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GMM_SALTI
ID   GMM_SALTI               Reviewed;         157 AA.
AC   Q8Z5H2;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   27-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=GDP-mannose mannosyl hydrolase {ECO:0000255|HAMAP-Rule:MF_00941};
DE            Short=GDPMH {ECO:0000255|HAMAP-Rule:MF_00941};
DE            EC=3.6.1.- {ECO:0000255|HAMAP-Rule:MF_00941};
GN   Name=gmm {ECO:0000255|HAMAP-Rule:MF_00941}; Synonyms=nudD, wcaH;
GN   OrderedLocusNames=STY2319, t0764;
OS   Salmonella typhi.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT18;
RX   PubMed=11677608; DOI=10.1038/35101607;
RA   Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA   Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA   Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA   Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA   Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA   Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA   Barrell B.G.;
RT   "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT   serovar Typhi CT18.";
RL   Nature 413:848-852(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700931 / Ty2;
RX   PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA   Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA   Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT   "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT   CT18.";
RL   J. Bacteriol. 185:2330-2337(2003).
CC   -!- FUNCTION: Hydrolyzes GDP-mannose. {ECO:0000255|HAMAP-Rule:MF_00941}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GDP-alpha-D-mannose + H2O = D-mannose + GDP + H(+);
CC         Xref=Rhea:RHEA:28102, ChEBI:CHEBI:4208, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57527, ChEBI:CHEBI:58189;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00941};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00941};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00941};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00941}.
CC   -!- SIMILARITY: Belongs to the Nudix hydrolase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00941}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAO68457.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAD02470.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AL513382; CAD02470.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AE014613; AAO68457.1; ALT_INIT; Genomic_DNA.
DR   PIR; AH0768; AH0768.
DR   RefSeq; NP_456655.1; NC_003198.1.
DR   RefSeq; WP_001688181.1; NZ_WSUR01000002.1.
DR   AlphaFoldDB; Q8Z5H2; -.
DR   SMR; Q8Z5H2; -.
DR   STRING; 220341.16503336; -.
DR   EnsemblBacteria; AAO68457; AAO68457; t0764.
DR   KEGG; stt:t0764; -.
DR   KEGG; sty:STY2319; -.
DR   PATRIC; fig|220341.7.peg.2339; -.
DR   eggNOG; COG1051; Bacteria.
DR   HOGENOM; CLU_037162_12_0_6; -.
DR   OMA; HDNSRAY; -.
DR   Proteomes; UP000000541; Chromosome.
DR   Proteomes; UP000002670; Chromosome.
DR   GO; GO:0008727; F:GDP-mannose mannosyl hydrolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR   CDD; cd03430; GDPMH; 1.
DR   HAMAP; MF_00941; GDPMH_gmm; 1.
DR   InterPro; IPR033715; GDPMH.
DR   InterPro; IPR028613; GDPMH_Gmm.
DR   InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR   InterPro; IPR020084; NUDIX_hydrolase_CS.
DR   InterPro; IPR000086; NUDIX_hydrolase_dom.
DR   Pfam; PF00293; NUDIX; 1.
DR   PIRSF; PIRSF037599; GDPMH; 1.
DR   SUPFAM; SSF55811; SSF55811; 1.
DR   PROSITE; PS51462; NUDIX; 1.
DR   PROSITE; PS00893; NUDIX_BOX; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Magnesium; Metal-binding.
FT   CHAIN           1..157
FT                   /note="GDP-mannose mannosyl hydrolase"
FT                   /id="PRO_0000056985"
FT   DOMAIN          3..153
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00941"
FT   MOTIF           50..71
FT                   /note="Nudix box"
FT   BINDING         2..3
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00941"
FT   BINDING         8
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00941"
FT   BINDING         36
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00941"
FT   BINDING         49
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00941"
FT   BINDING         69
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00941"
FT   BINDING         122
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00941"
SQ   SEQUENCE   157 AA;  17680 MW;  755A117468E3F12A CRC64;
     MFLRQEDFAA VVRTTPLISL DFIVENGQGE ILLGQRLNRP AQGYWFVPGG RVCKDETLEA
     AFARLTQAEL GVRLPLAAGT FYGVWQHFYD DNFSSEDFST HYIVLGFRLR VAESDLRLPD
     AQHGSYRWLT PEQLLAGDNV HENSRAYFSP DAPAVGL
 
 
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