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trpE

Gene
trpE
Protein
Anthranilate synthase component 1
Organism
Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633)
Length
541 amino acids
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).
Similarity
Belongs to the anthranilate synthase component I family.
Mass
59.771 kDa
Sequence
MRLCTAGRLKQLQGGLVNKAIEIKKLGQLEVLKASVPYTQDPTRLFHTICENKTDSLLLESAEIDSKQNLKSLLIVDSAVRIVCYGHTVSFHALTENGKNLLTHVNQNVRGEVASQFDGETLTLEFIQPCDTIDEDSRLREASSFDALRLVQHSFDLSSQDKHAIFLGGLFAYDLVANFEPLGDAVATNQCPDYVFYVAETLLVVDHQTESCQLQATLFVDGSQKAALESRIEDIRAQCTSPKRLPDATQVANITAQPSVPDQDFCQIVRDLKEFVVKGDIFQVVPSRRFTLPCPSPLAAYKELKQSNPSPYMFYMQDELFTLFGASPESALKYETDTNQIEIYPIAGTRRRGKRPNGEIDFDLDSRIELELRSDKKENAEHMMLVDLARNDVARISQAGTRHVADLLKVDRYSHVMHLVSRVVGQLRDDLDALHAYQACMNMGTLTGAPKIRAMQLIRDVEGARRGSYGGAVGYLTGEGTLDTCIVIRSAYVENGIAQVQAGAGVVFDSDPQAEADETRGKAQAVISAIQAAHSQPANKE

Gene
trpE
Protein
Anthranilate synthase component 1
Organism
Arthrobacter globiformis
Length
531 amino acids
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).
Similarity
Belongs to the anthranilate synthase component I family.
Mass
57.369 kDa
Sequence
MQDLGIISPGLEEFRELAAHSRVIPVRLKVLADAETPIGLYRKLAQGQPGTFLMESAAVGGAWSRYSFIGSRSRATLTTKDGQAHWLGEPPAGVPVDGNPVDAIRDTIEALRTDRFDGLPPFTSGLVGFLGWETVRHWEKLTRPPEDDLQLPELALNLVTDMAVHDNMDGTVLLIANAINFDNSSERVDEAWHDAVARVKELLARISTPVLQPVSVLEPAALDFAASVQERWNEPEYLAALDRGKEAIVDGEVFQVVISRRFEMECGASPLDVYRVLRNTNPSPYMYIFSLEDAAGRQYSIVGSSPEALVTVTGEDVITHPIAGSRPRGKTVDADKALAEELLADQKERAEHLMLVDLSRNDLSKVCVAGSVDVTQFMEVERFSHIMHLVSTVVGRLAPTAKAYDVLKATFPAGTLSGAPKPRALRLLDELEPHRRGIYGGVVGYLDFAGDMDMAIAIRSALLREGRAYVQAGGGIVADSSNPAEAQETVNKAAAPLRAVHTAGSLHNITPDSVSAPDSVSSPDSVTEANS

Gene
trpE
Protein
Anthranilate synthase component 1
Organism
Buchnera aphidicola subsp. Schlechtendalia chinensis
Length
530 amino acids
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).
Similarity
Belongs to the anthranilate synthase component I family.
Mass
60.189 kDa
Sequence
MCEHLKSMDVLKVETFYQPNPTAIFHHICRNRSNTLLLESAEINNKKNLESMMIVDSALRISALNMVVTLEALTKNGESLLPVFKSLLPKEVRILSNDNFLKIKFPSIVKDIDEDKKLHVLSIFDSIRFLINSVKNNKGSKSMFFGGLFAYDLVSSFENLPKLKTSQSCPDFCFYLSEILLVLNHKRRTCYIQASLFSSSNLERNKLQHRLLEVKNKLSQNFYPLESTSLKKMILKCNRTDREYEKIIKEMKKSIMIGEIFQVVPSRKFYLPCTNSLAAYDVLKKNNPSPYMFFMQDSNFTLFGASPESSLKYDTLSRKIEIYPIAGTRPRARKIDGSIDLDLDSRIELEMRTNHKELSEHLMLVDLARNDLAKICDPGTRYVADLTQVDKYSHVMHLVSRVVGKLRLDLDVFHAYQACMNMGTLSGAPKIRAMELISNAEKEKRGSYGGSIGYFTASGTLDMCIIIRSAYVENNIATIQVGAGIVLDSIPQLEVDESKNKAKAVLQAISESHSCHIELNIENERHTFAG

Gene
trpE
Protein
Anthranilate synthase component 1
Organism
Mycobacterium leprae (strain TN)
Length
529 amino acids
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).
Similarity
Belongs to the anthranilate synthase component I family.
Mass
57.031 kDa
Sequence
MHAHLAATTSREDFRQLAVDHRVVPVTRKVLADSETPLSAYRKLAANRPSTFLLESAENGRSWSQWSFIGVGAPSALTIRDGEAVWLGTVPQDAPTGGDPLHVLQATLELLATAAMPGLPPLSSGMVGFFAYDMVRRLERLPELALNDLQLPDMLLLLATDVAAVDHHEGTITLIANAVNWNGTDERVDQAYDDAIARLDVMTAALGQPLPSTIATFSRPDPRRRAQCTIEEYGAIVDHLVDQIAAGEAFQVVPSQRFEVDTDVDPIDVYRMLRVTNPSPYMYLLHVPNSDGATGFSIVGSSPEALVTVKDGRVTTHPIAGTRWRGQTEEEDQLLEKELLADEKERAEHLMLVDLGRNDLGRVCTPGTVRVEDYSHVERYSHVMHMVSTVTGLLGEGRTALDAVTACFPAGTLSGAPKVRSMELIEEVEKTRRGLYGGVVGYLDFAGNADFAIAIRTALMRDGIAYVQAGGGVVADSNGPYEYIEASNKARAVLNAIAAAETLTSLDFGVALAPGRVAARGEAGNQGRL

Gene
trpE
Protein
Anthranilate synthase component 1
Organism
Buchnera aphidicola subsp. Tetraneura caerulescens
Length
526 amino acids
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).
Similarity
Belongs to the anthranilate synthase component I family.
Mass
60.469 kDa
Sequence
MYYRSIKSEIIQTICTYHEEPSLIFNKICRTKTETLLLESATVHGKKNIESMLIIDTAIKISCFKNIVEIEAISNNGLFLLNTIDLKILKKKSTKIKKKKSNVLEIHFPIFNYFTDEDKKLFLTSVFDALRIIKKSIKNPEKSKMGVFFGGILSYDLISSFEPIPRVFNSKYNHPDFCFYLSENLLIFDHKKKKCKLQTNIFTDNEEEKLNILKRIKIIYNQIKEINSKKKNNRINTFNDFKTKNKKWVDCKNDSKVYKNKVKKMKQMILNGEVFQIVISRKFFLPCPYPLESYIFLKKNNPSPYMFFMQDRHFVLFGASPESSLKFSSITRKIEIHPIAGTRPRAFSSIKKIDINEDNKMELAMRINSKELAEHCMLVDLARNDLSRICLPGSRVVSDLMKVVKYSHVMHLVSKVEGVLRNDLDIFHAYQCCMNMGTLTGAPKIRAMQIIAEEGEIRECYGGAIGYFTGKGDLDTCIVIRSAYVRNGIACVQAGAGIVLDSIADEENEECKNKAMAVINAINKTL

Gene
trpE
Protein
Anthranilate synthase component 1
Organism
Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)
Length
524 amino acids
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).
Similarity
Belongs to the anthranilate synthase component I family.
Mass
55.915 kDa
Sequence
MTAPDTDREEFVSLAGDADGPVVTHLVADLDVSVDPLAAYTTLADRSDYGFLLESAEKVSSSNPQGAFSAPATAADSHARFSFVGYDPEAVVTVGPDGVDVTDLGGPAAEFVGAGDGDVLDSLRGALPDLPRVNFPETDRQTLTGGLVGFLAYEAVYDLWLDEVGRERPDTDDPDAEFVLTTRTLSFDHREDAVRLVCTPVVSPDDDPGEVYDGVVAEAERVAEKLRAADDPAPGGFERTGEDAGSREEYEAAVRKTKEHVRDGDIYQGVISRTRKLRGQVDPVGLYASLREVNPSPYMFLLRHGDRRVVGASPETLVSVRGDRVVVNPIAGTCQRGSGPVEDRRLAGELLADAKERAEHTMLVDLGRNDVRRVSTPGSVRVEDFMSIIKYSHVQHIESTVSGTLDADADAFDATRATFPAGTLTGAPKVRAMEIIDDLEAEPRGVYGGGVGYYSWTGDADVAIVIRTATVDSGGADDAITVRAGAGIVADSDPTAEYEETEQKMGGVLDAVRRIEYGTEEASQ

Gene
trpE
Protein
Anthranilate synthase component 1
Organism
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Length
524 amino acids
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).
Similarity
Belongs to the anthranilate synthase component I family.
Mass
56.311 kDa
Sequence
MQTTANHSSRSTQTGTRAHGAALAETTSREDFRALATEHRVVPVIRKVLADSETPLSAYRKLAANRPGTFLLESAENGRSWSRWSFIGAGAPSALTVRDNAAAWLGTAPEGAPSGGDPLDALRATLDLLKTEAMAGLPPLSSGLVGFFAYDMVRRLERLPELAVDDLGLPDMLLLLATDIAAVDHHEGTITLIANAVNWNGTDERVDWAYDDAVARLDVMTKALGQPLTSAVATFSRPAPDHRAQRTMEEYTEIVDKLVGDIEAGEAFQVVPSQRFEMDTAADPLDVYRILRVTNPSPYMYLLNIPDADGGLDFSIVGSSPEALVTVKDGRATTHPIAGTRWRGATEEEDVLLEKELLADEKERAEHLMLVDLGRNDLGRVCRPGTVRVDDYSHIERYSHVMHLVSTVTGELAEDKTALDAVTACFPAGTLSGAPKVRAMELIEEVEKTRRGLYGGVVGYLDFAGNADFAIAIRTALMRNGTAYVQAGGGVVADSNGPYEYTEAANKARAVLNAIAAAATLAEP

