ID   GUAA_HELAH              Reviewed;         508 AA.
AC   Q17YH9;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 105.
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=Hac_0466;
OS   Helicobacter acinonychis (strain Sheeba).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=382638;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sheeba;
RX   PubMed=16789826; DOI=10.1371/journal.pgen.0020120;
RA   Eppinger M., Baar C., Linz B., Raddatz G., Lanz C., Keller H., Morelli G.,
RA   Gressmann H., Achtman M., Schuster S.C.;
RT   "Who ate whom? Adaptive Helicobacter genomic changes that accompanied a
RT   host jump from early humans to large felines.";
RL   PLoS Genet. 2:1097-1110(2006).
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; AM260522; CAJ99297.1; -; Genomic_DNA.
DR   RefSeq; WP_011577411.1; NC_008229.1.
DR   AlphaFoldDB; Q17YH9; -.
DR   SMR; Q17YH9; -.
DR   STRING; 382638.Hac_0466; -.
DR   MEROPS; C26.957; -.
DR   EnsemblBacteria; CAJ99297; CAJ99297; Hac_0466.
DR   KEGG; hac:Hac_0466; -.
DR   eggNOG; COG0518; Bacteria.
DR   eggNOG; COG0519; Bacteria.
DR   HOGENOM; CLU_014340_0_5_7; -.
DR   OMA; KRKIIGH; -.
DR   OrthoDB; 504464at2; -.
DR   BioCyc; HACI382638:HAC_RS02135-MON; -.
DR   UniPathway; UPA00189; UER00296.
DR   Proteomes; UP000000775; 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; 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; Glutamine amidotransferase; GMP biosynthesis; Ligase;
KW   Nucleotide-binding; Purine biosynthesis.
FT   CHAIN           1..508
FT                   /note="GMP synthase [glutamine-hydrolyzing]"
FT                   /id="PRO_1000120314"
FT   DOMAIN          1..189
FT                   /note="Glutamine amidotransferase type-1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT   DOMAIN          190..383
FT                   /note="GMPS ATP-PPase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT   ACT_SITE        78
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT   ACT_SITE        163
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT   ACT_SITE        165
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
FT   BINDING         217..223
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00344"
SQ   SEQUENCE   508 AA;  56512 MW;  13E5783FBCA5A05D CRC64;
     MIVVLDFGSQ YTQLIARRLR ESGIYAEIVP FFESTENIQK KAPKGLILSG GPASVYAKDA
     YTPSEKIFDL NLPILGICYG MQYLVDFFGG AVACANEQEF GKAALEIIQD SVIFKGVKAK
     SLVWMSHMDK VITLPKGFTT IAKSPNSLHC AIESGKVFGL QFHPEVIQSE EGGKILENFA
     LLVCGCEKTW GMQNFAQKEM TRLKEKISDA RVLCAVSGGV DSTVVATLLH RAIKDNLIAV
     FVDHGLLRKN EKEKVQAMFK DLQIPLNTID AKEIFLSKLK GVSEPELKRK IIGETFIEVF
     EKEAKKHHLK GKIEFLAQGT LYPDVIESVS VKGPSKVIKS HHNVGGLPEW MDFKLIEPLR
     ELFKDEVRLL GKELGVSQDF LMRHPFPGPG LAVRILGEVS ESKIKCLQEA DFIFIEELKK
     ANLYDKVWQA FCVLLNAHSV GVMGDNRTYE NAICLRAVDA SDGMTASFSH LGHSFLEKVS
     NRITNEVSGI NRVVYDITSK PPGTIEWE