ID   TRPG2_HALMA             Reviewed;         190 AA.
AC   Q5V632;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Anthranilate synthase component II;
DE            EC=4.1.3.27;
GN   Name=trpG2; OrderedLocusNames=pNG7325;
OS   Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS   B-1809) (Halobacterium marismortui).
OG   Plasmid pNG700.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Haloarcula.
OX   NCBI_TaxID=272569;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX   PubMed=15520287; DOI=10.1101/gr.2700304;
RA   Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA   Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA   Hood L., Ng W.V.;
RT   "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT   Dead Sea.";
RL   Genome Res. 14:2221-2234(2004).
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: Tetramer of two components I and two components II.
CC       {ECO:0000250}.
CC   -!- MISCELLANEOUS: Component I catalyzes the formation of anthranilate
CC       using ammonia rather than glutamine, whereas component II provides
CC       glutamine amidotransferase activity.
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DR   EMBL; AY596296; AAV45020.1; -; Genomic_DNA.
DR   RefSeq; WP_007190565.1; NZ_CP039137.1.
DR   AlphaFoldDB; Q5V632; -.
DR   SMR; Q5V632; -.
DR   EnsemblBacteria; AAV45020; AAV45020; pNG7325.
DR   GeneID; 40151224; -.
DR   KEGG; hma:pNG7325; -.
DR   PATRIC; fig|272569.17.peg.752; -.
DR   HOGENOM; CLU_014340_1_2_2; -.
DR   OMA; FNIGLYH; -.
DR   UniPathway; UPA00035; UER00040.
DR   Proteomes; UP000001169; Plasmid pNG700.
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; Reference proteome;
KW   Tryptophan biosynthesis.
FT   CHAIN           1..190
FT                   /note="Anthranilate synthase component II"
FT                   /id="PRO_0000056881"
FT   DOMAIN          1..190
FT                   /note="Glutamine amidotransferase type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        76
FT                   /note="Nucleophile; for GATase activity"
FT                   /evidence="ECO:0000250|UniProtKB:P00900"
FT   ACT_SITE        167
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        169
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT   BINDING         51..53
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000250|UniProtKB:P00900"
FT   BINDING         80
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000250|UniProtKB:P00900"
FT   BINDING         126..127
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000250|UniProtKB:P00900"
SQ   SEQUENCE   190 AA;  20308 MW;  6752B48DD811FFD8 CRC64;
     MILIIDNYDS FAYNLVQYVG EFDDVTVRRN DAIDVEGIHE LDPDGIVVSP GPGTPAEAGV
     SIDVFAETEY PALGVCLGHQ ALCAAHGTPV GHAPSVVHGK PSEVRHDGTR LYDGVDDPFE
     VGRYHSLAVK ASELPDTLSE TAHTNDEQGI VMGVQHAEKP HIGVQFHPES ILTDAGKQIV
     ENFCTGIAKA