Gene
trpE
Protein
Anthranilate synthase component 1
Organism
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Length
523 amino acids
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).
Similarity
Belongs to the anthranilate synthase component I family.
Mass
58.118 kDa
Sequence
MNKAINIKKTAPLEVLHSELPYTQDPTALFHALCAGRSDCLLLESAEIDSKQNLKSLLLVDAAVRIVCEGHQVTYHALSANGQALLNIIHSNLTDRIPCKVEKAKLTLTFSTPCDTLDEDSRLREASSFDALRLVQHSFDLTDHGKFALFLGGLFAYDLVANFEPLGEAPADNQCPDYVFYVAETLMVIDHQRETCQLQATQFQPGDALHSQLKSRMREIRAQVNQKLPLPSAQSLSDVEVTTNISDAAFCDIVRDLKQYVVKGDVFQVVPSRRFRLPCPSPLAAYQRLKQSNPSPYMFYMQDERFTLFGASPESALKYEMHTNQVEIYPIAGTRRRGKRADGSIDFDLDSRIELELRTDKKENAEHMMLVDLARNDVARISQAGTRHVADLLQVDRYSHVMHLVSRVVGQLREDLDALHAYQACMNMGTLTGAPKIRAMQLIRDVEQARRGSYGGAVGYLTGEGDLDTCIVIRSAYVENGIAQVQAGAGVVYDSDPQAEADETRGKAQAVISAILYAHQGKE

Gene
trpE
Protein
Anthranilate synthase component 1
Organism
Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp)
Length
522 amino acids
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).
Similarity
Belongs to the anthranilate synthase component I family.
Mass
59.507 kDa
Sequence
MKKNLISIDVFLTETRYQPNPTAIFNQICKKKSETLLLESAEINKKHHLESMMIIDAALKISFLNQIVIVEALTKNGVNLLSVFKSLLPKNVIILSDNNPLEIKFPILSMYLDEDQRLRSLSVFDAIRFLIKSVKNLSEFAPKSMFFGGLFSYDLITSFENLPILNTHQHCPDFCFYLSETLLILDHKNKTSIVQVTSFTNDNFEKKRLKDRLEILKNKLSKNLCPIKFDTLKNMKLWCNKTDEEYNKIIVNVKKFILQGEIFQVVPSRKFYLSCVNPLSSYEVLKKNNPSPYMFFMQDRKFTLFGASPESALKYDINSRQIEIYPIAGTRPRGRRSDGSLDLDLDNRIELEMRTNNKELAEHLMLVDLARNDLAKICEPGTRHVADLIRVDRYSHVMHLVSRVIGKLRFDLDFLHAYQACMNMGTLTGAPKVRAMELISEIEGEKRGSYGGAIGYFTGLGMLDTCIVIRSAYVENKIATIQAGAGIVLDSVPQLESDESKNKAKAVIQAIANSHSCQIEYL

Gene
trpE
Protein
Anthranilate synthase component 1
Organism
Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS)
Length
521 amino acids
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).
Similarity
Belongs to the anthranilate synthase component I family.
Mass
58.793 kDa
Sequence
MFLIEKRRKLIQKKANYHSDPTTVFNHLCGSRPATLLLETAEVNKKNNLESIMIVDSAIRVSAVKNSVKITALSENGAEILSILKENPHKKIKFFEKNKSINLIFPSLDNNLDEDKKIFSLSVFDSFRFIMKSVNNTKRTSKAMFFGGLFSYDLISNFESLPNVKKKQKCPDFCFYLAETLLVVDHQKKTCLIQSSLFGRNVDEKNRIKKRTEEIEKKLEEKLTSIPKNKTTVPVQLTSNISDFQYSSTIKKLQKLIQKGEIFQVVPSRKFFLPCDNSLSAYQELKKSNPSPYMFFMQDEDFILFGASPESSLKYDEKNRQIELYPIAGTRPRGRKKDGTLDLDLDSRIELEMRTNHKELAEHLMLVDLARNDLARICEPGSRYVSDLVKVDKYSHVMHLVSKVVGQLKYGLDALHAYSSCMNMGTLTGAPKVRAMQLIAEYEGEGRGSYGGAIGYFTDLGNLDTCITIRSAYVESGVATIQAGAGVVFNSIPEDEVKESLNKAQAVINAIKKAHFTMGSS

Gene
trpE
Protein
Anthranilate synthase component 1
Organism
Buchnera aphidicola subsp. Pemphigus spyrothecae
Length
520 amino acids
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).
Similarity
Belongs to the anthranilate synthase component I family.
Mass
59.502 kDa
Sequence
MKNRRYEVEILQIEGIYQSDPTTIFNQLCNKKKCTLLLESAEIDKKHALESMIIIDSALRISSLDNIVTIEALTENGKSLLFKLDLLLPLTVKNVLFENSRRLIFPFINHEIDEDKKLRSVSIFDTFRLLIKTMKIPKNLTKSMFFGGLFSYDLVNNFEKLPILNRNQKCPDLCFYLAETLLILDHKKKNCIIQSSLFNRKSSEKNRLKKNLQEIKTKLTQNVPKIEHRKIDQISLKCNLTDKEYIKIIKKMKQSIKKGDIFQVVPSRKFYLPCISSLSAYQRLKQSNPSPYMFFMQDSDFTLFGASPESSLKYDSKSKKIEIYPIAGTRPRGKTENGLIDLDLDSKIELEMRMNEKELSEHLMLVDLARNDLARICEPGSRYVASLTKVDRYSCVMHLVSKIVGRLKSNLDIFHAYCACMNMGTLTGAPKIKAMELISKFEKERRGSYGGSIGYFTESNNFDTCIIIRSAYVENNLATVQAGAGIVLDSVPQEEANESRNKAQAVIQAIIYAHSSREVV

Gene
trpE
Protein
Anthranilate synthase component 1
Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Length
520 amino acids
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.
Similarity
Belongs to the anthranilate synthase component I family.
Mass
57.088 kDa
Sequence
MQTPKPTLELLTCDAAYRENPTALFHQVCGDRPATLLLESADIDSKDDLKSLLLVDSALRITALGDTVTIQALSDNGASLLPLLDTALPAGVENDVLPAGRVLRFPPVSPLLDEDARLCSLSVFDAFRLLQGVVNIPTQEREAMFFGGLFAYDLVAGFEALPHLEAGNNCPDYCFYLAETLMVIDHQKKSTRIQASLFTASDREKQRLNARLAYLSQQLTQPAPPLPVTPVPDMRCECNQSDDAFGAVVRQLQKAIRAGEIFQVVPSRRFSLPCPSPLAAYYVLKKSNPSPYMFFMQDNDFTLFGASPESSLKYDAASRQIEIYPIAGTRPRGRRADGTLDRDLDSRIELDMRTDHKELSEHLMLVDLARNDLARICTPGSRYVADLTKVDRYSYVMHLVSRVVGELRHDLDALHAYRACMNMGTLSGAPKVRAMQLIADAEGQRRGSYGGAVGYFTAHGDLDTCIVIRSALVENGIATVQAGAGIVLDSVPQSEADETRNKARAVLRAIATAHHAQETF

Gene
trpE
Protein
Anthranilate synthase component 1
Organism
Escherichia coli (strain K12)
Length
520 amino acids
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.
Similarity
Belongs to the anthranilate synthase component I family.
Mass
57.494 kDa
Sequence
MQTQKPTLELLTCEGAYRDNPTALFHQLCGDRPATLLLESADIDSKDDLKSLLLVDSALRITALGDTVTIQALSGNGEALLALLDNALPAGVESEQSPNCRVLRFPPVSPLLDEDARLCSLSVFDAFRLLQNLLNVPKEEREAMFFGGLFSYDLVAGFEDLPQLSAENNCPDFCFYLAETLMVIDHQKKSTRIQASLFAPNEEEKQRLTARLNELRQQLTEAAPPLPVVSVPHMRCECNQSDEEFGGVVRLLQKAIRAGEIFQVVPSRRFSLPCPSPLAAYYVLKKSNPSPYMFFMQDNDFTLFGASPESSLKYDATSRQIEIYPIAGTRPRGRRADGSLDRDLDSRIELEMRTDHKELSEHLMLVDLARNDLARICTPGSRYVADLTKVDRYSYVMHLVSRVVGELRHDLDALHAYRACMNMGTLSGAPKVRAMQLIAEAEGRRRGSYGGAVGYFTAHGDLDTCIVIRSALVENGIATVQAGAGVVLDSVPQSEADETRNKARAVLRAIATAHHAQETF

