ID F2KS85_ARCVS Unreviewed; 192 AA.
AC F2KS85;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=anthranilate synthase {ECO:0000256|ARBA:ARBA00012266};
DE EC=4.1.3.27 {ECO:0000256|ARBA:ARBA00012266};
GN OrderedLocusNames=Arcve_2033 {ECO:0000313|EMBL:AEA48024.1};
OS Archaeoglobus veneficus (strain DSM 11195 / SNP6).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=693661 {ECO:0000313|EMBL:AEA48024.1, ECO:0000313|Proteomes:UP000008136};
RN [1] {ECO:0000313|EMBL:AEA48024.1, ECO:0000313|Proteomes:UP000008136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SNP6;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Mikhailova N., Lu M.,
RA Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V.,
RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., Brambilla E.,
RA Klenk H.-P., Eisen J.A.;
RT "The complete genome of Archaeoglobus veneficus SNP6.";
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
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};
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DR EMBL; CP002588; AEA48024.1; -; Genomic_DNA.
DR RefSeq; WP_013684675.1; NC_015320.1.
DR AlphaFoldDB; F2KS85; -.
DR STRING; 693661.Arcve_2033; -.
DR MEROPS; C26.959; -.
DR GeneID; 10395166; -.
DR KEGG; ave:Arcve_2033; -.
DR eggNOG; arCOG00086; Archaea.
DR HOGENOM; CLU_014340_1_2_2; -.
DR OrthoDB; 3321at2157; -.
DR Proteomes; UP000008136; Chromosome.
DR GO; GO:0004049; F:anthranilate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
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; 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,
KW ECO:0000313|EMBL:AEA48024.1}; Lyase {ECO:0000313|EMBL:AEA48024.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008136};
KW Transferase {ECO:0000313|EMBL:AEA48024.1}.
FT DOMAIN 3..173
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT ACT_SITE 78
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 164
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 166
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 192 AA; 21099 MW; 3AC0A612AC77EDFE CRC64;
MILLIDNRDS FVWNLAEYAS IFDRVKVVPN TVSVDEVKRI DPDGIIISPG PGSPENRRDI
GNCPEIVEEV DVPTLGVCLG HQLIAHVFGG KVGRVKPVHG KASIVKHDGK TIFEGVRNPL
KAGRYHSLAV LEVPKGFELS AISDDGIVMG IRHKSRQIEG VQFHPESVLT EFESGDGLRI
VKNFVDMCRG RL
//
