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 24-JAN-2024, entry version 95. 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}; OrderedLocusNames=SARI_00366; OS Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980). OC Bacteria; Pseudomonadota; 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., Nash W., RA 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. {ECO:0000255|HAMAP- CC Rule:MF_00344}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O + L-glutamine + XMP = AMP + diphosphate + GMP + 2 CC 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 AlphaFoldDB; A9MHM5; -. DR SMR; A9MHM5; -. DR STRING; 41514.SARI_00366; -. DR MEROPS; C26.957; -. DR KEGG; ses:SARI_00366; -. DR HOGENOM; CLU_014340_0_5_6; -. DR OMA; DQLTCMF; -. DR UniPathway; UPA00189; UER00296. DR Proteomes; UP000002084; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0003921; F:GMP synthase activity; IEA:InterPro. DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW. DR CDD; cd01742; GATase1_GMP_Synthase; 1. DR CDD; cd01997; GMP_synthase_C; 1. DR Gene3D; 3.30.300.10; -; 1. DR Gene3D; 3.40.50.880; -; 1. DR Gene3D; 3.40.50.620; HUPs; 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 NCBIfam; TIGR00884; guaA_Cterm; 1. DR NCBIfam; TIGR00888; guaA_Nterm; 1. DR PANTHER; PTHR11922:SF2; GMP SYNTHASE [GLUTAMINE-HYDROLYZING]; 1. DR PANTHER; PTHR11922; GMP SYNTHASE-RELATED; 1. DR Pfam; PF00117; GATase; 1. DR Pfam; PF00958; GMP_synt_C; 1. DR Pfam; PF02540; NAD_synthase; 1. DR PRINTS; PR00097; ANTSNTHASEII. DR PRINTS; PR00099; CPSGATASE. DR PRINTS; PR00096; GATASE. DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1. DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1. DR SUPFAM; SSF54810; GMP synthetase C-terminal dimerisation domain; 1. DR PROSITE; PS51273; GATASE_TYPE_1; 1. DR PROSITE; PS51553; GMPS_ATP_PPASE; 1. PE 3: Inferred from homology; KW ATP-binding; Glutamine amidotransferase; GMP biosynthesis; Ligase; KW Nucleotide-binding; Purine biosynthesis; Reference proteome. FT CHAIN 1..525 FT /note="GMP synthase [glutamine-hydrolyzing]" FT /id="PRO_1000120387" FT DOMAIN 9..207 FT /note="Glutamine amidotransferase type-1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344" FT DOMAIN 208..400 FT /note="GMPS ATP-PPase" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344" FT ACT_SITE 86 FT /note="Nucleophile" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344" FT ACT_SITE 181 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344" FT ACT_SITE 183 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344" FT BINDING 235..241 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="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 //