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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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