKYQLMGVFSKDHLDLLSKSAYELDFNKIILVYGEPGIDEVSPIGNTFMKIVSKRGIEEVKLNVTDFGISPIPIEKLIVNSAEDSAIKIVRAFLGKDEHVAEFIKINTAVALFALDRVGDFREGYEYADHLIEKSLDKLNEIISMNGDVTKLKTIVVKSSG | 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): 37574
Sequence Length: 345
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 2/5.
EC: 2.4.2.18
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Q2S1Z6 | MNTLLQTIADGDPLSRPEAEEAMATMMSGSARDEHIAALLMGLRTRGETLDELVGFTKTMREFAVSVETDDPQTIDLCGTGGDGASTFNISTTASFIAAGAGATVAKHGNRSVSSQSGSADVLEALGVQIDLEKEGVEHCLHEAGIAFLFAPFFHPAMRHVMPVRKALGVRTFFNILGPLCNPAGVTRQIVGAFDTSTAQTMVRILAELDADHVITLHADDGLDEVSISASTTLFEYDASDQNPVPRSHEVGPERHDLDRASISTLEGGTAQQNASILRNILSGEDQGPRRDVALLNAAYALHVSDQYADLDACLEAAAESIDSGAALDALNTLASVSKEAKSE | 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): 36308
Sequence Length: 344
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 2/5.
EC: 2.4.2.18
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O60122 | MINTFNPEVRLAIHDLDKVGPAIPLENYEAALRAILTGKASPVETASFLASLHLTKAEEVPDILMQTVQILKSYSTPIANIEMVSPRFVDIVGTGGDGHNTFNVSTASAIVAAGAGLWVCKHGNKASTSASGSADLLMSFGCDLLNVTPKNIVSITEQCKFSFLFAPMCHPTLKNVAPIRKQLGLPTIFNLVGPLLNPIPTYARIIGVSKLSLGEVVAKTLLKLGAGRSLVVCGEEGLDEISPAGPTHTWLVRDGTITHEVYTPESFHLQSHPLSSVASGTPSANAILLEELLSNMLHANHPILDYVLMNTAALLHVAGMAESLREGVKIAQQSISSGAALRELSNFSTISQQP | 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
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Q06128 | MEVHPISEFASPFEVFKCIERDFKVAGLLESIGGPQYKARYSVIAWSTNGYLKIHDDPVNILNGYLKDLKLADIPGLFKGGMIGYISYDAVRFWEKIRDLKPAAEDWPYAEFFTPDNIIIYDHNEGKVYVNADLSSVGGCGDIGEFKVSFYDESLNKNSYERIVSESLEYIRSGYIFQVVLSRFYRYIFSGDPLRIYYNLRRINPSPYMFYLKFDEKYLIGSSPELLFRVQDNIVETYPIAGTRPRGADQEEDLKLELELMNSEKDKAEHLMLVDLARNDLGKVCVPGTVKVPELMYVEKYSHVQHIVSKVIGTLKKKYNALNVLSATFPAGTVSGAPKPMAMNIIETLEEYKRGPYAGAVGFISADGNAEFAIAIRTAFLNKELLRIHAGAGIVYDSNPESEYFETEHKLKALKTAIGVR | 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.
Catalytic Activity: chorismate + L-glutamine = anthranilate + H(+) + L-glutamate + pyruvate
Sequence Mass (Da): 47652
Sequence Length: 421
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 1/5.
EC: 4.1.3.27
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P00898 | MQTPKPTLELLTCDAAYRENPTALFHQVCGDRPATLLLESADIDSKDDLKSLLLVDSALRITALGDTVTIQALSDNGASLLPLLDTALPAGVENDVLPAGRVLRFPPVSPLLDEDARLCSLSVFDAFRLLQGVVNIPTQEREAMFFGGLFAYDLVAGFEALPHLEAGNNCPDYCFYLAETLMVIDHQKKSTRIQASLFTASDREKQRLNARLAYLSQQLTQPAPPLPVTPVPDMRCECNQSDDAFGAVVRQLQKAIRAGEIFQVVPSRRFSLPCPSPLAAYYVLKKSNPSPYMFFMQDNDFTLFGASPESSLKYDAASRQIEIYPIAGTRPRGRRADGTLDRDLDSRIELDMRTDHKELSEHLMLVDLARNDLARICTPGSRYVADLTKVDRYSYVMHLVSRVVGELRHDLDALHAYRACMNMGTLSGAPKVRAMQLIADAEGQRRGSYGGAVGYFTAHGDLDTCIVIRSALVENGIATVQAGAGIVLDSVPQSEADETRNKARAVLRAIATAHHAQETF | 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.
Catalytic Activity: chorismate + L-glutamine = anthranilate + H(+) + L-glutamate + pyruvate
Sequence Mass (Da): 57088
Sequence Length: 520
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 1/5.
