ID Q2S3X4_SALRD Unreviewed; 245 AA.
AC Q2S3X4;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE SubName: Full=GMP synthase {ECO:0000313|EMBL:ABC44677.1};
DE EC=6.3.5.2 {ECO:0000313|EMBL:ABC44677.1};
GN Name=guaA {ECO:0000313|EMBL:ABC44677.1};
GN OrderedLocusNames=SRU_0975 {ECO:0000313|EMBL:ABC44677.1};
OS Salinibacter ruber (strain DSM 13855 / M31).
OC Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Salinibacteraceae;
OC Salinibacter.
OX NCBI_TaxID=309807 {ECO:0000313|EMBL:ABC44677.1, ECO:0000313|Proteomes:UP000008674};
RN [1] {ECO:0000313|EMBL:ABC44677.1, ECO:0000313|Proteomes:UP000008674}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13855 / CECT 5946 / M31
RC {ECO:0000313|Proteomes:UP000008674};
RX PubMed=16330755; DOI=10.1073/pnas.0509073102;
RA Mongodin E.F., Nelson K.E., Daugherty S., Deboy R.T., Wister J., Khouri H.,
RA Weidman J., Walsh D.A., Papke R.T., Sanchez Perez G., Sharma A.K.,
RA Nesbo C.L., MacLeod D., Bapteste E., Doolittle W.F., Charlebois R.L.,
RA Legault B., Rodriguez-Valera F.;
RT "The genome of Salinibacter ruber: convergence and gene exchange among
RT hyperhalophilic bacteria and archaea.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:18147-18152(2005).
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DR EMBL; CP000159; ABC44677.1; -; Genomic_DNA.
DR RefSeq; WP_011403735.1; NC_007677.1.
DR RefSeq; YP_445107.1; NC_007677.1.
DR AlphaFoldDB; Q2S3X4; -.
DR STRING; 309807.SRU_0975; -.
DR EnsemblBacteria; ABC44677; ABC44677; SRU_0975.
DR GeneID; 83727903; -.
DR KEGG; sru:SRU_0975; -.
DR PATRIC; fig|309807.25.peg.1011; -.
DR eggNOG; COG0518; Bacteria.
DR HOGENOM; CLU_054974_4_1_10; -.
DR OrthoDB; 9807137at2; -.
DR Proteomes; UP000008674; Chromosome.
DR GO; GO:0003922; F:GMP synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-EC.
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; PR00097; ANTSNTHASEII.
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 Ligase {ECO:0000313|EMBL:ABC44677.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008674}.
FT DOMAIN 55..193
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT REGION 33..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 98
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 181
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 183
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 245 AA; 26509 MW; 034477E3F04DA81B CRC64;
MHLALIDASL GTPHAQRNFE REVDASLTVY NANEGEMPPP IGEPAPVQTD GETPPSFDGA
IISGSQSSVY DSHRAWIQEL SRWVEGAISD GLPLLGVCWG HQLLAQILGG TVRGGSYELG
YIEVQQEADD PIWNGLPDPF TVFATHSDHV VTMPPDARLL ASNETGVQAL RYEQVYGVQF
HPEYDLKTAE AMIHSKDLSG RKIQRALDTC TDANVEAAGT ATRVFENFLD HVASAPETSS
SPLNA
//
