GUAA_HELPY
ID GUAA_HELPY Reviewed; 508 AA.
AC O25165;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=GMP synthase [glutamine-hydrolyzing];
DE EC=6.3.5.2;
DE AltName: Full=GMP synthetase;
DE AltName: Full=Glutamine amidotransferase;
GN Name=guaA; OrderedLocusNames=HP_0409;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
CC -!- FUNCTION: Catalyzes the synthesis of GMP from XMP. {ECO:0000250}.
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 -!- PATHWAY: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln
CC route): step 1/1.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
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DR EMBL; AE000511; AAD07477.1; -; Genomic_DNA.
DR PIR; A64571; A64571.
DR RefSeq; NP_207207.1; NC_000915.1.
DR RefSeq; WP_000604593.1; NC_018939.1.
DR AlphaFoldDB; O25165; -.
DR SMR; O25165; -.
DR DIP; DIP-3393N; -.
DR IntAct; O25165; 1.
DR MINT; O25165; -.
DR STRING; 85962.C694_02085; -.
DR MEROPS; C26.957; -.
DR PaxDb; O25165; -.
DR EnsemblBacteria; AAD07477; AAD07477; HP_0409.
DR KEGG; hpy:HP_0409; -.
DR PATRIC; fig|85962.47.peg.434; -.
DR eggNOG; COG0518; Bacteria.
DR eggNOG; COG0519; Bacteria.
DR OMA; KRKIIGH; -.
DR PhylomeDB; O25165; -.
DR UniPathway; UPA00189; UER00296.
DR Proteomes; UP000000429; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003921; F:GMP synthase activity; IBA:GO_Central.
DR GO; GO:0016462; F:pyrophosphatase activity; IEA:InterPro.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006177; P:GMP biosynthetic process; IBA:GO_Central.
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; Reference proteome.
FT CHAIN 1..508
FT /note="GMP synthase [glutamine-hydrolyzing]"
FT /id="PRO_0000140133"
FT DOMAIN 1..189
FT /note="Glutamine amidotransferase type-1"
FT DOMAIN 190..383
FT /note="GMPS ATP-PPase"
FT ACT_SITE 78
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 163
FT /evidence="ECO:0000250"
FT ACT_SITE 165
FT /evidence="ECO:0000250"
FT BINDING 217..223
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 508 AA; 56824 MW; 19F1FC3CA4331B3F CRC64;
MILVLDFGSQ YTQLIARRLR ERGIYTEIVP FFESIENIQK KAPKGLILSG GPASVYAKDA
YKPSGKIFDL NVPILGICYG MQYLVDFFGG VVVGANEQEF GKAVLEITQN SVIFEGVKIK
SLVWMSHMDK VIELPKGFTT LAKSPNSPHC AIENGKIFGL QFHPEVVQSE EGGKILENFA
LLVCGCEKTW GMQHFAQREI ARLKEKIANA KVLCAVSGGV DSTVVATLLH RAIKDNLIAV
FVDHGLLRKN EKERVQAMFK DLKIPLNTID AKEVFLSKLK GVSEPELKRK IIGETFIEVF
EKEAKKHHLK GKIEFLAQGT LYPDVIESVS VKGPSKVIKT HHNVGGLPEW MDFKLIEPLR
ELFKDEVRLL GKELGVSQDF LMRHPFPGPG LAVRILGEIS ESKIKRLQEA DFIFIEELKK
ANLYDKVWQA FCVLLNVNSV GVMGDNRTYE NAICLRAVNA SDGMTASFSF LEHSFLEKVS
NRITNEVSGI NRVVYDITSK PPGTIEWE
