>15380 FitnessBrowser__Keio:15380
MERYESLFAQLKERKEGAFVPFVTLGDPGIEQSLKIIDTLIEAGADALELGIPFSDPLADGPTIQNATLRAFAAGVTPAQCFEMLALIRQKHPTIPIGLLMYANLVFNKGIDEFYAQCEKVGVDSVLVADVPVEESAPFRQAALRHNVAPIFICPPNADDDLLRQIASYGRGYTYLLSRAGVTGAENRAALPLNHLVAKLKEYNAAPPLQGFGISAPDQVKAAIDAGAAGAISGSAIVKIIEQHINEPEKMLAALKVFVQPMKAATRS
>BRENDA__P00929 tryptophan synthase (EC 4.2.1.20) (Salmonella enterica subsp. enterica serovar Typhimurium)
MERYENLFAQLNDRREGAFVPFVTLGDPGIEQSLKIIDTLIDAGADALELGVPFSDPLADGPTIQNANLRAFAAGVTPAQCFEMLALIREKHPTIPIGLLMYANLVFNNGIDAFYARCEQVGVDSVLVADVPVEESAPFRQAALRHNIAPIFICPPNADDDLLRQVASYGRGYTYLLSRSGVTGAENRGALPLHHLIEKLKEYHAAPALQGFGISSPEQVSAAVRAGAAGAISGSAIVKIIEKNLASPKQMLAELRSFVSAMKAASRA
>biolip__8b08A Tryptophan synthase - cryo-trapping by the spitrobot crystal plunger after 30 sec
HMERYENLFAQLNDRREGAFVPFVTLGDPGIEQSLKIIDTLIDAGADALELGVPFSDPLADGPTIQNANLRAFAAGVTPAQCFEMLALIREKHPTIPIGLLMYANLVFNNGIDAFYARCEQVGVDSVLVADVPVEESAPFRQAALRHNIAPIFICPPNADDDLLRQVASYGRGYTYLLSRSGVTGAENRGALPLHHLIEKLKEYHAAPALQGFGISSPEQVSAAVRAGAAGAISGSAIVKIIEKNLASPKQMLAELRSFVSAMKAASRA
>PDB_1tjp_A Crystal structure of wild-type tryptophan synthase complexed with 1- [(2-hydroxylphenyl)amino]3-glycerolphosphate
MERYENLFAQLNDRREGAFVPFVTLGDPGIEQSLKIIDTLIDAGADALELGVPFSDPLADGPTIQNANLRAFAAGVTPAQ
CFEMLALIREKHPTIPIGLLMYANLVFNNGIDAFYARCEQVGVDSVLVADVPVEESAPFRQAALRHNIAPIFICPPNADD
DLLRQVASYGRGYTYLLSRSGVTGAENRGALPLHHLIEKLKEYHAAPALQGFGISSPEQVSAAVRAGAAGAISGSAIVKI
IEKNLASPKQMLAELRSFVSAMKAASR
>PDB_1k3u_A Crystal structure of wild-type tryptophan synthase complexed with n- [1h-indol-3-yl-acetyl]aspartic acid
MERYENLFAQLNDRREGAFVPFVTLGDPGIEQSLKIIDTLIDAGADALELGVPFSDPLADGPTIQNANLRAFAAGVTPAQ
CFEMLALIREKHPTIPIGLLMYANLVFNNGIDAFYARCEQVGVDSVLVADVPVEESAPFRQAALRHNIAPIFICPPNADD
DLLRQVASYGRGYTYLLSRSGVTGAENRGALPLHHLIEKLKEYHAAPALQGFGISSPEQVSAAVRAGAAGAISGSAIVKI
IEKNLASPKQMLAELRSFVSAMKAASRA
>PDB_2clk_A Tryptophan synthase in complex with d-glyceraldehyde 3- phosphate (g3p)
MERYENLFAQLNDRREGAFVPFVTLGDPGIEQSLKIIDTLIDAGADALELGVPFSDPLADGPTIQNANLRAFAAGVTPAQ
CFEMLAIIREKHPTIPIGLLMYANLVFNNGIDAFYARCEQVGVDSVLVADVPVEESAPFRQAALRHNIAPIFICPPNADD
DLLRQVASYGRGYTYLLSRSGVTGAENRGALPLHHLIEKLKEYHAAPALQGFGISSPEQVSAAVRAGAAGAISGSAIVKI
IEKNLASPKQMLAELRSFVSAMKAASR
>PDB_7jll_A The internal aldimine crystal structure of salmonella typhimurium tryptophan synthase mutant beta-s377a in complex with inhibitor 2- ({[4-(trifluoromethoxy)phenyl]sulfonyl}amino)ethyl dihydrogen phosphate (f9f) at the alpha-site, cesium ion at the metal coordination site and l-tryptophan at the enzyme beta-site
ERYENLFAQLNDRREGAFVPFVTLGDPGIEQSLKIIDTLIDAGADALELGVPFSDPLADGPTIQNANLRAFAAGVTPAQC
