ID   G2WHI3_YEASK            Unreviewed;       484 AA.
AC   G2WHI3;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   13-SEP-2023, entry version 43.
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}.
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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: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: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
//