GUAA_HELPJ
ID GUAA_HELPJ Reviewed; 508 AA.
AC Q9ZKG4;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 140.
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=jhp_0972;
OS Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J99 / ATCC 700824;
RX PubMed=9923682; DOI=10.1038/16495;
RA Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT "Genomic sequence comparison of two unrelated isolates of the human gastric
RT pathogen Helicobacter pylori.";
RL Nature 397:176-180(1999).
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; AE001439; AAD06548.1; -; Genomic_DNA.
DR PIR; F71865; F71865.
DR RefSeq; WP_000604672.1; NZ_CP011330.1.
DR AlphaFoldDB; Q9ZKG4; -.
DR SMR; Q9ZKG4; -.
DR STRING; 85963.jhp_0972; -.
DR MEROPS; C26.957; -.
DR EnsemblBacteria; AAD06548; AAD06548; jhp_0972.
DR KEGG; hpj:jhp_0972; -.
DR PATRIC; fig|85963.30.peg.1619; -.
DR eggNOG; COG0518; Bacteria.
DR eggNOG; COG0519; Bacteria.
DR OMA; KRKIIGH; -.
DR UniPathway; UPA00189; UER00296.
DR Proteomes; UP000000804; 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_0000140134"
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; 56977 MW; D549FF5AFAA131D6 CRC64;
MILVLDFGSQ YTQLIARRLR ESGIYAEIVP FFESVENIQK KAPKGLILSG GPASVYAKDA
YKPSEKIFDL NLPILGICYG MQYLVDFFGG VVAYANEQEF GKAILEIVQN SVIFEGVKIK
SLVWMSHMDK VIELPKGFTT LAKSPNSPYC AIESDKIFGL QFHPEVIQSE EGGKILENFA
LLVCGCEKTW GMQHFAQREI VRLKEKIANA KVLCAVSGGV DSTVVATLLH RAIKDNLIAV
FVDHGLLRKN EKEKVQAMFK DLQIPLNTID AKEVFLSKLK GVSEPELKRK IIGETFIEVF
EKEAKKHHLK GKIEFLAQGT LYPDVIESVS VKGPSKVIKT HHNVGGLPEW MDFKLIEPLR
ELFKDEVRLL GKELGVSQDF LMRHPFPGPG LAIRILGEIN ENKIKRLQEA DAIFIEELKK
ANLYDKVWQA FCVLLNVNSV GVMGDNRTYE NAICLRAVNA SDGMTASFSF LEHSFLEKVS
NRITNEVNGI NRVVYDITSK PPGTIEWE