FEMLALIREKHPTIPIGLLMYANLVFNNGIDAFYARCEQVGVDSVLVADVPVEESAPFRQAALRHNIAPIFICPPNADDD
LLRQVASYGRGYTYLLSRSGVTGAENRGALPLHHLIEKLKEYHAAPALQGFGISSPEQVSAAVRAGAAGAISGSAIVKII
EKNLASPKQMLAELRSFVSAMKAASRA
>PDB_6xnc_A Salmonella typhimurium tryptophan synthase complexed with l-tryptophan and d-glycerol-3-phosphate
ERYENLFAQLNDRREGAFVPFVTLGDPGIEQSLKIIDTLIDAGADALELGVPFSDPLADGPTIQNANLRAFAAGVTPAQC
FEMLALIREKHPTIPIGLLMYANLVFNNGIDAFYARCEQVGVDSVLVADVPVEESAPFRQAALRHNIAPIFICPPNADDD
LLRQVASYGRGYTYLLSRSGVTGAENRGALPLHHLIEKLKEYHAAPALQGFGISSPEQVSAAVRAGAAGAISGSAIVKII
EKNLASPKQMLAELRSFVSAMKAASRA
>PDB_3cep_A Structure of a tryptophan synthase quinonoid intermediate
ERYENLFAQLNDRREGAFVPFVTLGDPGIEQSLKIIDTLIDAGADALELGVPFSDPLADGPTIQNANLRAFAAGVTPAQC
FEMLAIIREKHPTIPIGLLMYANLVFNNGIDAFYARCEQVGVDSVLVADVPVEESAPFRQAALRHNIAPIFICPPNADDD
LLRQVASYGRGYTYLLSRSGVTGAENRGALPLHHLIEKLKEYHAAPALQGFGISSPEQVSAAVRAGAAGAISGSAIVKII
EKNLASPKQMLAELRSFVSAMKAASR
>PDB_1cx9_A Crystal structure of the complex of bacterial tryptophan synthase with the transition state analogue inhibitor 4-(2-aminophenylthio)- butylphosphonic acid
ERYENLFAQLNDRREGAFVPFVTLGDPGIEQSLKIIDTLIDAGADALELGVPFSDPLADGPTIQNANLRAFAAGVTPAQC
FEMLALIREKHPTIPIGLLMYANLVFNNGIDAFYARCEQVGVDSVLVADVPVEESAPFRQAALRHNIAPIFICPPNADDD
LLRQVASYGRGYTYLLSRSGVTGAENRGPLHHLIEKLKEYHAAPALQGFGISSPEQVSAAVRAGAAGAISGSAIVKIIEK
NLASPKQMLAELRSFVSAMKAASR
>PDB_1cw2_A Crystal structure of the complex of bacterial tryptophan synthase with the transition state analogue inhibitor 4-(2-hydroxyphenylsulfinyl)- butylphosphonic acid
ERYENLFAQLNDRREGAFVPFVTLGDPGIEQSLKIIDTLIDAGADALELGVPFSDPLADGPTIQNANLRAFAAGVTPAQC
FEMLALIREKHPTIPIGLLMYANLVFNNGIDAFYARCEQVGVDSVLVADVPVEESAPFRQAALRHNIAPIFICPPNADDD
LLRQVASYGRGYTYLLSRSGVTGAENRGPLHHLIEKLKEYHAAPALQGFGISSPEQVSAAVRAGAAGAISGSAIVKIIEK
NLASPKQMLAELRSFVSAMKAASR
>PDB_1c9d_A Crystal structure of the complex of bacterial tryptophan synthase with the transition state analogue inhibitor 4-(2-hydroxy-4- fluorophenylthio)-butylphosphonic acid
ERYENLFAQLNDRREGAFVPFVTLGDPGIEQSLKIIDTLIDAGADALELGVPFSDPLADGPTIQNANLRAFAAGVTPAQC
FEMLALIREKHPTIPIGLLMYANLVFNNGIDAFYARCEQVGVDSVLVADVPVEESAPFRQAALRHNIAPIFICPPNADDD
LLRQVASYGRGYTYLLSRSGVTGAENRGPLHHLIEKLKEYHAAPALQGFGISSPEQVSAAVRAGAAGAISGSAIVKIIEK
NLASPKQMLAELRSFVSAMKAASR
>PDB_1c29_A Crystal structure of the complex of bacterial tryptophan synthase with the transition state analogue inhibitor 4-(2-hydroxyphenylthio)-1- butenylphosphonic acid
ERYENLFAQLNDRREGAFVPFVTLGDPGIEQSLKIIDTLIDAGADALELGVPFSDPLADGPTIQNANLRAFAAGVTPAQC
FEMLALIREKHPTIPIGLLMYANLVFNNGIDAFYARCEQVGVDSVLVADVPVEESAPFRQAALRHNIAPIFICPPNADDD
