ID   TRPG_BUCAP              Reviewed;         196 AA.
AC   P42388;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 106.
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; OrderedLocusNames=BUsg_PT2;
OS   Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OG   Plasmid pBSc.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=198804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sg;
RX   PubMed=8170994; DOI=10.1073/pnas.91.9.3819;
RA   Lai C.-Y., Baumann L., Baumann P.;
RT   "Amplification of trpEG: adaptation of Buchnera aphidicola to an
RT   endosymbiotic association with aphids.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:3819-3823(1994).
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; Z21938; CAA79932.1; -; Genomic_DNA.
DR   PIR; I40053; I40053.
DR   AlphaFoldDB; P42388; -.
DR   SMR; P42388; -.
DR   MEROPS; C26.960; -.
DR   PRIDE; P42388; -.
DR   OMA; HQVVIYR; -.
DR   UniPathway; UPA00035; UER00040.
DR   Proteomes; UP000000416; Plasmid pBsc.
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; Plasmid; Tryptophan biosynthesis.
FT   CHAIN           1..196
FT                   /note="Anthranilate synthase component 2"
FT                   /id="PRO_0000056873"
FT   DOMAIN          3..196
FT                   /note="Glutamine amidotransferase type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        84
FT                   /note="Nucleophile; for GATase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        170
FT                   /note="For GATase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        172
FT                   /note="For GATase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT   BINDING         57..59
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000250|UniProtKB:P00900"
FT   BINDING         88
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000250|UniProtKB:P00900"
FT   BINDING         134..135
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000250|UniProtKB:P00900"
SQ   SEQUENCE   196 AA;  21867 MW;  2FB23F9DAB441F3E CRC64;
     MANILLLDNF DSFTYNLVEQ LRNKNSNVLI YRNTVDINTI LNSIKKIRNP ILMLSPGPST
     PKNAGCMLNL IKKVKGEIPI VGICLGHQAI VEAYGGIIGY AGEIFHGKAS LINHDGLEMF
     EGLPQPLPVA RYHSLICNKI PKNFIINSYF NDMIMSVRNN LDYVCGFQFH PESILTTSGA
     LLLEKIINWA SLKYKG