Gene
trpE
Protein
Anthranilate synthase component 1
Organism
Buchnera aphidicola subsp. Diuraphis noxia
Length
519 amino acids
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).
Similarity
Belongs to the anthranilate synthase component I family.
Mass
59.521 kDa
Sequence
MEKKPYEIKIIQKKAKYHPDPTIVFNHICGSQKQTLLLETAEINKKNDLESIMIIDAALRISSERNHSVQLTALSKNGENILSILKSNLKQKVQMFIQDTSIRLEFPHFQKNLDEDKKIFSLSIFDTFRFIMKFFKNRNKVQKAMFFGGLFSYDLISNFELLPKLKKTQKCPHFCFYLAETLLIVDHQKKTCLIQNSLFTKNSHEQMRVEKRGREIQKKLEASLNSIPVRQEVKNSMLTANMSDEQYCSIIKKLQILIRKGEIFQVVPSRKFFLPCSNPLSAYQKLKKSNPSPYMFFMQDKDFTLFGASPESSLKYDDTTRQVELYPIAGTRPRGRNMDGTLNLDLDSRIELEMRTNHKELAEHLMLVDLARNDLARICEPGSRYVSDLVRVDKYPHVMHLVSRVVGTLKPELDALHAYAACMNMGTLTGAPKIRAMELIAEYEMEQRGSYGGAIGYFTDLGNLDTCITIRSAYVEDNIATIQSGSGIVYNSIPEDEVKEGINKAKRVINAIQHAHHLV

Gene
trpE
Protein
Anthranilate synthase component 1
Organism
Serratia marcescens
Length
519 amino acids
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 (Probable).
Similarity
Belongs to the anthranilate synthase component I family.
Mass
57.658 kDa
Sequence
MNTKPQLTLLKVQASYRGDPTTLFHQLCGARPATLLLESAEINDKQNLQSLLVIDSALPITALGHTVSVQALTANGPALLPVLDEALPPEVRNQARPNGRELTFPAIDAVQDEDARLRSLSVFDALRTLLTLVDSPADEREAVMLGGLFAYDLVAGFENLPAVRQDQRCPDFCFYLAETLLVLDHQRGSARLQASVFSEQASEAQRLQHRLEQLQAELQQPPQPIPHQKLENMQLSCNQSDEEYGAVVSELQEAIRQGEIFQVVPSRRFSLPCPAPLGPYQTLKDNNPSPYMFFMQDDDFTLFGASPESALKYDAGNRQIEIYPIAGTRPRGRRADGSLDLDLDSRIELEMRTDHKELAEHLMLVDLARNDLARICQAGSRYVADLTKVDRYSFVMHLVSRVVGTLRADLDVLHAYQACMNMGTLSGAPKVRAMQLIAALRSTRRGSYGGRVGYFTAHRHLDTCIVIRSAYVEDGHRTVQAGAGVVQDSIRRREADETRNKARAVLRAIATAHHAKEVF

Gene
trpE
Protein
Anthranilate synthase component 1
Organism
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Length
518 amino acids
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).
Similarity
Belongs to the anthranilate synthase component I family.
Mass
56.384 kDa
Sequence
MSTNPHVFSLDVRYHEDASALFAHLGGTTADDAALLESADITTKNGISSLAVLKSSVRITCTGNTVVTQPLTDSGRAVVARLTQQLGQYNTAENTFSFPASDAVDERERLTAPSTIEVLRKLQFESGYSDASLPLLMGGFAFDFLETFETLPAVEESVNTYPDYQFVLAEIVLDINHQDQTAKLAGVSNAPGELEAELNKLSLLIDAALPATEHAYQTTPHDGDTLRVVADIPDAQFRTQINELKENIYNGDIYQVVPARTFTAPCPDAFAAYLQLRATNPSPYMFYIRGLNEGRSYELFGASPESNLKFTAANRELQLYPIAGTRPRGLNPDGSINDELDIRNELDMRTDAKEIAEHTMLVDLARNDLARVSVPASRRVADLLQVDRYSRVMHLVSRVTATLDPELDALDAYRACMNMGTLTGAPKLRAMELLRGVEKRRRGSYGGAVGYLRGNGDMDNCIVIRSAFVQDGVAAVQAGAGVVRDSNPQSEADETLHKAYAVLNAIALAAGSTLEVIR

Gene
trpE
Protein
Anthranilate synthase component 1
Organism
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Length
518 amino acids
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).
Similarity
Belongs to the anthranilate synthase component I family.
Mass
57.522 kDa
Sequence
MNIQTQAFIAVTAQPIPYYADTTAIFNTLCQSNSNSLLLDSAEIGSKNSLQSLILVNAAVKITCLGHNVTFKALNNNGKQVLKEIHPKLTALGKVSAVNFEDEFSVQFLPLDNQLDEDSKLQSATIFDGLRVISSLYQHSQTPIFLGGLFAYDLVANFIPMDGITLKNDGINCPDYSFYLAEHLITIDHQNQQATLKSFCFAQEEQVNIAKTSLSIAQKLKNIDHVLSIKAASDEVKTNFDDPEFTGIVKALKHHINIGDVFQIVPSRRFSLACPNTLASYAQLKQNNPSPYMFYMNDEDFILFGASPESALKYAPENRQLEIYPIAGSRPRGFDAHGNIDPELDARLELELRLDHKEQAEHLMLVDLARNDIARVCQSGTRKVAELMQVDRYSHIMHLVSRVVGKLRPELDALHAYQACMNMGTLTGAPKIKAMQLIYQFEQQKRHSYGGAVGYLTSDGHFDTCIVIRSAFVQNGMAHVQAGCGEVLDSDPQMEADETRHKAAAVLKAIRQVNTQAK

Gene
trpE
Protein
Anthranilate synthase component 1
Organism
Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)
Length
516 amino acids
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).
Similarity
Belongs to the anthranilate synthase component I family.
Mass
55.849 kDa
Sequence
MHADLAATTSREDFRLLAAEHRVVPVTRKVLADSETPLSAYRKLAANRPGTFLLESAENGRSWSRWSFIGAGAPTALTVREGQAVWLGAVPKDAPTGGDPLRALQVTLELLATADRQSEPGLPPLSGGMVGFFAYDMVRRLERLPERAVDDLCLPDMLLLLATDVAAVDHHEGTITLIANAVNWNGTDERVDWAYDDAVARLDVMTAALGQPLPSTVATFSRPEPRHRAQRTVEEYGAIVEYLVDQIAAGEAFQVVPSQRFEMDTDVDPIDVYRILRVTNPSPYMYLLQVPNSDGAVDFSIVGSSPEALVTVHEGWATTHPIAGTRWRGRTDDEDVLLEKELLADDKERAEHLMLVDLGRNDLGRVCTPGTVRVEDYSHIERYSHVMHLVSTVTGKLGEGRTALDAVTACFPAGTLSGAPKVRAMELIEEVEKTRRGLYGGVVGYLDFAGNADFAIAIRTALMRNGTAYVQAGGGVVADSNGSYEYNEARNKARAVLNAIAAAETLAAPGANRSGC

Gene
trpE
Protein
Anthranilate synthase component 1
Organism
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Length
516 amino acids
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).
Similarity
Belongs to the anthranilate synthase component I family.
Mass
55.849 kDa
Sequence
MHADLAATTSREDFRLLAAEHRVVPVTRKVLADSETPLSAYRKLAANRPGTFLLESAENGRSWSRWSFIGAGAPTALTVREGQAVWLGAVPKDAPTGGDPLRALQVTLELLATADRQSEPGLPPLSGGMVGFFAYDMVRRLERLPERAVDDLCLPDMLLLLATDVAAVDHHEGTITLIANAVNWNGTDERVDWAYDDAVARLDVMTAALGQPLPSTVATFSRPEPRHRAQRTVEEYGAIVEYLVDQIAAGEAFQVVPSQRFEMDTDVDPIDVYRILRVTNPSPYMYLLQVPNSDGAVDFSIVGSSPEALVTVHEGWATTHPIAGTRWRGRTDDEDVLLEKELLADDKERAEHLMLVDLGRNDLGRVCTPGTVRVEDYSHIERYSHVMHLVSTVTGKLGEGRTALDAVTACFPAGTLSGAPKVRAMELIEEVEKTRRGLYGGVVGYLDFAGNADFAIAIRTALMRNGTAYVQAGGGVVADSNGSYEYNEARNKARAVLNAIAAAETLAAPGANRSGC

Gene
trpE
Protein
Anthranilate synthase component 1
Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Length
516 amino acids
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).
Similarity
Belongs to the anthranilate synthase component I family.
Mass
55.849 kDa
Sequence
MHADLAATTSREDFRLLAAEHRVVPVTRKVLADSETPLSAYRKLAANRPGTFLLESAENGRSWSRWSFIGAGAPTALTVREGQAVWLGAVPKDAPTGGDPLRALQVTLELLATADRQSEPGLPPLSGGMVGFFAYDMVRRLERLPERAVDDLCLPDMLLLLATDVAAVDHHEGTITLIANAVNWNGTDERVDWAYDDAVARLDVMTAALGQPLPSTVATFSRPEPRHRAQRTVEEYGAIVEYLVDQIAAGEAFQVVPSQRFEMDTDVDPIDVYRILRVTNPSPYMYLLQVPNSDGAVDFSIVGSSPEALVTVHEGWATTHPIAGTRWRGRTDDEDVLLEKELLADDKERAEHLMLVDLGRNDLGRVCTPGTVRVEDYSHIERYSHVMHLVSTVTGKLGEGRTALDAVTACFPAGTLSGAPKVRAMELIEEVEKTRRGLYGGVVGYLDFAGNADFAIAIRTALMRNGTAYVQAGGGVVADSNGSYEYNEARNKARAVLNAIAAAETLAAPGANRSGC

