ID GUAA_SALAR Reviewed; 525 AA. AC A9MHM5; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 05-FEB-2008, sequence version 1. DT 05-DEC-2018, entry version 77. DE RecName: Full=GMP synthase [glutamine-hydrolyzing] {ECO:0000255|HAMAP-Rule:MF_00344}; DE EC=6.3.5.2 {ECO:0000255|HAMAP-Rule:MF_00344}; DE AltName: Full=GMP synthetase {ECO:0000255|HAMAP-Rule:MF_00344}; DE AltName: Full=Glutamine amidotransferase {ECO:0000255|HAMAP-Rule:MF_00344}; GN Name=guaA {ECO:0000255|HAMAP-Rule:MF_00344}; GN OrderedLocusNames=SARI_00366; OS Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=41514; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-731 / CDC346-86 / RSK2980; RG The Salmonella enterica serovar Arizonae Genome Sequencing Project; RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S., RA Fulton R., Chunyan W., Wollam A., Shah N., Pepin K., Bhonagiri V., RA Nash W., Johnson M., Thiruvilangam P., Wilson R.; RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the synthesis of GMP from XMP. CC {ECO:0000255|HAMAP-Rule:MF_00344}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O + L-glutamine + XMP = AMP + diphosphate + GMP + CC 2 H(+) + L-glutamate; Xref=Rhea:RHEA:11680, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57464, ChEBI:CHEBI:58115, CC ChEBI:CHEBI:58359, ChEBI:CHEBI:456215; EC=6.3.5.2; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00344}; CC -!- PATHWAY: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln CC route): step 1/1. {ECO:0000255|HAMAP-Rule:MF_00344}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00344}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000880; ABX20303.1; -; Genomic_DNA. DR RefSeq; WP_000131513.1; NC_010067.1. DR ProteinModelPortal; A9MHM5; -. DR SMR; A9MHM5; -. DR STRING; 882884.SARI_00366; -. DR EnsemblBacteria; ABX20303; ABX20303; SARI_00366. DR KEGG; ses:SARI_00366; -. DR eggNOG; ENOG4105CM0; Bacteria. DR eggNOG; COG0518; LUCA. DR eggNOG; COG0519; LUCA. DR HOGENOM; HOG000223964; -. DR KO; K01951; -. DR OMA; KRKIIGH; -. DR OrthoDB; POG091H00MK; -. DR UniPathway; UPA00189; UER00296. DR Proteomes; UP000002084; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0003922; F:GMP synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-UniRule. DR GO; GO:0016462; F:pyrophosphatase activity; IEA:InterPro. DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW. DR GO; GO:0006177; P:GMP biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd01742; GATase1_GMP_Synthase; 1. DR CDD; cd01997; GMP_synthase_C; 1. DR Gene3D; 3.40.50.620; -; 1. DR Gene3D; 3.40.50.880; -; 1. DR HAMAP; MF_00344; GMP_synthase; 1. DR InterPro; IPR029062; Class_I_gatase-like. DR InterPro; IPR017926; GATASE. DR InterPro; IPR001674; GMP_synth_C. DR InterPro; IPR004739; GMP_synth_GATase. DR InterPro; IPR022955; GMP_synthase. DR InterPro; IPR025777; GMPS_ATP_PPase_dom. DR InterPro; IPR022310; NAD/GMP_synthase. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR Pfam; PF00117; GATase; 1. DR Pfam; PF00958; GMP_synt_C; 1. DR Pfam; PF02540; NAD_synthase; 1. DR SUPFAM; SSF52317; SSF52317; 1. DR TIGRFAMs; TIGR00884; guaA_Cterm; 1. DR TIGRFAMs; TIGR00888; guaA_Nterm; 1. DR PROSITE; PS51273; GATASE_TYPE_1; 1. DR PROSITE; PS51553; GMPS_ATP_PPASE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Glutamine amidotransferase; KW GMP biosynthesis; Ligase; Nucleotide-binding; Purine biosynthesis; KW Reference proteome. FT CHAIN 1 525 GMP synthase [glutamine-hydrolyzing]. FT /FTId=PRO_1000120387. FT DOMAIN 9 207 Glutamine amidotransferase type-1. FT {ECO:0000255|HAMAP-Rule:MF_00344}. FT DOMAIN 208 400 GMPS ATP-PPase. {ECO:0000255|HAMAP- FT Rule:MF_00344}. FT NP_BIND 235 241 ATP. {ECO:0000255|HAMAP-Rule:MF_00344}. FT ACT_SITE 86 86 Nucleophile. {ECO:0000255|HAMAP- FT Rule:MF_00344}. FT ACT_SITE 181 181 {ECO:0000255|HAMAP-Rule:MF_00344}. FT ACT_SITE 183 183 {ECO:0000255|HAMAP-Rule:MF_00344}. SQ SEQUENCE 525 AA; 58642 MW; B757F7DB6C8685F9 CRC64; MTDNIHKHRI LILDFGSQYT QLVARRVREL GVYCELWAWD VTEAQIREFN PSGIILSGGP ESTTEENSPR APQYVFEAGV PVFGVCYGMQ TMAMQLGGHV EGSNEREFGY AQVEVLTDSA LIRGIEDSLT ADGKPLLDVW MSHGDKVTAI PSDFVTVAST ESCPFAIMAN EEKRFYGVQF HPEVTHTRQG MRMLERFVRD ICQCEALWTP AKIIDDAVAR IREQVGDDKV ILGLSGGVDS SVTAMLLHRA IGKNLTCVFV DNGLLRLNEA EQVMDMFGDH FGLNIVHVPA EDRFLSALAG ENDPEAKRKI IGRVFVEVFD EEALKLEDVK WLAQGTIYPD VIESAASATG KAHVIKSHHN VGGLPKEMKM GLVEPLKELF KDEVRKIGLE LGLPYDMLYR HPFPGPGLGV RVLGEVKKEY CDLLRRADAI FIEELRKADL YDKVSQAFTV FLPVRSVGVM GDGRKYDWVV SLRAVETIDF MTAHWAHLPY GFLGRVSNRI INEVNGISRV VYDISGKPPA TIEWE //