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Database: UniProt
Entry: M0KTH1_9EURY
LinkDB: M0KTH1_9EURY
Original site: M0KTH1_9EURY 
ID   M0KTH1_9EURY            Unreviewed;       237 AA.
AC   M0KTH1;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=anthranilate synthase {ECO:0000256|ARBA:ARBA00012266};
DE            EC=4.1.3.27 {ECO:0000256|ARBA:ARBA00012266};
GN   ORFNames=C442_08316 {ECO:0000313|EMBL:EMA23015.1};
OS   Haloarcula amylolytica JCM 13557.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Haloarcula.
OX   NCBI_TaxID=1227452 {ECO:0000313|EMBL:EMA23015.1, ECO:0000313|Proteomes:UP000011623};
RN   [1] {ECO:0000313|EMBL:EMA23015.1, ECO:0000313|Proteomes:UP000011623}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 13557 {ECO:0000313|EMBL:EMA23015.1,
RC   ECO:0000313|Proteomes:UP000011623};
RX   PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA   Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT   strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(2014).
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EMA23015.1}.
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DR   EMBL; AOLW01000015; EMA23015.1; -; Genomic_DNA.
DR   RefSeq; WP_008309418.1; NZ_AOLW01000015.1.
DR   AlphaFoldDB; M0KTH1; -.
DR   PATRIC; fig|1227452.3.peg.1662; -.
DR   Proteomes; UP000011623; Unassembled WGS sequence.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
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   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; 2.
DR   PRINTS; PR00097; ANTSNTHASEII.
DR   PRINTS; PR00096; GATASE.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
PE   4: Predicted;
KW   Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605}.
FT   DOMAIN          19..171
FT                   /note="Glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00117"
FT   DOMAIN          191..232
FT                   /note="Glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00117"
FT   REGION          172..193
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        172..191
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        100
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        214
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        216
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   237 AA;  25038 MW;  09757A79160E2613 CRC64;
     MSGAGTTTGD PDAPAPTVLV VDNYDSFAYN LVQYVGEVVI RLGGTEDDVV VRRNDAIDVE
     DIRELDPDGI VVSPGPGTPE EAGVSIPIFE ELEYPTLGVC LGHQALCAAN GAPVGHAEAV
     VHGKSSSVTH DGTGVFEDIP DPFEVGRYHS LAVDRENLPD VLIETAYTVN EDGSTNTAAT
     PDSSEPATAD GTDESQVVMG VRHSNRPHIG VQFHPESILT DHGKTMIENF CLLCNTT
//
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