Gene
trpE
Protein
Anthranilate synthase component 1
Organism
Bacillus subtilis (strain 168)
Length
515 amino acids
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).
Similarity
Belongs to the anthranilate synthase component I family.
Mass
58.116 kDa
Sequence
MNFQSNISAFLEDSLSHHTIPIVETFTVDTLTPIQMIEKLDREITYLLESKDDTSTWSRYSFIGLNPFLTIKEEQGRFSAADQDSKSLYTGNELKEVLNWMNTTYKIKTPELGIPFVGGAVGYLSYDMIPLIEPSVPSHTKETDMEKCMLFVCRTLIAYDHETKNVHFIQYARLTGEETKNEKMDVFHQNHLELQNLIEKMMDQKNIKELFLSADSYKTPSFETVSSNYEKSAFMADVEKIKSYIKAGDIFQGVLSQKFEVPIKADAFELYRVLRIVNPSPYMYYMKLLDREIVGSSPERLIHVQDGHLEIHPIAGTRKRGADKAEDERLKVELMKDEKEKAEHYMLVDLARNDIGRVAEYGSVSVPEFTKIVSFSHVMHIISVVTGRLKKGVHPVDALMSAFPAGTLTGAPKIRAMQLLQELEPTPRETYGGCIAYIGFDGNIDSCITIRTMSVKNGVASIQAGAGIVADSVPEAEYEESCNKAGALLKTIHIAEDMFHSKEDKADEQISTIVR

Gene
trpE
Protein
Anthranilate synthase component 1
Organism
Buchnera aphidicola subsp. Schizaphis graminum (strain Sg)
Length
515 amino acids
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).
Similarity
Belongs to the anthranilate synthase component I family.
Mass
58.687 kDa
Sequence
MSKNPYEIEIIQKTAPYHPDPTMIFNHLCASRPGTLLLETAEVNKKRDLESIMIIDSAMRISSEDNSVKLTPLSINGTDILSTLKKTIPKKIEIYEKNNSTILVFPKIKKNIDEDKKLFSLSVFDAFRLMIRIFENREKKSKAMFFGGLFSYDLISVFESLPKLKGNQKCSNFCFYLAETLLVLDHQKKTCLIQNSLFSKNLKERKRIKKRSVEIERKLNEKLKLIPKTKIKDINLTSNMNNFEYGTIIKKLQKLIQKGEIFQVVPSRKFYLPCPNPLSAYQKLKKSNPSPYMFFMQDQDFTLFGASPESSLKYDEKTRKIELYPIAGTRPRGKTEDGNLDLDLDSRIELEMRTNHKELAEHLMLVDLARNDLARICKPGSRYVSDLVRVDRYSHVMHLVSRVIGELREGLDALHAYASCMNMGTLTGAPKVRAMQLIAEHEGEKRGSYGGAIGYFTDLGNLDTCITIRSAYVEKQVATIQAGAGIVYNSIPENEVNESLNKAQAVINAIKNAHY

Gene
trpE
Protein
Anthranilate synthase component 1
Organism
Buchnera aphidicola subsp. Rhopalosiphum maidis
Length
514 amino acids
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).
Similarity
Belongs to the anthranilate synthase component I family.
Mass
58.772 kDa
Sequence
MKKKPYQIEIIQKKAPYHPDPTMIFNHLCESRSATLLLETAEVNKKKDLESIMIIDSAIRISSKKNLVKLKPLSINGEEILLALKKRIPKKIEIYEKNKNIILVFPKIEKNLDEDKKLFSLSVFDAFRFMIKIFENKEKKSKAMFFGGLFSYDLSQFFESLPKLKGNQKCSNFCFYLAETLLVLDHQKKTCLIQNSLFTKNANEKKRIKERSIEIEKKLNEKLKSIPKVKITDINLTSNMNNFEYGSIIKKLQKLIQKGEIFQVVPSRKFYLPCPNPLSAYQKLKKSNPSPYMFFMQDKDFTLFGASPESSLKYDEKTRKIELYPIAGTRPRGRTEDGNLDLDLDSRIELEMRTNHKELAEHLMLVDLARNDLARICKPGSRYVSDLVKVDKYSHVMHLVSKVIGELKEGLDALHAYASCMNMGTLTGAPKVRAMQLIAEYEKEKRGSYGGAIGYFTDLGNLDTCITIRSAYVENIATIQAGAGIVYNSIPEDEVNESLNKAQAVINAIKNAHY

Gene
trpE
Protein
Anthranilate synthase component 1
Organism
Buchnera aphidicola subsp. Rhopalosiphum padi
Length
514 amino acids
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).
Similarity
Belongs to the anthranilate synthase component I family.
Mass
58.985 kDa
Sequence
MKKSAYPIEIIQKQAPYHPDPTMIFNHLCESRSETLLLETADNKKKRSRKIMIIDSAMRISSEHNAVKLTPLSINGMEILLVLKKIISKKIEIYRRKKNTILIFPNIEKDLDEDKKLFSLSVFDAFRLIIKTFENREKKSKAMFFGGLFSYDLISVFETLPKLKGNQKCSNFCFYLAETLLVLDHQQKTCLIQSSLFTKNSNEKKRIEERSVEIKQKLNQKLNSIPKIKIKDINLTSNMNNFEYGSIIKKLQKLIQKGEIFQVVPSRKFYLPCPNPLSAYQKLKKSNPSPYMFFMQDQDFTLFGASPESSLKYDEKTRKIELYPIAGTRPRGRTKDGNLDLDLDSRIELEMRTNHKELAEHLMLVDLARNDLARICKPGSRYVSDLVRVDRYSHVMHLVSRVIGELREGLDALHAYASCMNMGTLTGAPKVCAMQLIAEYEKEKRGSYGGAIGYFTDLGNLDTCITIRSAYVEKRYCYNQAGAGIVYNSIPEDEVNESLNKAQAVINAIKNAHY

Gene
trpE
Protein
Anthranilate synthase component 1
Organism
Bacillus pumilus
Length
513 amino acids
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).
Similarity
Belongs to the anthranilate synthase component I family.
Mass
58.091 kDa
Sequence
MNSQSNLTQFLKDSESYKTIPIVETITVDTLSPIQIVEKLKQDIVYLLESKDESSSWSRYSFIGLHPFLTLHDDQNKYIARDAAGQKLMQKQELKELLDWMKEQYQIKTPDIDIPFTGGAVGYLSYDLIPTLTSVRPHRSASTIENAHICLPTMIAFDHETNHVHFIQYTQLTGHETEDEKIRAYKEKQKQLEQMIHKLHSKVDMKELILSGNMNEPPSFEHVTSTYEKAQFLKDVEKIKEYIRAGDIFQGVLSQRFDIPVSVSSFELYRVLRIVNPSPYMYFMKLKDRDLVGSSPERLIHAKNGHLEIHPIAGTRKRGTTREEDAELARELLEDEKEKAEHYMLVDLARNDVGRVAEYGSVSVPTFTKVVNFSHVMHIISIVTGKLKRDTHPVDALMSAFPAGTLTGAPKIRAMQLLNEMEPEPRETYGGCIAYIGFDGNIDSCITIRTMSVKNHTASIQAGAGIVADSVPENEWEETCNKAGALLKAIQLAEHIFSEKESVQDESPTISSC

Gene
trpE
Protein
Anthranilate synthase component 1
Organism
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Length
511 amino acids
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).
Similarity
Belongs to the anthranilate synthase component I family.
Mass
54.829 kDa
Sequence
MTTHAAEAPTTDPQGAPGSQKTPDATEAEEAARATVPHRAAAAALAREHDVVPLHQEFLDDSVSPVTAFAQLCGPDEAGFLLESVPVSGGVARYSYVGHRPVPLEPTGGDPLTALRSHLARSVAPVPGLPPFHGGVVGYLGYEAARHFEDLPLAAGPPPGLPESAFLAADDLVVFDHATRRVLLMTLYRPARESYDDAVARIVRLNRALRRAPAPAAFSGRPLAAATPADHGTQGWTANLTEAQFTERVARAREHIAAGDAFQIVLSRRLSRPLRARPTDLYRHLRATNPSPYMYHLSLGGGRHVIGASPELLVKAEGRTVRTRPLAGTRPRHPDPAEDLRLERELRADEKERAEHVMLVDLGRNDLGRVTEPGTVRVERLMRVERFSHVMHLSSTVRGRLAEGRDALDALRSAFPAGTLSGAPKIRAMEIIAELEPEQRGVYGGALGFVGADGLTDFAIALRTMVVADGHVHVQAGAGIVADSDPAAEFRETLHKSRAMLTAVRRAEAAA

Gene
trpE
Protein
Anthranilate synthase component 1
Organism
Bacillus caldotenax
Length
508 amino acids
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).
Similarity
Belongs to the anthranilate synthase component I family.
Mass
56.493 kDa
Sequence
MSADGLAAFLAEANEFRTIPIVRKFVADVIEPLGVFANLREEAVFLLESKDDESPWARYSFIGVAPFLTLESETGETFSVKDENGNEQITAPTLKEAFQWVERTLAVKPLAETVPFTGGAVGFLGYDFISAIEKVPRHKNRDVPMKTAYFVFCESLFAFDQKKRELLVIHYIRLSGNETEEEKIEAYRAAERRMADLAAKAARPQAEQPLLPAESESGRTASFAKAVSNYDKKQFLRDVEAVKRYIAAGDVFQAVLSQRFCVPVQAGGFAIYRLLRYINPSPYMFYFQLDGVEIVGSSPEKLIQVHRRRVEIDPIAGTRRRGRSPEEDERLADELYHDPKERAEHYMLVDLARNDIGRVAKYGTVEVPVLLQIGKFSHVMHLISKVVGELDDNVHPIDALLAAFPAGTVSGAPKVRAMQILQELEPTARGLYAGAIAYIGFDGNIDSCIAIRTAVVKDGYAYVQAGAGIVADSVPELEWKETRNKASALMNAIEQAERLFAKGERAVC