LLRQVASYGRGYTYLLSRSGVTGAENRGPLHHLIEKLKEYHAAPALQGFGISSPEQVSAAVRAGAAGAISGSAIVKIIEK
NLASPKQMLAELRSFVSAMKAASR
>PDB_2trs_A Crystal structures of mutant (betak87t) tryptophan synthase alpha2 beta2 complex with ligands bound to the active sites of the alpha and beta subunits reveal ligand-induced conformational changes
MERYENLFAQLNDRREGAFVPFVTLGDPGIEQSLKIIDTLIDAGADALELGVPFSDPLADGPTIQNANLRAFAAGVTPAQ
CFEMLALIREKHPTIPIGLLMYANLVFNNGIDAFYARCEQVGVDSVLVADVPVEESAPFRQAALRHNIAPIFICPPNADD
DLLRQVASYGRGYTYLLSRSGVTGAENHHLIEKLKEYHAAPALQGFGISSPEQVSAAVRAGAAGAISGSAIVKIIEKNLA
SPKQMLAELRSFVSAMKAASRA
>biolip__1xc4A Crystal structure of wild-type tryptophan synthase alpha-subunits from escherichia coli
MERYESLFAQLKERKEGAFVPFVTLGDPGIEQSLKIIDTLIEAGADALELGIPFVTPAQCFEMLALIREKHPTIPIGLLMYANLVFNKGIDEFYARCEKVGVDSVLVADVPVEESAPFRQAALRHNVAPIFICPPNADDDLLRQIASYGRGYTYLLSRAGAALPLNHLVAKLKEYNAAPPLQGFGISAPDQVKAAIDAGAAGAISGSAIVKIIEQHINEPEKMLAALKVFVQPMKAATRS
>PDB_1k7e_A Crystal structure of wild-type tryptophan synthase complexed with n- [1h-indol-3-yl-acetyl]glycine acid
MERYENLFAQLNDRREGAFVPFVTLGDPGIEQSLKIIDTLIDAGADALELGVPFSDPLADGPTIQNANLRAFAAGVTPAQ
CFEMLALIREKHPTIPIGLLMYANLVFNNGIDAFYARCEQVGVDSVLVADVPVEESAPFRQAALRHNIAPIFICPPNADD
DLLRQVASYGRGYTYLLSRSGVTGPLHHLIEKLKEYHAAPALQGFGISSPEQVSAAVRAGAAGAISGSAIVKIIEKNLAS
PKQMLAELRSFVSAMKAASRA
>PDB_1a50_A Crystal structure of wild-type tryptophan synthase complexed with 5- fluoroindole propanol phosphate
ERYENLFAQLNDRREGAFVPFVTLGDPGIEQSLKIIDTLIDAGADALELGVPFSDPLADGPTIQNANLRAFAAGVTPAQC
FEMLALIREKHPTIPIGLLMYANLVFNNGIDAFYARCEQVGVDSVLVADVPVEESAPFRQAALRHNIAPIFICPPNADDD
LLRQVASYGRGYTYLLSRSGVTGAENHHLIEKLKEYHAAPALQGFGISSPEQVSAAVRAGAAGAISGSAIVKIIEKNLAS
PKQMLAELRSFVSAMKAASR
>PDB_2clh_A Tryptophan synthase in complex with (naphthalene-2'-sulfonyl)-2-amino- 1-ethylphosphate (f19)
MERYENLFAQLNDRREGAFVPFVTLGDPGIEQSLKIIDTLIDAGADALELGVPFSDPLADGPTIQNANLRAFAAGVTPAQ
CFEMLALIREKHPTIPIGLLMYANLVFNNGIDAFYARCEQVGVDSVLVADVPVEESAPFRQAALRHNIAPIFICPPNADD
DLLRQVASYGRGYTYLLSRSGVTGHHLIEKLKEYHAAPALQGFGISSPEQVSAAVRAGAAGAISGSAIVKIIEKNLASPK
QMLAELRSFVSAMKAASR
>PDB_2cli_A Tryptophan synthase in complex with n-(4'- trifluoromethoxybenzenesulfonyl)-2-amino-1-ethylphosphate (f9)
MERYENLFAQLNDRREGAFVPFVTLGDPGIEQSLKIIDTLIDAGADALELGVPFSDPLADGPTIQNANLRAFAAGVTPAQ
CFEMLALIREKHPTIPIGLLMYANLVFNNGIDAFYARCEQVGVDSVLVADVPVEESAPFRQAALRHNIAPIFICPPNADD
DLLRQVASYGRGYTYLLSRSGVTGHLIEKLKEYHAAPALQGFGISSPEQVSAAVRAGAAGAISGSAIVKIIEKNLASPKQ
MLAELRSFVSAMKAASRA
>PDB_6xin_A The crystal structure of tryptophan synthase from salmonella enterica serovar typhimurium in complex with (2s)-3-amino-3-imino-2- phenyldiazenylpropanamide at the enzyme alpha-site.