EC: 4.1.3.27
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P21690 | MFLFVETIRPQQRGESLLETVIKVVPGERFTPYGLALKLGARVVLESSSSKKGRDRYSLLLLQEAFRVAQEGTEVYFVKDGRRSKVKANHRDILDVLMYFARQHSDPGQDFPFPAGGVGYLSFEFCRYCDTIHLNPAKPDPLELPDALFLFGHVFLIYDHYTDLIYLVGLNYKEASIDLEAALAAVEARVNDGDWSALGSVGAPYDAEVLPQDYDPDETYKANVGAMRQEVIAGNLLQGVPSRRLLVKTEMPAIEAYRRLRSSNPSPYMFYLDFGDYQLFRASPELHVKVKGGTAEIRPIAGTRRRGATDAEDRALEAELLADVKERAEHLMLVDLARNDLGRICQPGTVQVKDSYFIERYSHVMHIVSSVEGRLKDDKTGIDALRASFPAGTVSGAPKIRAIEVIDRLEPVQRRFYSGVVGHLSPDGSLDTCIAIRSALKKGDTMVLQAGGGIVFDSNPDRELEETYEKMRATARSLGLEI | 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): 53699
Sequence Length: 482
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 1/5.
EC: 4.1.3.27
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Q9Z4W7 | MTTHAAEAPTTDPQGAPGSQKTPDATEAEEAARATVPHRAAAAALAREHDVVPLHQEFLDDSVSPVTAFAQLCGPDEAGFLLESVPVSGGVARYSYVGHRPVPLEPTGGDPLTALRSHLARSVAPVPGLPPFHGGVVGYLGYEAARHFEDLPLAAGPPPGLPESAFLAADDLVVFDHATRRVLLMTLYRPARESYDDAVARIVRLNRALRRAPAPAAFSGRPLAAATPADHGTQGWTANLTEAQFTERVARAREHIAAGDAFQIVLSRRLSRPLRARPTDLYRHLRATNPSPYMYHLSLGGGRHVIGASPELLVKAEGRTVRTRPLAGTRPRHPDPAEDLRLERELRADEKERAEHVMLVDLGRNDLGRVTEPGTVRVERLMRVERFSHVMHLSSTVRGRLAEGRDALDALRSAFPAGTLSGAPKIRAMEIIAELEPEQRGVYGGALGFVGADGLTDFAIALRTMVVADGHVHVQAGAGIVADSDPAAEFRETLHKSRAMLTAVRRAEAAA | 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): 54829
Sequence Length: 511
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 1/5.
EC: 4.1.3.27
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P20170 | MISPGFSHFTELAQQGNFIPVYQEWVADLETPVSAWYKVCSSQPYNFLLESVEGGESIGRYSFLGCDPMWVLEARGDETTQVLRNGQTETFRGNPLDILSQCLESIRPVNLPQLPPGIGGLFGVWGYELIRWMEPRVPVYEPQPEDPPDGIWMQVDHLLIFDQVKRKIWAIAFADLRGENVDLETAYRNACQRVTKLVLQLQLPLPPEATALELLTKTQLEGKELNYSSNTEQEKFLEEVAIAKDYITAGDIFQVVLSQRLSTIYRDDPFKLYRSLRLINPSPYMAYYNFGHWQIIGSSPEVMVKADRQLDGKLMATVRPIAGTRPRGKTHPEDEQLAEELLNDPKEIAEHVMLVDLGRNDLGRVCVQGSVKVNELMVIERYSHVMHIVSNVVGELASDKTAWDLLKACFPAGTVSGAPKIRAMEIINELEPERRGPYSGVYGYYDFEGQLNTAIAIRTMVVQEQPDGAHRVSVQTGAGIVADSDPQKEYEETLNKARGLLEAIRALS | 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): 57147
Sequence Length: 508
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 1/5.
EC: 4.1.3.27
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Q9YGB3 | MPLKKLKPVDPLKLYSALRDFGMPFMLRSAEKDSRKARFTYISAEPEFVVEVGEGTEIDGERVSDERNPLRALKGLMGERVEGRRFMGGFVGYVSYDSVHSIIGGKIEEPSVFGYYPWTFIYDHSTGALSFFYLREAPFDPEALVERARREESRLEDGGSEVISTDAGMEEFVEIVRAGKEYIYSGDVFQVVLSREYRVRTDLDALEIYKRLVELNPSPYTFILEFEKTVVGASPETMGSVEGRTFKINPIAGTAPRGRTGEEDRELEKALLSDEKERAEHVMLVDLARNDVRRVSKPGSVRLTRFFDVLKYSHVQHIESEVVGELDEGKNAFDAMEAAFPAGTLTGAPKIRAMEIIDELERSRRKVYGGAVGYFSLTGDADMAIAIRMAEIEGRKASVRAGAGIVADSVPEKEFFETENKMRAVLKALGVRE | 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): 48541
Sequence Length: 433
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 1/5.