Gene
trpE
Protein
Anthranilate synthase component 1
Organism
Synechocystis sp. (strain PCC 6803 / Kazusa)
Length
508 amino acids
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).
Similarity
Belongs to the anthranilate synthase component I family.
Mass
57.147 kDa
Sequence
MISPGFSHFTELAQQGNFIPVYQEWVADLETPVSAWYKVCSSQPYNFLLESVEGGESIGRYSFLGCDPMWVLEARGDETTQVLRNGQTETFRGNPLDILSQCLESIRPVNLPQLPPGIGGLFGVWGYELIRWMEPRVPVYEPQPEDPPDGIWMQVDHLLIFDQVKRKIWAIAFADLRGENVDLETAYRNACQRVTKLVLQLQLPLPPEATALELLTKTQLEGKELNYSSNTEQEKFLEEVAIAKDYITAGDIFQVVLSQRLSTIYRDDPFKLYRSLRLINPSPYMAYYNFGHWQIIGSSPEVMVKADRQLDGKLMATVRPIAGTRPRGKTHPEDEQLAEELLNDPKEIAEHVMLVDLGRNDLGRVCVQGSVKVNELMVIERYSHVMHIVSNVVGELASDKTAWDLLKACFPAGTVSGAPKIRAMEIINELEPERRGPYSGVYGYYDFEGQLNTAIAIRTMVVQEQPDGAHRVSVQTGAGIVADSDPQKEYEETLNKARGLLEAIRALS

Gene
trpE
Protein
Anthranilate synthase component 1
Organism
Geobacillus stearothermophilus
Length
508 amino acids
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).
Similarity
Belongs to the anthranilate synthase component I family.
Mass
56.441 kDa
Sequence
MSIDRLAAFLADARQFRTIPIMRKFLADVIEPLQVFANLREEAVFLLESKDDESPWARYSFIGVAPFLTLESETGETFLIKDENGNVQMTASTLKEAFQAVERALCVKPLAEAAPFTGGAVGFLGYDFISAIEKVPRHRAPDLAMKAGHFVFCESLFAFDHEKRELSLIHYIRLKGHETMQEKIAIYRAAEERIAALAAKASRPRAEQPLLPAEDEAERAALFSKASSNYEKEQFLRDVEAVKQYIAAGDVFQAVLSQRFSVPVQAGGFAIYRILRHINPSPYMFYFRLDGIEIVGSSPEKLIQVRNRRAEIDPIAGTRRRGRSPAEDEKLADELYHDPKERAEHYMLVDLARNDIGRVAKYGTVEVPVLMEIGKFSHVMHLISKVVGVLDDDIHPIDALLAAFPAGTVSGAPKVRAMQILQELEPTARGLYAGAIAYIGFDGSIDSCIAIRTAVIKDGYAYVQAGAGIVADSVPELEWKETRNKASALIYAIEQAERLFAKGEQIVC

Gene
trpE
Protein
Anthranilate synthase component 1
Organism
Pseudomonas savastanoi
Length
505 amino acids
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).
Similarity
Belongs to the anthranilate synthase component I family.
Mass
56.084 kDa
Sequence
MNREEFLRLAAEGYNRIPLARETLADFDTPLSIYLKLADQPNSYLLESVQGGEKWGRYSIIGLPCRTVMRVHGHHVSVTHDGVEIESLDVEDPLDFVETFKARYNVPTIAGLPRFNGGLVGYFGYDCVRYVEKRLANCPNPDPLGVPDILLMVSDAVVVFDNLAGKMHAIVLVDPAQQDAYARGVAQLDELMHKLRQPITPRRGLDLDRAPRADPVFRSSFTQGDYEAAVDTIKQYILAGDVMQVVPSQRMSIDFKAAPIDLYRALRCFNPTPYMYFFNFGDFHVVGSSPEVLVRVEDNLITVRPIAGTRPRGATEEADLALEEDLLSDHKEIAEHLMLIDLGRNDVGRVSEIGTVKLTEKMVIERYSNVMHIVSNVTGQLKNGLTAMDALRAILPAGTLSGAPKIRAMEIIDELEPVKRGVYGGAVGYMAWNGNMDTAIAIRTAVIKNGELHVQAGGGIVADSVPVLEWEETLNKRRAMVGSAWWPWPRRLPRVEQACCSGNER

Gene
trpE
Protein
Anthranilate synthase component 1
Organism
Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158)
Length
500 amino acids
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).
Similarity
Belongs to the anthranilate synthase component I family.
Mass
54.909 kDa
Sequence
MTSFESFERGWKAGQNQIVYARLTADLDTPVSLMLKLAEARTDTFMLESVTGGEIRGRYSVVGMKPDLIWQCHGQDSRINREARFDRQAFQPLEGHPLETLRALIAESRIEMPADLPPIAAGLFGYLGYDMIRLVEHLPGINPDPLGLPDAVLMRPSVVAVLDGVKGEVTVVAPAWVSSGLSARAAYAQAAERVMDALRDLDRAPPAQRDFGEVAQVGEMRSNFTHEGYKAAVEKAKDYIRAGDIFQVVPSQRWAQDFRLPPFALYRSLRKTNPSPFMFFFNFGGFQVVGASPEILVRLRDREVTVRPIAGTRKRGATPEEDRALEADLLSDKKELAEHLMLLDLGRNDVGRVAKIGTVRPTEKFIIERYSHVMHIVSNVVGEIAEGEDALSALLAGLPAGTVSGAPKVRAMEIIDELEPEKRGVYGGGVGYFAANGEMDFCIALRTAVLKDETLYIQSGGGVVYDSDPEAEYQETVNKARALRRAAEDAGLFARRAGNG

Gene
trpE
Protein
Anthranilate synthase component 1
Organism
Helicobacter pylori (strain J99 / ATCC 700824)
Length
500 amino acids
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).
Similarity
Belongs to the anthranilate synthase component I family.
Mass
56.587 kDa
Sequence
MISLIEKAPYIPYPLALYEKLEQRHTLLFESAEIESKAHTKSLLMAKACLKLVCNHNIVTITSLTPNGGAFLQTLSAFFKTPIQDNALTLTYTKDKKIQDEFLKLFEPSPFDALRGLFKSVKTRPKHPFTLFSAGVFSFEMLNFFEDLPHLKANDNTANDFIFYVAQNLIIIDHKEKSAEILGACFDERFKTEIAKELQDLKELVKNIKSDFIPKKAKQSIEVSVSCDDSEFEKKVLFLQEEIKKGEIFQAVLSRSFYMECLEGLSAYYHLKLSNPSPYMFYIKDSDFILFGASPESALKYNALTNTAEIYPIAGTRLRGKDKQGNIDYDLDSKMEFDLQHDYKERAEHIMLVDLARNDMARVSKKRYCDKLLKVDKYSNVMHLVSRVVGELKKGCDSLHAYRSFMNAGTLSGAPKISAIKLIYQLENQRRGSYGGSVGYLNSEGSMDSCITIRSCFVKNNRAVIQAGAGIVLDSVPQNEANETRAKVQALIDAIRKTIS

Gene
trpE
Protein
Anthranilate synthase component 1
Organism
Helicobacter pylori (strain ATCC 700392 / 26695)
Length
500 amino acids
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).
Similarity
Belongs to the anthranilate synthase component I family.
Mass
56.556 kDa
Sequence
MISLIEKAPYIPYPLALYEKLEQPHTLLFESAEIESKAHTKSLLMAKACLKLICNHNIVTITSLTPNGGAFLQKLSAFFKTPIQDNALILTYTKNKKTQDEFLKLFEPSPFDALRGLFKSVKTKPKHPFTLLSAGVFSFEMLNFFEDLPHLKAKDNTVHDFIFYLAQNLIIIDHKEKSVEILGACFDERFKTEIAQELQDLKELAKSIKSDFVPKKSKQSREVSANCSDSEFEKRVLSLQEEIKKGEIFQAVLSRSFYMECLEGLSAYYHLKLTNPSPYMFYIKDSDFILFGASPESALKYNALTNTAEIYPIAGTRLRGKDKQGNIDYDLDSKMEFDLQHDYKERAEHIMLVDLARNDMARVSKKRYCDKLLKVDKYSNVMHLVSRVVGELKKGCDSLHAYRSFMNAGTLSGAPKISAIRLIYQLENQRRGSYGGSVGYLNSEGSMDSCITIRSCFVKNNRAVIQAGAGIVLDSVPQNEANETRAKAQALIDAIRKTSL

Gene
trpE
Protein
Anthranilate synthase component 1
Organism
Acinetobacter calcoaceticus
Length
497 amino acids
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).
Similarity
Belongs to the anthranilate synthase component I family.
Mass
55.386 kDa
Sequence
MTSLTQFEQLKTAGYNTIPVYRQRLADTDTPLSVFARLKDYTQAYLFESVEGGENWARYSIIGLGESTVFSCNAGQLTIKNAQGNITTQSCADPFQYIRDYQSQFKVPPHALIPDLPQFTGGLVGYFGYDAVRYIEPRLSNVPEADPVGLPDIWMMLSKTVIIFDNLKDTLFLIVHANTTDEEAYQRAQNQLDYLERLLATPVSLQAKKHKAPHFESLTGKEKFLESVETVKEYIRAGDVMQVVPGHRMVSDFDGDPLQVYRALRHLNPSPYLFLVQGHTLTDNTPFHIVGSSPEILSRLEDGIATVRPLAGTRPRGKTKEEDLALEQELLADEKEIAEHLMLIDLGRNDVGRVSKIGKVQVTDRMVIERYSHVMHIVSNVQGEVRDDIDALDVFKATFPAGTLSGAPKIRAMEIIDEVEPVKRGIFGGAVGYLGWHGEMDMSIAIRTCVIRENKVYVQAGAGLVADSNPESEWNETQIKARAVIKAVELSSNGLIL

