ID   TRPG_LEPBI              Reviewed;         201 AA.
AC   P20441;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Anthranilate synthase component 2;
DE            Short=AS;
DE            Short=ASII;
DE            EC=4.1.3.27;
DE   AltName: Full=Anthranilate synthase, GATase component;
DE   AltName: Full=Anthranilate synthase, glutamine amidotransferase component;
GN   Name=trpG;
OS   Leptospira biflexa.
OC   Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX   NCBI_TaxID=172;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Serovar Patoc;
RX   PubMed=2703466; DOI=10.1128/jb.171.4.2083-2089.1989;
RA   Yelton D.B., Peng S.L.;
RT   "Identification and nucleotide sequence of the Leptospira biflexa serovar
RT   patoc trpE and trpG genes.";
RL   J. Bacteriol. 171:2083-2089(1989).
CC   -!- FUNCTION: Part of a heterotetrameric complex that catalyzes the two-
CC       step biosynthesis of anthranilate, an intermediate in the biosynthesis
CC       of L-tryptophan. In the first step, the glutamine-binding beta subunit
CC       (TrpG) of anthranilate synthase (AS) provides the glutamine
CC       amidotransferase activity which generates ammonia as a substrate that,
CC       along with chorismate, is used in the second step, catalyzed by the
CC       large alpha subunit of AS (TrpE) to produce anthranilate. In the
CC       absence of TrpG, TrpE can synthesize anthranilate directly from
CC       chorismate and high concentrations of ammonia (By similarity).
CC       {ECO:0000250}.
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   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 1/5.
CC   -!- SUBUNIT: Heterotetramer consisting of two non-identical subunits: a
CC       beta subunit (TrpG) and a large alpha subunit (TrpE). {ECO:0000250}.
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DR   EMBL; M22468; AAA88217.1; -; Genomic_DNA.
DR   PIR; C32840; C32840.
DR   AlphaFoldDB; P20441; -.
DR   SMR; P20441; -.
DR   MEROPS; C26.959; -.
DR   UniPathway; UPA00035; UER00040.
DR   GO; GO:0004049; F:anthranilate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd01743; GATase1_Anthranilate_Synthase; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR017926; GATASE.
DR   InterPro; IPR006221; TrpG/PapA_dom.
DR   Pfam; PF00117; GATase; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
DR   TIGRFAMs; TIGR00566; trpG_papA; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW   Glutamine amidotransferase; Lyase; Tryptophan biosynthesis.
FT   CHAIN           1..201
FT                   /note="Anthranilate synthase component 2"
FT                   /id="PRO_0000056887"
FT   DOMAIN          2..201
FT                   /note="Glutamine amidotransferase type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        89
FT                   /note="Nucleophile; for GATase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        182
FT                   /note="For GATase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        184
FT                   /note="For GATase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT   BINDING         59..61
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000250|UniProtKB:P00900"
FT   BINDING         93
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000250|UniProtKB:P00900"
FT   BINDING         139..140
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000250|UniProtKB:P00900"
SQ   SEQUENCE   201 AA;  22158 MW;  A662F2AE9B519095 CRC64;
     MKVLILDNYD SFTFNLYQIV GEILEEREKP FQLDVIRNDE KPFEWIKSAN YDKIIISPGP
     GHPADPAYFG VSADILKELG KTPPVLGICL GMQGMATVFG GEVVRANIAM HGKLSPIEHD
     GKGVFSGLTQ GIEIMRYHSL VAKEISLPND LEITARVSAG EGKGEIMGLR HKSLKIEGVQ
     FHPESFGSEE GKCLLRNFIN S