MERYENLFAQLNDRREGAFVPFVTLGDPGIEQSLKIIDTLIDAGADALELGVPFSDPLADGPTIQNANLRAFAAGVTPAQ
CFEMLALIREKHPTIPIGLLMYANLVFNNGIDAFYARCEQVGVDSVLVADVPVEESAPFRQAALRHNIAPIFICPPNADD
DLLRQVASYGRGYTYLLSRALPLHHLIEKLKEYHAAPALQGFGISSPEQVSAAVRAGAAGAISGSAIVKIIEKNLASPKQ
MLAELRSFVSAMKAASRA
>PDB_1k7f_A Crystal structure of wild-type tryptophan synthase complexed with n- [1h-indol-3-yl-acetyl]valine acid
MERYENLFAQLNDRREGAFVPFVTLGDPGIEQSLKIIDTLIDAGADALELGVPFSDPLADGPTIQNANLRAFAAGVTPAQ
CFEMLALIREKHPTIPIGLLMYANLVFNNGIDAFYARCEQVGVDSVLVADVPVEESAPFRQAALRHNIAPIFICPPNADD
DLLRQVASYGRGYTYLLSLHHLIEKLKEYHAAPALQGFGISSPEQVSAAVRAGAAGAISGSAIVKIIEKNLASPKQMLAE
LRSFVSAMKAASR
>PDB_7jqw_A The external aldimine crystal structure of salmonella typhimurium tryptophan synthase mutant beta-s377a in complex with cesium ion at the metal coordination site. The single beta-q114 rotamer conformation allows a hydrogen bond to form with the plp oxygen at the position 3 in the ring
MERYENLFAQLNDRREGAFVPFVTLGDPGIEQSLKIIDTLIDAGADALELGVPFSDPLADGPTIQNANLRAFAAGVTPAQ
CFEMLALIREKHPTIPIGLLMYANLVFNNGIDAFYARCEQVGVDSVLVADVPVEESAPFRQAALRHNIAPIFICPPNADD
DLLRQVASYGRGYTYLLLHHLIEKLKEYHAAPALQGFGISSPEQVSAAVRAGAAGAISGSAIVKIIEKNLASPKQMLAEL
RSFVSAMKAASRA
>PDB_6x0c_A Tryptophan synthase mutant beta-q114a in complex with cesium ion at the metal coordination site and aminoacrylate and benzimidazole at the enzyme beta site
MERYENLFAQLNDRREGAFVPFVTLGDPGIEQSLKIIDTLIDAGADALELGVPFSDPLADGPTIQNANLRAFAAGVTPAQ
CFEMLALIREKHPTIPIGLLMYANLVFNNGIDAFYARCEQVGVDSVLVADVPVEESAPFRQAALRHNIAPIFICPPNADD
DLLRQVASYGRGYTYLLLHHLIEKLKEYHAAPALQGFGISSPEQVSAAVRAGAAGAISGSAIVKIIEKNLASPKQMLAEL
RSFVSAMKAASRA
>PDB_6vfd_A Tryptophan synthase mutant q114a in complex with cesium ion at the metal coordination site and 2-aminophenol quinonoid at the enzyme beta site
MERYENLFAQLNDRREGAFVPFVTLGDPGIEQSLKIIDTLIDAGADALELGVPFSDPLADGPTIQNANLRAFAAGVTPAQ
CFEMLALIREKHPTIPIGLLMYANLVFNNGIDAFYARCEQVGVDSVLVADVPVEESAPFRQAALRHNIAPIFICPPNADD
DLLRQVASYGRGYTYLLLHHLIEKLKEYHAAPALQGFGISSPEQVSAAVRAGAAGAISGSAIVKIIEKNLASPKQMLAEL
RSFVSAMKAASRA
>PDB_2cle_A Tryptophan synthase in complex with n-(4'- trifluoromethoxybenzoyl)-2-amino-1-ethylphosphate (f6) - lowf6 complex