Gene
trpE
Protein
Anthranilate synthase component 1
Organism
Aquifex aeolicus (strain VF5)
Length
494 amino acids
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).
Similarity
Belongs to the anthranilate synthase component I family.
Mass
57.087 kDa
Sequence
MNLNLSLEEVRKLSENYNVIPLYTELLVDTETPLSIFLKLKEKGQFNILLESAEGGEKWGRYSFIITGSSFYLRTRKDIGEIYERGKVNFFETKDPLSKIKEVVKKFIPYHDERLPRFWGGLVGYFAYDVVKFYEPVEDKNPDPIHTYDIYLVLTDVVVIHDNLTGKIKVVVPIFAQNGIEEEYERAKNLIRDTVKKLKERGTTFLNVVEKEPDFKNWRSNFTKEEFEDIVKKAKEYIAQGDVIQVVLSQRFRKRFKGNPDNIYRVLRFLNPSPYMYYLDFDQLKVIGSSPEILVRLEEGRIETRPIAGTRKRGRTEEEDKRLEEDLLSDEKERAEHLMLVDLARNDIGRVAKTGSVRVENFMRIERYSHVMHIVSDVVGELREGYDALDVLKATFPAGTVSGAPKVRAMQIIEELENERRGIYAGSVGYISFQGNMDMAIAIRTAVYRDRDIFVQAGAGIVADSVPEKEWEETVNKAKALMKAIEIAEESQEE

Gene
trpE
Protein
Anthranilate synthase component 1
Organism
Clostridium thermocellum
Length
494 amino acids
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).
Similarity
Belongs to the anthranilate synthase component I family.
Mass
56.02 kDa
Sequence
MFYPTLDEVKIMAKDYNIIPVTMEVYADMETPISLFKRFEESSCCFLLESVEGGEKWARYSIIGKNPFLVVESYKNKTIIRERNGSQREVEGNPVEIIKGIMGKFKGANLPNLPRFNGGAVGYFGYDLIRHYENLPNVPEDDMGLPECHFMFTDEVLVYDHLKQKIHIIVNLHVNGNIERAYISAVDRIKTIHREILDTRWKTADNSVLSYNKKKNELAVTSNISKEDFCRNVLKAKQYIRDGDIFQVVLSQRLCVETNENPFNIYRALRVINPSPYMYYLKFGGYRIIGSSPEMLVRVENGIVETCPIAGTRKRGRTKEEDEALEKELLSDEKEIAEHVMLVDLGRNDIGRVSKFGTVAVKNLMHIERYSHVMHVVTNVQGEIREDKTPFDALMSILPAGTLSGAPKVRAMEIIDELETVKRGPYGGAIGYLSFNGNLDSCITIRTIILKDGKAYVQAGAGIVADSVPEREYEECYNKAMALLKAIEEAGEIR

Gene
trpE
Protein
Anthranilate synthase component 1
Organism
Pseudomonas putida
Length
493 amino acids
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.
Similarity
Belongs to the anthranilate synthase component I family.
Mass
54.449 kDa
Sequence
MNREEFLRLAAVGYNRIPLACETLADFDTPLSIYLKLADQPNSYLLESVQGGEKWGRYSMIGLPSRTVMRVHGYHVSILHDGVEVESHDVEDPLAFVESFKDRYKVADIPGLPRFNGGLVGYFGYDCVRYVEKRLGVSPNPDPLGVPDILLMVSDAVVVFDNLAGKMHAIVLVDPAEEQAFEQGQARLQGLLETLRQPITPRRGLDLSGPQAAEPEFRSSYTREDYENAVGRIKEYILAGDCMQVVPSQRMSIDFKAAPIDLYRALRCFNPTPYMYFFNFGDFHVVGSSPEVLVRVEDNLVTVRPIAGTRPRGATEEADRALEDDLLSDDKEIAEHLMLIDLGRNDVGRVSSTGSVRLTEKMVIERYSNVMHIVSNVAGQLREGLTAMDALRAILPAGTLSGAPKIRAMEIIDELEPVKRGVYGGAVGYFAWNGNMDTAIAIRTAVINDGELHVQAGGGIVADSVPALEWEETINKRRAMFRAVALAEQTSAK

Gene
trpE
Protein
Anthranilate synthase component 1
Organism
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Length
492 amino acids
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.
Similarity
Belongs to the anthranilate synthase component I family.
Mass
54.555 kDa
Sequence
MNREEFLRLAADGYNRIPLSFETLADFDTPLSIYLKLADAPNSYLLESVQGGEKWGRYSIIGLPCRTVLRVYDHQVRISIDGVETERFDCADPLAFVEEFKARYQVPTVPGLPRFDGGLVGYFGYDCVRYVEKRLATCPNPDPLGNPDILLMVSDAVVVFDNLAGKIHAIVLADPSEENAYERGQARLEELLERLRQPITPRRGLDLEAAQGREPAFRASFTREDYENAVGRIKDYILAGDCMQVVPSQRMSIEFKAAPIDLYRALRCFNPTPYMYFFNFGDFHVVGSSPEVLVRVEDGLVTVRPIAGTRPRGINEEADLALEQDLLSDAKEIAEHLMLIDLGRNDVGRVSDIGAVKVTEKMVIERYSNVMHIVSNVTGQLREGLSAMDALRAILPAGTLSGAPKIRAMEIIDELEPVKRGVYGGAVGYLAWNGNMDTAIAIRTAVIKNGELHVQAGGGIVADSVPALEWEETINKRRAMFRAVALAEQSVE

Gene
trpE
Protein
Anthranilate synthase component 1
Organism
Neisseria meningitidis serogroup C / serotype 2a (strain ATCC 700532 / DSM 15464 / FAM18)
Length
491 amino acids
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).
Similarity
Belongs to the anthranilate synthase component I family.
Mass
54.719 kDa
Sequence
MISKQEYQAQAAQGYNRIPLVQELLADLDTPLSLYLKLANRPYTYLLESVVGGERFGRYSFIGLPCSHYLKASGKHVDVYQNGEIVEQHDGNPLPFIEAFHNRFKTPEIPSLPRFTGGLVGYFGYETIYNFEHFAHRLKNTTKADPLGTPDILLMLSQELAVVDNLSGKIYLIVYADPSQPDGYERARERLEDIRTQLRQSCAIPLSLGSKHTEAVSEFGEEPFKACVNKIKDYIFAGDCMQVVPSQRMSMEFTDSSLALYRALRTLNPSPYLFYYDFGDFHIVGSSPEILVRRERDDVIVRPIAGTRLRGKTPAEDLANEQDLLSDAKEIAEHVMLIDLGRNDVGRISKTGEVKVTDKMVIEKYSHVMHIVSNVEGRLKDGMTNMDILAATFPAGTLSGAPKVRAMEIIEEVEPSKRGIYGGAVGVWGFNNDMDLAIAIRTAVVKNNTLYVQSGAGVVADSDPASEWQETQNKARAVIHAAQMVQEGLDK

Gene
trpE
Protein
Anthranilate synthase component 1
Organism
Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090)
Length
491 amino acids
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).
Similarity
Belongs to the anthranilate synthase component I family.
Mass
54.748 kDa
Sequence
MISKQEYQAQAAQGYNRIPLVQELLADLDTPLSLYLKLANRPYTYLLESVVGGERFGRYSFIGLPCSHYLKAGGKHVDVYQNGEIVEQYDGNPLPFIEAFHNRFKTPEIPSLPRFTGGLVGYFGYETVYNFEHFAHRLKNTAKANPLGTPDILLMLSQELAVIDNLSGKIHLIVYADPSQPDSYERARERLEDIRTQLRQSCAIPLSLGSKQTQAVSEFGEEPFKACVDKIKDYIFAGDCMQVVPSQRMSMEFTDNPLALYRALRTLNPSPYLFYYDFGDFHIVGSSPEILVRRERDDVIVRPIAGTRLRGKTPAEDLANEQDLLSDAKEIAEHVMLIDLGRNDVGRISKTGEVKVTDKMVIEKYSHVMHIVSNVEGCLKEGVTNMDILAATFPAGTLSGAPKVRAMEIIEEIEPEKRGIYGGAVGVWGFNNDMDLAIAIRTAVIKNNTLFIQSGAGVVADSDPTSEWQETQNKARAVVRAAQMVQEGLDK

Gene
trpE
Protein
Anthranilate synthase component 1
Organism
Neisseria gonorrhoeae
Length
491 amino acids
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).
Similarity
Belongs to the anthranilate synthase component I family.
Mass
54.748 kDa
Sequence
MISKQEYQAQAAQGYNRIPLVQELLADLDTPLSLYLKLANRPYTYLLESVVGGERFGRYSFIGLPCSHYLKAGGKHVDVYQNGEIVEQYDGNPLPFIEAFHNRFKTPEIPSLPRFTGGLVGYFGYETVYNFEHFAHRLKNTAKANPLGTPDILLMLSQELAVIDNLSGKIHLIVYADPSQPDSYERARERLEDIRTQLRQSCAIPLSLGSKQTQAVSEFGEEPFKACVDKIKDYIFAGDCMQVVPSQRMSMEFTDNPLALYRALRTLNPSPYLFYYDFGDFHIVGSSPEILVRRERDDVIVRPIAGTRLRGKTPAEDLANEQDLLSDAKEIAEHVMLIDLGRNDVGRISKTGEVKVTDKMVIEKYSHVMHIVSNVEGCLKEGVTNMDILAATFPAGTLSGAPKVRAMEIIEEIEPEKRGIYGGAVGVWGFNNDMDLAIAIRTAVIKNNTLFIQSGAGVVADSDPTSEWQETQNKARAVVRAAQMVQEGLDK

