GUAA_HELPG
ID GUAA_HELPG Reviewed; 508 AA.
AC B5Z842;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 75.
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=HPG27_988;
OS Helicobacter pylori (strain G27).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=563041;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G27;
RX PubMed=18952803; DOI=10.1128/jb.01416-08;
RA Baltrus D.A., Amieva M.R., Covacci A., Lowe T.M., Merrell D.S.,
RA Ottemann K.M., Stein M., Salama N.R., Guillemin K.;
RT "The complete genome sequence of Helicobacter pylori strain G27.";
RL J. Bacteriol. 191:447-448(2009).
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; CP001173; ACI27741.1; -; Genomic_DNA.
DR RefSeq; WP_000604708.1; NC_011333.1.
DR AlphaFoldDB; B5Z842; -.
DR SMR; B5Z842; -.
DR EnsemblBacteria; ACI27741; ACI27741; HPG27_988.
DR KEGG; hpg:HPG27_988; -.
DR HOGENOM; CLU_014340_0_5_7; -.
DR OMA; KRKIIGH; -.
DR OrthoDB; 504464at2; -.
DR UniPathway; UPA00189; UER00296.
DR Proteomes; UP000001735; 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_1000120317"
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; 56606 MW; 83286B332EC9405F CRC64;
MILVLDFGSQ YTQLIARRLR ESGIYTEIVP FFESIENIQK KAPKGLILSG GPASVYAKDA
YKPSGKIFDL NVPILGICYG MQYLVDFFGG VVVGANEQEF GKAVLEIAQN SVIFEGVKIK
SLVWMSHMDK VIELPKGFTT LAKSPNSPHC AIENGKIFGL QFHPEVVQSE EGGKILENFA
LLVCGCEKTW GMQHFAQREI ARLKEKIANA KVLCAVSGGV DSTVVATLLH RAIKDNLIAV
FVDHGLLRKN EKERVQAMFK DLQIPLNTID AKGIFLSKLK GVSEPELKRK IIGETFIEVF
EKEAKKHHLK GKIEFLAQGT LYPDVIESVS VKGPSKVIKT HHNVGGLPEW MDFKLIEPLR
ELFKDEARLL GKELGVSQDF LMHHPFPGPG LAVRILGEVS ESKIKRLQEA DFIFIEELKK
ANLYDKVWQA FCVLLNVNSV GVMGDNRTYE NAICLRAVNA SDGMTASFSF LEHSFLEKVS
NRITNEVSGI NRVVYDITSK PPGTIEWE