ERYENLFAQLNDRREGAFVPFVTLGDPGIEQSLKIIDTLIDAGADALELGVPFSDPLADGPTIQNANLRAFAAGVTPAQC
FEMLALIREKHPTIPIGLLMYANLVFNNGIDAFYARCEQVGVDSVLVADVPVEESAPFRQAALRHNIAPIFICPPNADDD
LLRQVASYGRGYTYLLSHHLIEKLKEYHAAPALQGFGISSPEQVSAAVRAGAAGAISGSAIVKIIEKNLASPKQMLAELR
SFVSAMKAASR
>PDB_1a5b_A Cryo-crystallography of a true substrate, indole-3-glycerol phosphate, bound to a mutant (alpha d60n) tryptophan synthase alpha2beta2 complex reveals the correct orientation of active site alpha glu 49
MERYENLFAQLNDRREGAFVPFVTLGDPGIEQSLKIIDTLIDAGADALELGVPFSDPLANGPTIQNANLRAFAAGVTPAQ
CFEMLALIREKHPTIPIGLLMYANLVFNNGIDAFYARCEQVGVDSVLVADVPVEESAPFRQAALRHNIAPIFICPPNADD
DLLRQVASYGRGYTYLLIEKLKEYHAAPALQGFGISSPEQVSAAVRAGAAGAISGSAIVKIIEKNLASPKQMLAELRSFV
SAMKAASRA
>biolip__5ey5A Lbcats
MNRIAEAFEELKKKGEKALIPFITAGDPDLETTLELVRALVEAGADIIELGIPFSDPLADGPTIQRASQRALASGTTLDKVFEMVRELREKNTDVPIVFLTYYNPIFRYGIERFVKECAEAGVDGLIVPDLPPEEAADLAAAAEKYGVDLIFLVAPTSTDERIKMIAKHASGFVYCVSVTGVTGARSEISRIRKHTDLPIAVGFGISTPEQAAEVAQVADGVIVGSAIVKRIEENQDEEDIVEEVREFVRELREAVKLEHH
>SwissProt__O22765 Tryptophan synthase alpha chain; Indole synthase; Indole-3-glycerol-phosphate lyase; EC 4.2.1.20; EC 4.1.2.8 (Arabidopsis thaliana (Mouse-ear cress))
MDLLKTPSSTVGLSETFARLKSQGKVALIPYITAGDPDLSTTAKALKVLDSCGSDIIELGVPYSDPLADGPAIQAAARRSLLKGTNFNSIISMLKEVIPQLSCPIALFTYYNPILRRGVENYMTVIKNAGVHGLLVPDVPLEETETLRNEARKHQIELVLLTTPTTPKERMNAIVEASEGFIYLVSSVGVTGTRESVNEKVQSLLQQIKEATSKPVAVGFGISKPEHVKQVAEWGADGVIVGSAMVKILGESESPEQGLKELEFFTKSLKSALVS
>BRENDA__B2Y0K4 indole-3-glycerol-phosphate lyase (EC 4.1.2.8) (Zea mays)
MAFALKAAAAGSASFSAAGPRRRAAATGRVSFRSAAPVVAVRAAAAAAAAVAEDKRSISGTFAELRQQGKTALIPFITAGDPDLATTAKALRILDACGSDVIELGVPYSDPLADGPVIQASATRALAKGTTFEDVISMVKGVIPDLSCPVALFTYYNPILKRGVPNFMSIVKEAGVHGLVVPDVPLEETDVLRSEAAKNNLELVLLTTPTTPNERMEKIAQASEGFIYLVSTVGVTGTRANVSGKVQSLLQDIKKVTEKPVAVGFGVSTPEHVRQIAGWGADGVIIGSAVMKTLEEAASPEEGLKKLEQFAKNLKAALP
>SwissProt__Q42529 Tryptophan synthase alpha chain, chloroplastic; Indole-3-glycerol-phosphate lyase, chloroplastic; Protein TRYPTOPHAN-REQUIRING 3; EC 4.2.1.20; EC 4.1.2.8 (Arabidopsis thaliana (Mouse-ear cress))