Gene
trpE
Protein
Anthranilate synthase component 1
Organism
Neisseria meningitidis serogroup A / serotype 4A (strain Z2491)
Length
491 amino acids
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).
Similarity
Belongs to the anthranilate synthase component I family.
Mass
54.722 kDa
Sequence
MISKQEYQAQAAQGYNRIPLVQELLADLDTPLSLYLKLANRPYTYLLESVVGGERFGRYSFIGLPCSHYLKASGKHVDVYQNGEIVEQHDGNPLPFIEAFHNRFKTPEIPSLPRFTGGLVGYFGYETIYNFEHFAHRLKNTTKADPLGTPDILLMLSQELAVIDNLSGKIHLVVYADPSQPDGYERARERLEDIRTQLRQSCAIPLSLGSKHTEAVSEFGEEPFKACVNKIKDYIFAGDCMQVVPSQRMSMEFTDSPLALYRALRTLNPSPYLFYYDFGDFHIVGSSPEILVRRERDDVIVRPIAGTRLRGKTPAEDLANEQDLLSDAKEIAEHVMLIDLGRNDVGRISKTGEVKVTDKMVIEKYSHVMHIVSNVEGRLKDGMTNMDILAATFPAGTLSGAPKVRAMEIIEEVEPSKRGIYGGAVGVWGFNNDMDLAIAIRTAVVKNNTLYVQSGAGVVADSDPASEWQETQNKARAVIRAAQMVQEGLDK

Gene
trpE
Protein
Anthranilate synthase component 1
Organism
Neisseria meningitidis serogroup B (strain MC58)
Length
491 amino acids
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).
Similarity
Belongs to the anthranilate synthase component I family.
Mass
54.702 kDa
Sequence
MISKQEYQAQAAQGYNRIPLVQELLADLDTPLSLYLKLANRPYTYLLESVVGGERFGRYSFIGLPCSHYLKASGKHVDVYQNGEIVEQHDGNPLPFIEAFHNRFKTPEIPSLPRFTGGLVGYFGYETIYNFEHFAHRLKNTTKADPLGTPDILLMLSQELAVIDNLSGKIHLVVYADPSQPDGYERARERLEDIRTQLRQSCAIPLSLGSKHTEAVSEFGEEPFKACVNKIKDYIFAGDCMQVVPSQRMSMEFTDSPLALYRALRTLNPSPYLFYYDFGDFHIVGSSPEILVRRERNDVIVRPIAGTRLRGKTPAEDLANEQDLLSDAKEIAEHVMLIDLGRNDVGRISKTGEVKVTDKMVIEKYSHVMHIVSNVEGRLKDGMTNMDILAATFPAGTLSGAPKVRAMEIIEEVEPSKRGIYGGAVGVWGFNNDMDLAIAIRTAVVKNNTLYVQSGAGVVADSDPASEWQETQNKARAVIHAAQMVQEGLDK

Gene
trpE
Protein
Anthranilate synthase component 1
Organism
Spirochaeta aurantia
Length
482 amino acids
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).
Similarity
Belongs to the anthranilate synthase component I family.
Mass
53.699 kDa
Sequence
MFLFVETIRPQQRGESLLETVIKVVPGERFTPYGLALKLGARVVLESSSSKKGRDRYSLLLLQEAFRVAQEGTEVYFVKDGRRSKVKANHRDILDVLMYFARQHSDPGQDFPFPAGGVGYLSFEFCRYCDTIHLNPAKPDPLELPDALFLFGHVFLIYDHYTDLIYLVGLNYKEASIDLEAALAAVEARVNDGDWSALGSVGAPYDAEVLPQDYDPDETYKANVGAMRQEVIAGNLLQGVPSRRLLVKTEMPAIEAYRRLRSSNPSPYMFYLDFGDYQLFRASPELHVKVKGGTAEIRPIAGTRRRGATDAEDRALEAELLADVKERAEHLMLVDLARNDLGRICQPGTVQVKDSYFIERYSHVMHIVSSVEGRLKDDKTGIDALRASFPAGTVSGAPKIRAIEVIDRLEPVQRRFYSGVVGHLSPDGSLDTCIAIRSALKKGDTMVLQAGGGIVFDSNPDRELEETYEKMRATARSLGLEI

Gene
trpE
Protein
Anthranilate synthase component 1
Organism
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Length
474 amino acids
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).
Similarity
Belongs to the anthranilate synthase component I family.
Mass
54.3 kDa
Sequence
MIIKKIKMDVCPLDVYEQIRGENTFLLESAEGVPKVARYSILGKAEGKVIFKNGKLKVESFTEFGDKAKDLEGKYECPLDALREVRNEYLKYIDISNIEPIPRFKGGLVGYLSYDIIRYWIDLSNINPKPINDLKFPDAEFFIVKDFISFDLKEKVINLIAEDDEGIRELERIIKNAKIGNNDNKEEKTTENKDLKIKSNMSKEEFIEAVKKAKEYIFAGDIFQVVLSRRIEIDLDNLDHLKIYKKVREINPSPYMYYLDFGDRKIIGSSPEILVRTDYKDNKRLVITRPIAGTIRRGKTEEEDKELEKKLLSDEKERAEHVMLVDLARNDIGKISKFGTVEVTDFMIIEKYSHVQHIVSNVVGELKDNYDSFLAVKATFPAGTLSGAPKVRAMEIIEELEKTWRGPYGGGVGYFGWDDLMDLAITIRTFVISKNKGYIQVGAGIVADSIPENEWEETERKGMANVKTIESLLK

Gene
trpE
Protein
Anthranilate synthase component 1
Organism
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Length
464 amino acids
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).
Similarity
Belongs to the anthranilate synthase component I family.
Mass
52.321 kDa
Sequence
MNVFGITELKNPVKEKIEFKEPFELFKSIYSEYDSSFLLESMESDTGLARYSFMGFEPQMIIRARSGFIEVEYEGSREEFDTENPFEFLRQFTRPAGKSRGFCGGLVGYISYQAARFFDSINLSPGNFPDFEFGLFLDGIMFNHLTGECSYISLKENRLPEISELLREETPTGHLKYRSMGTLFSRRRYLGMVEEARERIAEGEIFQAVLSNATDYRLRGDRLALYEALRRVNPSPYMYHLKLGSREITGSSPEMLVRVEDKQIETFPIAGTRPRGKTPHEDERIAAELLSDEKELAEHLMLVDLARNDLGRISEFGTVQVPEYMTIRRFSHVQHILSHVTGRLRKGMDALDALGAVFPAGTVSGAPKIRAMEIIESLEGVPRNAYAGALGYLSLNGNADFAITIRSMVAEGAYGRIQAGAGIVHDSVPEREYVECQNKAMAVLKSMELAGDGFDSDEPFIARR

Gene
trpE
Protein
Anthranilate synthase component 1
Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Length
462 amino acids
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).
Similarity
Belongs to the anthranilate synthase component I family.
Mass
51.635 kDa
Sequence
MERIRPYRKTFLADLETPVTAYLKLAEKAPVSFLLESVERGRQSRFSIVGVGARRTFRLKDGVFTVNGERVETRDPLRALYERVYAPLERHPDLPPFFGGVVGYAAYDLVRYYERLPSLKPDDLGLPDLLFVEPEVVAVFDHLKNLLHLVAPGRDPEEAEARLFWAERRLKGPLPGVPGERAGGRARFQADFSREAYLEAVRRALDYIRAGDIFQVVLSLRLSSPLTVHPFALYRALRSVNPSPYMGYLDLGEVVLVSASPESLLRSDGRRVVTRPIAGTRPRGKDEEEDKRLAEELLRDEKEVAEHVMLLDLSRNDIGRVAAFGTVRVLEPLHVEHYSHVMHLVSTVEGILAEGKTPLDALASVLPMGTVSGAPKIRAMEIIEELEPHRRGPYGGSFGYLAYDGAMDMALTLRTFVVAKGWMHVQAGAGIVADSVPEREYEECWNKARALLKAVEMAEAGL

Gene
trpE
Protein
Anthranilate synthase component 1
Organism
Leptospira biflexa
Length
462 amino acids
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).
Similarity
Belongs to the anthranilate synthase component I family.
Mass
51.834 kDa
Sequence
MSQTLPKIKIPKKPNYNSLALAEGIEFWELFRVIEAKYENCFLLESAGDNQYDSRYSVIGFQPSHLILGEPGILEIDGKKYPVENPYFALRELTDYNSLSISYAGGFVGYLGYQSMQFFEPKLQLKPHPDFPAMIFGLYLDGLIYDKFTGELIYFDNGTNRIHEVNQILEQLKKENSQKPKATVSLVKAGLSKEVHKQMVEEALEEVKAGNTFQCQIGFEEIYQVDGNPLAIYETLREINPSPHMYYVNLELVTILGASPSSLFRLRQGEMESFPLAGTTKRGVDAKEDTLLARKLLTDPKEIAEHNMLIDLHRNDVGRVAKFGTVKVRRRFDVKRFSHVQHISSEVVGILSSKEDMFSGLASSFPRGTLSGAPKIESDSKIIERIEKSPRGPYGGAVGSFGLNGDCTFAIPIRSFFVNGKKGFVRASGGIVFGFIEPEDEYQEIINKMASVRKALDLHKGP

