ID A0A0A0EWZ8_9GAMM Unreviewed; 245 AA.
AC A0A0A0EWZ8;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Glutamine amidotransferase {ECO:0000313|EMBL:KGM53682.1};
DE EC=6.3.5.2 {ECO:0000313|EMBL:KGM53682.1};
GN ORFNames=N799_11240 {ECO:0000313|EMBL:KGM53682.1};
OS Lysobacter arseniciresistens ZS79.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=913325 {ECO:0000313|EMBL:KGM53682.1, ECO:0000313|Proteomes:UP000029989};
RN [1] {ECO:0000313|EMBL:KGM53682.1, ECO:0000313|Proteomes:UP000029989}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZS79 {ECO:0000313|EMBL:KGM53682.1,
RC ECO:0000313|Proteomes:UP000029989};
RX PubMed=26516404; DOI=10.1186/s40793-015-0070-5;
RA Liu L., Zhang S., Luo M., Wang G.;
RT "Genomic information of the arsenic-resistant bacterium Lysobacter
RT arseniciresistens type strain ZS79(T) and comparison of Lysobacter draft
RT genomes.";
RL Stand. Genomic Sci. 10:88-88(2015).
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:KGM53682.1}.
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DR EMBL; AVPT01000036; KGM53682.1; -; Genomic_DNA.
DR RefSeq; WP_036213212.1; NZ_AVPT01000036.1.
DR AlphaFoldDB; A0A0A0EWZ8; -.
DR STRING; 913325.N799_11240; -.
DR eggNOG; COG0518; Bacteria.
DR OrthoDB; 9813383at2; -.
DR Proteomes; UP000029989; Unassembled WGS sequence.
DR GO; GO:0003922; F:GMP synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-EC.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd01741; GATase1_1; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR InterPro; IPR044992; ChyE-like.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR017926; GATASE.
DR PANTHER; PTHR42695; GLUTAMINE AMIDOTRANSFERASE YLR126C-RELATED; 1.
DR PANTHER; PTHR42695:SF5; GLUTAMINE AMIDOTRANSFERASE YLR126C-RELATED; 1.
DR Pfam; PF00117; GATase; 1.
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:KGM53682.1}; Ligase {ECO:0000313|EMBL:KGM53682.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000029989};
KW Transferase {ECO:0000313|EMBL:KGM53682.1}.
FT DOMAIN 58..199
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT ACT_SITE 99
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 189
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 191
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 245 AA; 25889 MW; 17E84A343136F1E0 CRC64;
MTAPVTAPFL IIETGKPVGP MQRHGDFPHW IRVAGGLSRD AAVVVDVQGG EPLPVREGFA
GVIVTGSGAM VTERLDWSEA TAAWLRDAAH AGLPLLGICY GHQLLAHALG GEVGNNPAGR
EMGTVEVELL PAAADDALLA PLPPRFAAQL THMQSVLRVP DGAVVLARSA GDPCQAFRWG
VAAWGVQFHP EFSATHMRGY IRARKVALQR EGLDPAAMLA AVGAAPEARR VLRRFVHHAR
GPARG
//