MAIAFKSGVFFLQSPKSQIGFRHSSPPDSSLSFKRFTPMASLSTSSPTLGLADTFTQLKKQGKVAFIPYITAGDPDLSTTAEALKVLDACGSDIIELGVPYSDPLADGPVIQAAATRSLERGTNLDSILEMLDKVVPQISCPISLFTYYNPILKRGLGKFMSSIRAVGVQGLVVPDVPLEETEMLRKEALNNDIELVLLTTPTTPTERMKLIVDASEGFIYLVSSIGVTGARSSVSGKVQSLLKDIKEATDKPVAVGFGISKPEHVKQIAGWGADGVIVGSAMVKLLGDAKSPTEGLKELEKLTKSLKSALL
>metacyc__MONOMER-3561 tryptophan synthase subunit α (EC 4.1.2.8) (Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1))
MFEKGSLIPYLTAGDPSVEKTLEFLLAVEEFAGLIELGIPFSDPMADGKTIQESHYRALRNGFKLDDTFRILREFRRHSSTPVILMTYYNPVFRTGVKKFLGEAKASGADGILVVDLPVSHAGEFLDAAKEEGLKTVFLAAPNTPDERLREIDKASTGFVYLISLYGTTGARDRLPETAFEFVRRARKICNNKLAVGFGVSRREQVEELLKAGADGVVVGSALIELISRSENPVEELRRKVAELSGYSRAL
>BRENDA__Q659I8 tryptophan synthase (EC 4.2.1.20) (Isatis tinctoria)
MAIAFKSGVCFLQSAKPQIGIRHSSPDSSLSFKRLTPIAALSTSSPTLGLADTFKELKKQGKVAFIPYITAGDPDLSTTAEALKVLAASGSDIIELGVPYSDPLADGPVIQAAATRALENGTNLDNILDMLDKVLPQVSCPVSLFTYYNPILKRGLGKFMSSIRDVGVQGLVEPDVPLEETEMLRKEALNNNIELVLLTTPTTPTERMKRIVDASEGFIYLVSSIGVTGARASVSGKVQSLLKDIKEATDKPVAVGFGISQPEHVKQIAGWGADGVIVGSAMVRLLGDAKSPTEGLKELERLTKSLKSALL
>SwissProt__P18284 Tryptophan synthase alpha chain; EC 4.2.1.20 (Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii))
MSLEDAFSDGPAFVPYLAAGDPDYESSLEYVEALERGGADVIELGLPFSEPIAEGPTIQNAVVRSLEGGMTPTRFFEFVEDLDVSVPLVCMTYYNLIYRYGDEPGPRPFVEKAAEVGIEGFVVPDLPAEEAGPLREACDEFGLDLVFIVAPTTRGERLDRIMEQVSGYVYVQARLGTTGAQSSVSDQTDSSLERLTDYDVPKAVGFGISDGDHAERIVASGADGIIVGSALVDIVAEGHENGDDAETVADRLETLARELEDGAVAGASQRPPHPERT
>BRENDA__Q8U094 tryptophan synthase (subunit 1/2) (EC 4.2.1.20) (Pyrococcus furiosus)
MFKDGSLIPYLTAGDPDKQSTLNFLLALDEYAGAIELGIPFSDPIADGKTIQESHYRALKNGFKLREAFWIVKEFRRHSSTPIVLMTYYNPIYRAGVRNFLAEAKASGVDGILVVDLPVFHAKEFTEIAREEGIKTVFLAAPNTPDERLKVIDDMTTGFVYLVSLYGTTGAREEIPKTAYDLLRRAKRICRNKVAVGFGVSKREHVVSLLKEGANGVVVGSALVKIIGEKGREATEFLKKKVEELLGI
>BRENDA__Q7Y1I9 indole-3-glycerol-phosphate lyase (EC 4.1.2.8) (Oryza sativa)
MAFTVKASSPSSPAASSSSSSAPAKLGAAPGRVAVRKLTAAATSLRLDRAPAAPATERGLSSVSRTMSRLMEKGKTAFIPYITAGDPDMGTTAEALRLLDACGADVIELGVPFSDPYNDGPVIQASAARALSAGATMDGIMSMLAEVTPELSCPVVLFSYLGPIVRRGPANFTAAAKEAGVQGLIVPDLPYLEACSFRSEVIKNNLELVLLTTPTTPPDRMKAITAASGGFVYLVSVNGVTGSRQDVNPRVEHLLQEIKQVTDKAVCVGYGISTPDHVRQIAEWGADGVIIGSAMVRQLGEAASPKQGLKRLEKYARSLKNALP
