ID M0IZ72_HALVA Unreviewed; 207 AA.
AC M0IZ72;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-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=C437_16866 {ECO:0000313|EMBL:EMA01388.1};
OS Haloarcula vallismortis ATCC 29715.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Haloarcula.
OX NCBI_TaxID=662477 {ECO:0000313|EMBL:EMA01388.1, ECO:0000313|Proteomes:UP000011534};
RN [1] {ECO:0000313|EMBL:EMA01388.1, ECO:0000313|Proteomes:UP000011534}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29715 {ECO:0000313|EMBL:EMA01388.1,
RC ECO:0000313|Proteomes:UP000011534};
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:EMA01388.1}.
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DR EMBL; AOLQ01000067; EMA01388.1; -; Genomic_DNA.
DR RefSeq; WP_004518139.1; NZ_AOLQ01000067.1.
DR AlphaFoldDB; M0IZ72; -.
DR PATRIC; fig|662477.6.peg.3298; -.
DR OrthoDB; 3321at2157; -.
DR Proteomes; UP000011534; Unassembled WGS sequence.
DR GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProt.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProt.
DR GO; GO:0044271; P:cellular nitrogen compound biosynthetic process; IEA:UniProt.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0018130; P:heterocycle biosynthetic process; IEA:UniProt.
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; NF041322; Anth_synII_Halo; 1.
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; 1.
DR PRINTS; PR00097; ANTSNTHASEII.
DR PRINTS; PR00099; CPSGATASE.
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 20..204
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT ACT_SITE 96
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 187
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 189
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 207 AA; 22448 MW; 2871BCBFD1E20B36 CRC64;
MSASQPAGED AVRDDLRVLF VDNFDSFTYN LVEYVSEHAE TEVVRNTATL DEVEAFDPDA
IILSPGPGHP KNERDVGVTL DVLREVSPDV PTLGVCLGLE SAVYAYGGTI GRAPEPIHGK
AFPIDHDEQG VFAGLEQGFQ GGRYHSLIAE EVPAEFVVSA TTETEDGTEL VMGVRHREYP
IEAVQFHPES VLTAVGHDVI RNFLSGL
//
