ID G2WHI3_YEASK Unreviewed; 484 AA. AC G2WHI3; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 29-MAY-2024, entry version 44. DE RecName: Full=Multifunctional tryptophan biosynthesis protein {ECO:0000256|ARBA:ARBA00018819}; DE EC=4.1.1.48 {ECO:0000256|ARBA:ARBA00012362}; DE EC=4.1.3.27 {ECO:0000256|ARBA:ARBA00012266}; GN Name=K7_TRP3 {ECO:0000313|EMBL:GAA24526.1}; GN ORFNames=SYK7_041151 {ECO:0000313|EMBL:GAA24526.1}; OS Saccharomyces cerevisiae (strain Kyokai no. 7 / NBRC 101557) (Baker's OS yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=721032 {ECO:0000313|EMBL:GAA24526.1, ECO:0000313|Proteomes:UP000001608}; RN [1] {ECO:0000313|EMBL:GAA24526.1, ECO:0000313|Proteomes:UP000001608} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Kyokai no. 7 / NBRC 101557 {ECO:0000313|Proteomes:UP000001608}; RX PubMed=21900213; DOI=10.1093/dnares/dsr029; RA Akao T., Yashiro I., Hosoyama A., Kitagaki H., Horikawa H., Watanabe D., RA Akada R., Ando Y., Harashima S., Inoue T., Inoue Y., Kajiwara S., RA Kitamoto K., Kitamoto N., Kobayashi O., Kuhara S., Masubuchi T., RA Mizoguchi H., Nakao Y., Nakazato A., Namise M., Oba T., Ogata T., Ohta A., RA Sato M., Shibasaki S., Takatsume Y., Tanimoto S., Tsuboi H., Nishimura A., RA Yoda K., Ishikawa T., Iwashita K., Fujita N., Shimoi H.; RT "Whole-genome sequencing of sake yeast Saccharomyces cerevisiae Kyokai no. RT 7."; RL DNA Res. 18:423-434(2011). CC -!- CATALYTIC ACTIVITY: CC Reaction=1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate + H(+) CC = (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O; CC Xref=Rhea:RHEA:23476, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16526, ChEBI:CHEBI:58613, ChEBI:CHEBI:58866; EC=4.1.1.48; CC Evidence={ECO:0000256|ARBA:ARBA00001633}; CC -!- CATALYTIC ACTIVITY: CC Reaction=chorismate + L-glutamine = anthranilate + H(+) + L-glutamate + CC pyruvate; Xref=Rhea:RHEA:21732, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16567, ChEBI:CHEBI:29748, ChEBI:CHEBI:29985, CC ChEBI:CHEBI:58359; EC=4.1.3.27; CC Evidence={ECO:0000256|ARBA:ARBA00000329}; CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L- CC tryptophan from chorismate: step 1/5. {ECO:0000256|ARBA:ARBA00004873}. CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L- CC tryptophan from chorismate: step 4/5. {ECO:0000256|ARBA:ARBA00004696}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; DG000047; GAA24526.1; -; Genomic_DNA. DR AlphaFoldDB; G2WHI3; -. DR SMR; G2WHI3; -. DR HOGENOM; CLU_039523_0_0_1; -. DR UniPathway; UPA00035; UER00040. DR Proteomes; UP000001608; Chromosome XI. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0046820; F:4-amino-4-deoxychorismate synthase activity; IEA:TreeGrafter. DR GO; GO:0004049; F:anthranilate synthase activity; IEA:UniProtKB-EC. DR GO; GO:0004425; F:indole-3-glycerol-phosphate synthase activity; IEA:UniProtKB-EC. DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule. DR GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:TreeGrafter. DR GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-UniPathway. DR CDD; cd01743; GATase1_Anthranilate_Synthase; 1. DR CDD; cd00331; IGPS; 1. DR Gene3D; 3.40.50.880; -; 1. DR Gene3D; 3.20.20.70; Aldolase class I; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR029062; Class_I_gatase-like. DR InterPro; IPR017926; GATASE. DR InterPro; IPR013798; Indole-3-glycerol_P_synth_dom. DR InterPro; IPR001468; Indole-3-GlycerolPSynthase_CS. DR InterPro; IPR011060; RibuloseP-bd_barrel. DR InterPro; IPR006221; TrpG/PapA_dom. DR NCBIfam; TIGR00566; trpG_papA; 1. DR PANTHER; PTHR43418:SF4; MULTIFUNCTIONAL TRYPTOPHAN BIOSYNTHESIS PROTEIN; 1. DR PANTHER; PTHR43418; MULTIFUNCTIONAL TRYPTOPHAN BIOSYNTHESIS PROTEIN-RELATED; 1. DR Pfam; PF00117; GATase; 1. DR Pfam; PF00218; IGPS; 1. DR PRINTS; PR00097; ANTSNTHASEII. DR PRINTS; PR00099; CPSGATASE. DR PRINTS; PR00096; GATASE. DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1. DR SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1. DR PROSITE; PS51273; GATASE_TYPE_1; 1. DR PROSITE; PS00614; IGPS; 1. PE 4: Predicted; KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605}; KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141}; KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962, KW ECO:0000256|PROSITE-ProRule:PRU00605}; KW Lyase {ECO:0000256|ARBA:ARBA00023239}; KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268}; KW Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822}. FT DOMAIN 15..197 FT /note="Glutamine amidotransferase" FT /evidence="ECO:0000259|Pfam:PF00117" FT DOMAIN 217..482 FT /note="Indole-3-glycerol phosphate synthase" FT /evidence="ECO:0000259|Pfam:PF00218" FT ACT_SITE 92 FT /note="Nucleophile" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605" FT ACT_SITE 181 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605" FT ACT_SITE 183 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605" SQ SEQUENCE 484 AA; 53489 MW; 34EF65E829279C1F CRC64; MSVHAATNPI NKHVVLIDNY DSFTWNVYEY LCQEGAKVSV YRNDAITVPE IAALNPDTLL ISPGPGHPKT DSGISRDCIR YFTGKIPVFG ICMGQQCMFD VFGGEVAYAG EIVHGKTSPI SHDNCGIFKN VPQGIAVTRY HSLAGTESSL PSCLKVTAST ENGIIMGVRH KKYTVEGVQF HPESILTEEG HLMIRNILNV SGGTWEENKS SPSNSILDRI YARRKIDVNE QSKIPGFTFQ DLQSNYDLGL APPLQDFYTV LSSSHKRAVV LAEVKRASPS KGPICLKAVA AEQALKYAEA GASAISVLTE PHWFHGSLQD LVNVRKILDL KFPPKERPCV LRKEFIFSKY QILEARLAGA DTVLLIVKML SQPLLKELYS YSKDLNMEPL VEVNSKEELQ RALEIGAKVV GVNNRDLHSF NVDLNTTSNL VESIPKDVLL IALSGITTRD DAEKYKKEGV HGFLVGEALM KSTDVKKFIH ELCE //