>metacyc__MONOMER-10161 indole-3-glycerol phosphate lyase (EC 4.1.2.8) (Zea mays)
MASAIKAASTSSRWSSSPAAVHSSPLSKRLPAAVAMPGRRRSVATVRAVAAVAPAAPAAPAKLTAGAGGRCLPVSQTMSRLRAQGKTAFIPYITAGDPDLATTAEALRLLDACGADVIELGVPFSDPYADGPVIQASAARALASGTTPDGVLAMLKEVTPELSCPVVLFSYFNPIVRWGLADFAAAVKEAGVHGLIVPDLPYGNSCALTLRTEAIKNSLELVLLTTPSTPADRMEEITRASRGFVYLATVNGVTGPRANVNTRVQSLIQEVKQVTDIPVAVGFGISKPEHVKQIAEWGADGVIIGSAMVRQLGEAASPKEGLKRLEKYARSMKNALPCQ
>BRENDA__A0A1C9CXC5 indole-3-glycerol-phosphate lyase (EC 4.1.2.8) (Persicaria tinctoria)
MAVSLRSTCFLQRRSCFDKPFITAPSPSSHKQSVVCFRSTKIMASLATSKVVGLSETFARLKEQNKVALISYITAGDPDLSVTAEALKLLDTCGSDIIELGLPYSDPLADGPVIQAASTRALAKGTNLNSVLSMLTKVLPDLSCPVALFCYYNPILKRGVENFMSTIREAGVHGLVVPDVPLEETEVLRREAAKKNIELVLLTTPTTPVARMKAIVEASEGFVYLVSAVGVTGTRTSVSNKVEMLLKDIKQAATKKHVAVGFGISTPEHVAQVAGWGADGVIVGSAMVKALGDAKSPEEGLKELELLTKSLKSALI
>CharProtDB__CH_122413 bifunctional tryptophan synthase TRPB (Emericella nidulans)
MEHIKNTFEKVKREKRAALVAYITAGYPTIEESVDILLGLENGGADIIELGVPFTDPIADGPTIQKANTKALANGVTVSTVLEMVQHQRNRGLKAPIMLMGYYNPMLSYGEERMLRDCKEVGVNGFIMVDLPPEEAVRFRDLCTSTGLSYVPLIAPATSESRMKLLCKIADSFIYVVSRMGVTGATGTLSSNIPELLARVHKWSGNVPTALGFGVSTREHFLSVQEISEGVVIGSQIITVLGEAPAGQAAQKAEEYLSSVTGRKLERDTSGALTREVNVLEPVLKIETPPMSQPTDVITEKDTPSGPGLGDQLEALNGGGSSSATPARFGEFGGQYVPESLMDCLAELERGFDSALKDPSFWEEYRSYYPYMGRPSSLHLATRLTEHVGGANIWLKREDLNHTGSHKINNALGQILLARRLGKTRIIAETGAGQHGVATATVCAKFGMKCVVYMGAEDVRRQALNVFRMKLLGASVVAVDAGSRTLRDAVNEALRAWVVDLDTTHYIIGSAIGPHPFPTIVRTYQSVIGEETKQQLQEQIGKLPDAVVACVGGGSNAVGSFYPFSKDTSVKLLGVEAGGDGIDTNRHSATLSGGSKGVLHGVRTYILQDEHGQVSETHSISAGLDYPGVGPELSNWKDSDRAHFIAATDAQALSGFRTMAQTEGIIPALESSHAIWGAQELAKTMKGKGDIVLTVSGRGDKDVESVAESLPKLGPQIGWDLRF
>SwissProt__P00931 Tryptophan synthase; EC 4.2.1.20 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast))
