ID F3Z2N9_DESAF Unreviewed; 193 AA.
AC F3Z2N9;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE SubName: Full=Glutamine amidotransferase of anthranilate synthase {ECO:0000313|EMBL:EGJ50206.1};
GN ORFNames=Desaf_1875 {ECO:0000313|EMBL:EGJ50206.1};
OS Desulfocurvibacter africanus subsp. africanus str. Walvis Bay.
OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC Desulfovibrionaceae; Desulfocurvibacter.
OX NCBI_TaxID=690850 {ECO:0000313|EMBL:EGJ50206.1, ECO:0000313|Proteomes:UP000007844};
RN [1] {ECO:0000313|EMBL:EGJ50206.1, ECO:0000313|Proteomes:UP000007844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Walvis Bay {ECO:0000313|EMBL:EGJ50206.1,
RC ECO:0000313|Proteomes:UP000007844};
RX PubMed=21642452; DOI=10.1128/JB.05223-11;
RA Brown S.D., Wall J.D., Kucken A.M., Gilmour C.C., Podar M., Brandt C.C.,
RA Teshima H., Detter J.C., Han C.S., Land M.L., Lucas S., Han J.,
RA Pennacchio L., Nolan M., Pitluck S., Woyke T., Goodwin L., Palumbo A.V.,
RA Elias D.A.;
RT "Genome sequence of the mercury-methylating and pleomorphic Desulfovibrio
RT africanus Strain Walvis Bay.";
RL J. Bacteriol. 193:4037-4038(2011).
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DR EMBL; CP003221; EGJ50206.1; -; Genomic_DNA.
DR RefSeq; WP_014259962.1; NC_016629.1.
DR AlphaFoldDB; F3Z2N9; -.
DR STRING; 690850.Desaf_1875; -.
DR MEROPS; C26.955; -.
DR KEGG; daf:Desaf_1875; -.
DR eggNOG; COG0512; Bacteria.
DR HOGENOM; CLU_014340_1_2_7; -.
DR Proteomes; UP000007844; Chromosome.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
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; 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:EGJ50206.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007844};
KW Transferase {ECO:0000313|EMBL:EGJ50206.1}.
FT DOMAIN 3..185
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT ACT_SITE 80
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 169
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 171
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 193 AA; 21287 MW; 99E94520CB5E98C2 CRC64;
MFLLIDNFDS FTFNLVQEFQ KQGRDPLVLR NDEERILDLA GSGELSMVCI SPGPSRPENA
GLCLEFLARL PKSVPVLGVC LGHQILGHFA GAPVEIAGRI MHGKTSMVEH DGRGLFTGLP
NPFEVCRYHS LLVMATPAHE NIEVTARTDQ GEVMGLRYRD RPWVGVQFHP ESILTPEGPK
LLANFPQAIL SEA
//