ID   GUAA_STAAE              Reviewed;         513 AA.
AC   A6QE71;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 99.
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=NWMN_0381;
OS   Staphylococcus aureus (strain Newman).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=426430;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Newman;
RX   PubMed=17951380; DOI=10.1128/jb.01000-07;
RA   Baba T., Bae T., Schneewind O., Takeuchi F., Hiramatsu K.;
RT   "Genome sequence of Staphylococcus aureus strain Newman and comparative
RT   analysis of staphylococcal genomes: polymorphism and evolution of two major
RT   pathogenicity islands.";
RL   J. Bacteriol. 190:300-310(2008).
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}.
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DR   EMBL; AP009351; BAF66653.1; -; Genomic_DNA.
DR   RefSeq; WP_000424966.1; NZ_CP023390.1.
DR   AlphaFoldDB; A6QE71; -.
DR   SMR; A6QE71; -.
DR   MEROPS; C26.957; -.
DR   EnsemblBacteria; BAF66653; BAF66653; NWMN_0381.
DR   KEGG; sae:NWMN_0381; -.
DR   HOGENOM; CLU_014340_0_5_9; -.
DR   OMA; KRKIIGH; -.
DR   UniPathway; UPA00189; UER00296.
DR   Proteomes; UP000006386; 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   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; IPR014729; Rossmann-like_a/b/a_fold.
DR   Pfam; PF00117; GATase; 1.
DR   Pfam; PF00958; GMP_synt_C; 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; Glutamine amidotransferase; GMP biosynthesis; Ligase;
KW   Nucleotide-binding; Purine biosynthesis.
FT   CHAIN           1..513
FT                   /note="GMP synthase [glutamine-hydrolyzing]"
FT                   /id="PRO_1000120424"
FT   DOMAIN          9..198
FT                   /note="Glutamine amidotransferase type-1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT   DOMAIN          199..388
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        172
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT   ACT_SITE        174
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT   BINDING         226..232
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
SQ   SEQUENCE   513 AA;  58230 MW;  F7DD8E6C6BD32E7A CRC64;
     MEMAKEQELI LVLDFGSQYN QLITRRIREM GVYSELHDHE ISIEEIKKMN PKGIILSGGP
     NSVYEEGSFT IDPEIYNLGI PVLGICYGMQ LTTKLLGGKV ERANEREYGK AIINAKSDEL
     FAGLPAEQTV WMSHSDKVIE IPEGFEVIAD SPSTDYAAIE DKKRRIYGVQ FHPEVRHTEY
     GNDLLNNFVR RVCDCRGQWT MENFIEIEIE KIRQRVGDRR VLCAMSGGVD SSVVAVLLHK
     AIGDQLTCIF VDHGLLRKGE GDMVMEQFGE GFNMNIIRVN AKDRFMNKLK GVSDPEQKRK
     IIGNEFVYVF DDEASKLKGV DFLAQGTLYT DVIESGTKTA QTIKSHHNVG GLPEDMEFEL
     IEPINTLFKD EVRKLGIELG IPEHLVWRQP FPGPGLGIRV LGEITEDKLE IVRESDAILR
     QVIREEGLER EIWQYFTVLP NIQSVGVMGD YRTYDHTVGI RAVTSIDGMT SDFARIDWEV
     LQKISSRIVN EVDHVNRVVY DITSKPPSTI EWE