EC: 4.1.3.27
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Q08653 | MGDSMHVLKLVSDLETPVSTFMKVSRGEEFAFLLESVELGSAFGRHSFIGIGKKDVLVFEKGILRTSNQQLDYTSSPLKAIKDWLEVYRYSVKHDELPSFRGGAVGFVSYDYISYIEKVKVKASVFPTFYFVVPEHLIIFDHLKNNVFIISDSPEELTSKVLSPFEEKPEKNVFVTEPESNFEREQFYKVVEKAKKYIVEGDIFQVVLSQAFTFKTTLDPFYIYRALRMINPSPYMFYLKFGDTVVLGSSPETMAKVEGDKATVKPIAGTRPRGRTVEEDLKLERELLNDEKEIAEHVMLVDLGRNDLGRVCKEGTVRVEKKMVIERYSHVMHIVSQVSGELKDDKDAVDVFEATFPAGTVSGAPKVRAMEIIEELEPTPRGPYAGAVGYFSFPDDKGRMNMDSAITIRSFFFKGKQGWLQAGAGIVYDSVPEREYQETLNKLRALFRSLEVAQKIQGGLF | 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): 52240
Sequence Length: 461
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 1/5.
EC: 4.1.3.27
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P05378 | MERIRPYRKTFLADLETPVTAYLKLAEKAPVSFLLESVERGRQSRFSIVGVGARRTFRLKDGVFTVNGERVETRDPLRALYERVYAPLERHPDLPPFFGGVVGYAAYDLVRYYERLPSLKPDDLGLPDLLFVEPEVVAVFDHLKNLLHLVAPGRDPEEAEARLFWAERRLKGPLPGVPGERAGGRARFQADFSREAYLEAVRRALDYIRAGDIFQVVLSLRLSSPLTVHPFALYRALRSVNPSPYMGYLDLGEVVLVSASPESLLRSDGRRVVTRPIAGTRPRGKDEEEDKRLAEELLRDEKEVAEHVMLLDLSRNDIGRVAAFGTVRVLEPLHVEHYSHVMHLVSTVEGILAEGKTPLDALASVLPMGTVSGAPKIRAMEIIEELEPHRRGPYGGSFGYLAYDGAMDMALTLRTFVVAKGWMHVQAGAGIVADSVPEREYEECWNKARALLKAVEMAEAGL | 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): 51635
Sequence Length: 462
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 1/5.
EC: 4.1.3.27
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P22099 | MRLCTAGRLKQLQGGLVNKAIEIKKLGQLEVLKASVPYTQDPTRLFHTICENKTDSLLLESAEIDSKQNLKSLLIVDSAVRIVCYGHTVSFHALTENGKNLLTHVNQNVRGEVASQFDGETLTLEFIQPCDTIDEDSRLREASSFDALRLVQHSFDLSSQDKHAIFLGGLFAYDLVANFEPLGDAVATNQCPDYVFYVAETLLVVDHQTESCQLQATLFVDGSQKAALESRIEDIRAQCTSPKRLPDATQVANITAQPSVPDQDFCQIVRDLKEFVVKGDIFQVVPSRRFTLPCPSPLAAYKELKQSNPSPYMFYMQDELFTLFGASPESALKYETDTNQIEIYPIAGTRRRGKRPNGEIDFDLDSRIELELRSDKKENAEHMMLVDLARNDVARISQAGTRHVADLLKVDRYSHVMHLVSRVVGQLRDDLDALHAYQACMNMGTLTGAPKIRAMQLIRDVEGARRGSYGGAVGYLTGEGTLDTCIVIRSAYVENGIAQVQAGAGVVFDSDPQAEADETRGKAQAVISAIQAAHSQPANKE | 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): 59771
Sequence Length: 541
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 1/5.
EC: 4.1.3.27
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P00899 | MTASIKIQPDIDSLKQLQQQNDDSSINMYPVYAYLPSLDLTPHVAYLKLAQLNNPDRKESFLLESAKTNNELDRYSFIGISPRKTIKTGPTEGIETDPLEILEKEMSTFKVAENVPGLPKLSGGAIGYISYDCVRYFEPKTRRPLKDVLRLPEAYLMLCDTIIAFDNVFQRFQIIHNINTNETSLEEGYQAAAQIITDIVSKLTDDSSPIPYPEQPPIKLNQTFESNVGKEGYENHVSTLKKHIKKGDIIQGVPSQRVARPTSLHPFNIYRHLRTVNPSPYLFYIDCLDFQIIGASPELLCKSDSKNRVITHPIAGTVKRGATTEEDDALADQLRGSLKDRAEHVMLVDLARNDINRICDPLTTSVDKLLTIQKFSHVQHLVSQVSGVLRPEKTRFDAFRSIFPAGTVSGAPKVRAMELIAELEGERRGVYAGAVGHWSYDGKTMDNCIALRTMVYKDGIAYLQAGGGIVYDSDEYDEYVETMNKMMANHSTIVQAEELWADIVGSA | 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
|
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
|
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
|
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
|
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
|
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
|
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
|
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
|
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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