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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
 
 
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