MSEQLRQTFANAKKENRNALVTFMTAGYPTVKDTVPILKGFQDGGVDIIELGMPFSDPIADGPTIQLSNTVALQNGVTLPQTLEMVSQARNEGVTVPIILMGYYNPILNYGEERFIQDAAKAGANGFIIVDLPPEEALKVRNYINDNGLSLIPLVAPSTTDERLELLSHIADSFVYVVSRMGTTGVQSSVASDLDELISRVRKYTKDTPLAVGFGVSTREHFQSVGSVADGVVIGSKIVTLCGDAPEGKRYDVAKEYVQGILNGAKHKVLSKDEFFAFQKESLKSANVKKEILDEFDENHKHPIRFGDFGGQYVPEALHACLRELEKGFDEAVADPTFWEDFKSLYSYIGRPSSLHKAERLTEHCQGAQIWLKREDLNHTGSHKINNALAQVLLAKRLGKKNVIAETGAGQHGVATATACAKFGLTCTVFMGAEDVRRQALNVFRMRILGAKVIAVTNGTKTLRDATSEAFRFWVTNLKTTYYVVGSAIGPHPYPTLVRTFQSVIGKETKEQFAAMNNGKLPDAVVACVGGGSNSTGMFSPFEHDTSVKLLGVEAGGDGVDTKFHSATLTAGRPGVFHGVKTYVLQDSDGQVHDTHSVSAGLDYPGVGPELAYWKSTGRAQFIAATDAQALLGFKLLSQLEGIIPALESSHAVYGACELAKTMKPDQHLVINISGRGDKDVQSVAEVLPKLGPKIGWDLRFEEDPSA
>CharProtDB__CH_123254 likely tryptophan synthetase alpha chain (Candida albicans)
MSALLKETFARCKKEGRNALVNFITAGFPTIDDTIPILQNMQNAGVDIIELGVPFSDPIADGPTIQQANNIALDNGITVPKCLELLSQARDQGVTVPIILMGYYNPILKYGEQKFLKDAAEAGANGFIVVDLPPEEAIKFRTECTKYGLSYVPLVAPATSNDRLKILGEIADSFIYVVSKMGTTGASTKVSTGIQELCDRVRKYAGPDTPLAVGFGVSTREHFLTVGEVADGVVIGSKIITLIGDSKPGERGKVAYDYVQSILGNDFKPNYPKTFERNNNNQAKETKPVLEENHKYNPRFGDFGGQYVPEALHTCLAELEKGFEDAVADPEFWKEFRDLYSYIGRPSSLHKAERLSEHAGGAQIWLKREDLNHTGSHKINNALAQVLIAKRLGKKKIIAETGAGQHGVATATACAKFGLECTVFMGAEDTRRQALNVFRMKILGANVVPVKNGTQTLRDATSEAFRFWVSNLETTHYVVGSAIGPHPYPTLVRTFQSVIGQETKEQFKALNNGKLPNAVVACVGGGSNSTGMFSPFENDKEVKLLGVEAGGDGLDTERHSATLTAGIPGVFHGVKTYVLQDNDGQVHDTHSVSAGLDYPGVGPELAYWKSIGRAEFVAATDAQALEGFRLLSQLEGIIPALESSHAIYGAVELAKTMSKDQHIVINVSGRGDKDVQSVAEVLPKLGEQIGWDLRFEEDPSKV
>metacyc__MONOMER-10162 indole-3-glycerol phosphate lyase (EC 4.1.2.8) (Zea mays)
MAFAPKTSSSSSLSSALQAAQSPPLLLRRMSSTATPRRRYDAAVVVTTTTTARAAAAAVTVPAAPPQAPAPAPVPPKQAAAPAERRSRPVSDTMAALMAKGKTAFIPYITAGDPDLATTAEALRLLDGCGADVIELGVPCSDPYIDGPIIQASVARALASGTTMDAVLEMLREVTPELSCPVVLLSYYKPIMSRSLAEMKEAGVHGLIVPDLPYVAAHSLWSEAKNNNLELVLLTTPAIPEDRMKEITKASEGFVYLVSVNGVTGPRANVNPRVESLIQEVKKVTNKPVAVGFGISKPEHVKQIAQWGADGVIIGSAMVRQLGEAASPKQGLRRLEEYARGMKNALP
>metacyc__MONOMER-344 α subunit of tryptophan synthase (EC 4.1.2.8) (Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8))
MKGFIAYIPAGFPDLETTRKILIALNELGITGVEIGVPFSDPVADGPVIQLAHSVALRNGVTIKKILEMLSEISVDYDLYLMSYLNPIVNYPEGKEKLLDELKKLGVKGLIIPDLPLREVKNVDIAYPIVPFVAPNTKDEEIDLINSVQAPFVYYISRYGVTGEREDLPFADHIKRVKERIKLPLFVGFGISRHEQVKKVWEIADGVIVGSALVRIMEENPKDEIPRKVVEKVKELLGK