ID GUAA_CERS1 Reviewed; 518 AA. AC A3PK79; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 03-APR-2007, sequence version 1. DT 29-MAY-2024, entry version 96. 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=Rsph17029_1635; OS Cereibacter sphaeroides (strain ATCC 17029 / ATH 2.4.9) (Rhodobacter OS sphaeroides). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales; OC Paracoccaceae; Cereibacter. OX NCBI_TaxID=349101; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17029 / ATH 2.4.9; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., RA Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P., RA Mackenzie C., Choudhary M., Donohue T.J., Kaplan S.; RT "Complete sequence of chromosome 1 of Rhodobacter sphaeroides ATCC 17029."; RL Submitted (FEB-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; CP000577; ABN76745.1; -; Genomic_DNA. DR AlphaFoldDB; A3PK79; -. DR SMR; A3PK79; -. DR MEROPS; C26.957; -. DR KEGG; rsh:Rsph17029_1635; -. DR HOGENOM; CLU_014340_0_5_5; -. DR UniPathway; UPA00189; UER00296. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. 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; 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. FT CHAIN 1..518 FT /note="GMP synthase [glutamine-hydrolyzing]" FT /id="PRO_1000120383" FT DOMAIN 6..200 FT /note="Glutamine amidotransferase type-1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344" FT DOMAIN 201..393 FT /note="GMPS ATP-PPase" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344" FT ACT_SITE 84 FT /note="Nucleophile" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344" FT ACT_SITE 175 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344" FT ACT_SITE 177 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344" FT BINDING 228..234 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00344" SQ SEQUENCE 518 AA; 56985 MW; 2AC907AD076C11C1 CRC64; MTQHDRLLII DFGSQVTQLI ARRLRELNVY CEIHPYQNVT EAFLKGFAPK AVIFSGGPSS VFAEGAPMPP AGVFDLGVPI LGICYGQQVM MHCLGGKVER GHGTAEFGRA FVTPTAERLA ILDGWFEEGR EQVWMSHGDH VSQIAPGFQV FGTSPNAPFA ITGDPARHFY AVQFHPEVHH TPKGAKLYEN FVRLAGFKGD WTMGAYREEA IARIRAQVGD QKVICGLSGG VDSSVAAVLI HEAIGDQLTC VFVDHGLLRL GEAEQVVTMF RDHYNMPLIH ADESDLFLGA LEGVSDPEVK RKTIGRLFID VFQKHAADVG GATFLAQGTL YPDVIESVSF SGGPSVTIKS HHNVGGLPEK MGLKLVEPLR ELFKDEVRAL GRELGLPESF IGRHPFPGPG LAIRCPGEIT REKLEILRRA DAVYIDQIRR HGLYDEIWQA FVALLPVRTV GVMGDGRTYD YACALRAVTS VDGMTADYYP FTHDFLGETA TRIINEVQGI NRVTYDITSK PPGTIEWE //