Gene
trpE
Protein
Anthranilate synthase component 1
Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Length
461 amino acids
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).
Similarity
Belongs to the anthranilate synthase component I family.
Mass
52.24 kDa
Sequence
MGDSMHVLKLVSDLETPVSTFMKVSRGEEFAFLLESVELGSAFGRHSFIGIGKKDVLVFEKGILRTSNQQLDYTSSPLKAIKDWLEVYRYSVKHDELPSFRGGAVGFVSYDYISYIEKVKVKASVFPTFYFVVPEHLIIFDHLKNNVFIISDSPEELTSKVLSPFEEKPEKNVFVTEPESNFEREQFYKVVEKAKKYIVEGDIFQVVLSQAFTFKTTLDPFYIYRALRMINPSPYMFYLKFGDTVVLGSSPETMAKVEGDKATVKPIAGTRPRGRTVEEDLKLERELLNDEKEIAEHVMLVDLGRNDLGRVCKEGTVRVEKKMVIERYSHVMHIVSQVSGELKDDKDAVDVFEATFPAGTVSGAPKVRAMEIIEELEPTPRGPYAGAVGYFSFPDDKGRMNMDSAITIRSFFFKGKQGWLQAGAGIVYDSVPEREYQETLNKLRALFRSLEVAQKIQGGLF

Gene
trpE
Protein
Anthranilate synthase component 1
Organism
Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg)
Length
461 amino acids
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).
Similarity
Belongs to the anthranilate synthase component I family.
Mass
51.911 kDa
Sequence
MGVNVFGIINLEKPRKEKLEFREPFEVFKSIYSEYESSFLLESMESDTGLARYSFIGFEPEMIIRAREGVIEIDDGDSREEFDSKNPFEDLRGFLKMEKNSGGFCGGLVGYISYQAARFFDTIRLSEGDFPDFEFGLFLDGIMFNHLTGECSYISRHGNRLPDISPLLGDEVPTGTLGYRRERTLLSKRRYMDMVLEAKERIREGEIFQAVLSSATDYRLRGDRLAFYESLRRINPSPYMYHLKLGEREITGSSPEMLVRVEDRRIETFPIAGTRPRGRTEEEDGVIASDLLSDEKELAEHLMLVDLARNDIGRVSEFGSVEVPEYMTIKRFSHVQHILSHVTGKLRDGMDAVDALGAVFPAGTVSGAPKIRAMEIIESLEGVPRNAYAGALGYLSLNGNADFAITIRSMVCQGKTGRIQAGAGIVHDSIPEMEYLECQNKARALLKSMEMAGEQVDPDNR

Gene
trpE
Protein
Anthranilate synthase component 1
Organism
Lactococcus lactis subsp. lactis (strain IL1403)
Length
456 amino acids
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).
Similarity
Belongs to the anthranilate synthase component I family.
Mass
51.676 kDa
Sequence
MRKIKEISADTMTPISVYLRLKGKNKVILESIPRENDQSRFSIIALNPVKHIKFTDGILSVNDEIISDENPMEFLEKLVCQPESTDENLDLPFTSGAIGYAGFDTYGIFEGIQPELKDSIGTPDMYFMLYESALIFDHKREKLIFIEDNTYSQRSEKELQNALSANIESLSLLTEAENELTELSKLNFVSNMSQELFEEKVAKAKELIRNGDMFQVVLSQRLTADFTDNPFNYYRKLRVENPSSYMYFMEFDNFHVIGSSPERLVAVHGNQVSTNPIAGTRKRGQTEFEDQALIEDLESDPKEVAEHKMLVDLGRNDIGKISKYGSIEVPVFMKVEKYRYVMHITSEVTGELRPEFTAMDALRATLPAGTLSGAPKHRAYQRIYEFETQKRGIYGGAIGYLTKNGNCDFAIAIRTMVLKDKKAHVQAGAGIVYDSVPEHEYQETLNKAQGLLKVGQ

Gene
trpE
Protein
Anthranilate synthase component 1
Organism
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Length
438 amino acids
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).
Similarity
Belongs to the anthranilate synthase component I family.
Mass
48.31 kDa
Sequence
MPSPPEPPLHWRDCRLEPILGFPRPRELAKSLEVQGEEWIALLESGGGLQHRSRYSFLAWGRRKSSETDAIRAYEELERLADDKCRALPCRSPTFFLVSYEAVVGEEPWLSRLVGRHEWPGMTAFSPEYVVVYDHAGGRVSVCPGDTPLPAPASRKESFSAEGPTYETSRKGFEAMVADALERIRAGEAFQVVLSRVERYRVWGSLFSAYERLADANPSPYLYYARLGGRVIIGSSPELLVKLEAGRVETHPIAGTRPRGSTPIEDIELEVELLNDEKERAEHVMLVDLARNDITRVSIPGTVQVTSFMDIERYETVMHIVSRVEGVTRPSTTFVEALKALHPAGTVSGAPKPRAMEIIAELEEEARGPYAGAIGVAGSSAGEAAIVLRSAWLLDDGETLEARAGAGIVYDSKPEREYMETVQKLGSLKRALGVDMCG

Gene
trpE
Protein
Anthranilate synthase component 1
Organism
Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
Length
433 amino acids
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).
Similarity
Belongs to the anthranilate synthase component I family.
Mass
48.541 kDa
Sequence
MPLKKLKPVDPLKLYSALRDFGMPFMLRSAEKDSRKARFTYISAEPEFVVEVGEGTEIDGERVSDERNPLRALKGLMGERVEGRRFMGGFVGYVSYDSVHSIIGGKIEEPSVFGYYPWTFIYDHSTGALSFFYLREAPFDPEALVERARREESRLEDGGSEVISTDAGMEEFVEIVRAGKEYIYSGDVFQVVLSREYRVRTDLDALEIYKRLVELNPSPYTFILEFEKTVVGASPETMGSVEGRTFKINPIAGTAPRGRTGEEDRELEKALLSDEKERAEHVMLVDLARNDVRRVSKPGSVRLTRFFDVLKYSHVQHIESEVVGELDEGKNAFDAMEAAFPAGTLTGAPKIRAMEIIDELERSRRKVYGGAVGYFSLTGDADMAIAIRMAEIEGRKASVRAGAGIVADSVPEKEFFETENKMRAVLKALGVRE

Gene
trpE
Protein
Anthranilate synthase component 1
Organism
Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Length
421 amino acids
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.
Similarity
Belongs to the anthranilate synthase component I family.
Mass
47.652 kDa
Sequence
MEVHPISEFASPFEVFKCIERDFKVAGLLESIGGPQYKARYSVIAWSTNGYLKIHDDPVNILNGYLKDLKLADIPGLFKGGMIGYISYDAVRFWEKIRDLKPAAEDWPYAEFFTPDNIIIYDHNEGKVYVNADLSSVGGCGDIGEFKVSFYDESLNKNSYERIVSESLEYIRSGYIFQVVLSRFYRYIFSGDPLRIYYNLRRINPSPYMFYLKFDEKYLIGSSPELLFRVQDNIVETYPIAGTRPRGADQEEDLKLELELMNSEKDKAEHLMLVDLARNDLGKVCVPGTVKVPELMYVEKYSHVQHIVSKVIGTLKKKYNALNVLSATFPAGTVSGAPKPMAMNIIETLEEYKRGPYAGAVGFISADGNAEFAIAIRTAFLNKELLRIHAGAGIVYDSNPESEYFETEHKLKALKTAIGVR

Gene
trpE
Protein
Anthranilate synthase component 1
Organism
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Length
411 amino acids
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).
Similarity
Belongs to the anthranilate synthase component I family.
Mass
46.346 kDa
Sequence
MQKHEYVNPVKLYSAIRDEKFPFILESAEKSGRARYTYISFNPLYTVRVGSRTRVDGEVISKISDPFDALNEIHVKGLLVGYVAYEAVKNYIGKKPQTPSVFGCYDGYFVYDHYLRKLFSVNVENADKIVERAKRVEVEQVRGNSEVLRAGSREKFEKMVERGKEQIFEGEVYQIVLSREYVVDTDLSPFQMYLNLRETNPSPYMFLLEFDRALIGSSPETMGRVEGNSFIINPIAGTARREAGREKEIAEKLLSDEKERAEHVMLVDLARNDVRKVCRAGSVRVSRFMEVVEYPSVLHIESEVVGELKAGVTHFDAMKATFPAGTVTGAPKLRAIELIDEIEGDCRGVYAGAVGYFSENVSDLAIAIRMIEFDGKARIRAGAGIVADSVPEREFFETENKIARVLRAVGL

Gene
trpE
Protein
Anthranilate synthase component 1
Organism
Citrobacter freundii
Length
150 amino acids
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).
Similarity
Belongs to the anthranilate synthase component I family.
Mass
16.187 kDa
Fragment
single
Sequence
MQTQKPTLELVACDAAYRENPTALFHQVCGARPATLLLESADIDSKDDLKSLLLVDSALRITAIGDTVTIQALSANGASLLPLLDAALPAGVENKQQPNGRHLRFPAVSPLLDEDVRLRSLSAPDAFRPLQELVNVPAQEREVMFLGGMF