ID   TRPG1_HALMA             Reviewed;         207 AA.
AC   Q5V214;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Anthranilate synthase component II;
DE            EC=4.1.3.27;
GN   Name=trpG1; OrderedLocusNames=rrnAC1517;
OS   Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS   B-1809) (Halobacterium marismortui).
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; AY596297; AAV46438.1; -; Genomic_DNA.
DR   RefSeq; WP_011223671.1; NZ_CP039138.1.
DR   AlphaFoldDB; Q5V214; -.
DR   SMR; Q5V214; -.
DR   STRING; 272569.rrnAC1517; -.
DR   MEROPS; C26.959; -.
DR   EnsemblBacteria; AAV46438; AAV46438; rrnAC1517.
DR   GeneID; 40152479; -.
DR   KEGG; hma:rrnAC1517; -.
DR   PATRIC; fig|272569.17.peg.2206; -.
DR   eggNOG; arCOG00086; Archaea.
DR   HOGENOM; CLU_014340_1_2_2; -.
DR   OMA; HQVVIYR; -.
DR   UniPathway; UPA00035; UER00040.
DR   Proteomes; UP000001169; Chromosome I.
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; Reference proteome;
KW   Tryptophan biosynthesis.
FT   CHAIN           1..207
FT                   /note="Anthranilate synthase component II"
FT                   /id="PRO_0000056880"
FT   DOMAIN          17..207
FT                   /note="Glutamine amidotransferase type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        96
FT                   /note="Nucleophile; for GATase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        187
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        189
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT   BINDING         66..68
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000250|UniProtKB:P00900"
FT   BINDING         146..147
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000250|UniProtKB:P00900"
SQ   SEQUENCE   207 AA;  22292 MW;  C9DBC7C50BD983B7 CRC64;
     MSTAQPAGAD AVRDDLRVLF VDNFDSFTYN LVEYVSEHAE TEVVRNTASL DDVEAFDPDA
     IILSPGPGHP KNERDVGVTL DVLREVSPDV PTLGVCLGLE SAVYAYGGTI GRAPEPIHGK
     AFPIDHDGKG VFAGLEQGFQ GGRYHSLIAD DVPEEFVVSA TTETEDGTEL VMGVRHREHP
     IEAVQFHPES VLTAVGHDVI RNFLAGL