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NUDK_YERE8
ID   NUDK_YERE8              Reviewed;         191 AA.
AC   A1JL31;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=GDP-mannose pyrophosphatase;
DE            EC=3.6.1.- {ECO:0000250|UniProtKB:P37128};
DE   AltName: Full=GDP-mannose hydrolase;
DE   AltName: Full=GDPMK;
GN   Name=nudK; OrderedLocusNames=YE1161;
OS   Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 /
OS   8081).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=393305;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 13174 / 8081;
RX   PubMed=17173484; DOI=10.1371/journal.pgen.0020206;
RA   Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L.,
RA   Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T.,
RA   Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S.,
RA   Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J.,
RA   Prentice M.B.;
RT   "The complete genome sequence and comparative genome analysis of the high
RT   pathogenicity Yersinia enterocolitica strain 8081.";
RL   PLoS Genet. 2:2039-2051(2006).
CC   -!- FUNCTION: Nucleoside diphosphate sugar hydrolase that hydrolyzes GDP-
CC       mannose as its preferred substrate, yielding GMP and mannose-1-
CC       phosphate. {ECO:0000250|UniProtKB:P37128}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GDP-alpha-D-mannose + H2O = alpha-D-mannose 1-phosphate + GMP
CC         + 2 H(+); Xref=Rhea:RHEA:27978, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57527, ChEBI:CHEBI:58115, ChEBI:CHEBI:58409;
CC         Evidence={ECO:0000250|UniProtKB:P37128};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P37128};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P37128}.
CC   -!- DOMAIN: In the dimer, the N-terminal domains are swapped between the
CC       two monomers, such that residues of both chains contribute to the
CC       active site. {ECO:0000250|UniProtKB:P37128}.
CC   -!- SIMILARITY: Belongs to the Nudix hydrolase family. NudK subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AM286415; CAL11255.1; -; Genomic_DNA.
DR   RefSeq; WP_011815831.1; NC_008800.1.
DR   RefSeq; YP_001005488.1; NC_008800.1.
DR   AlphaFoldDB; A1JL31; -.
DR   SMR; A1JL31; -.
DR   STRING; 393305.YE1161; -.
DR   EnsemblBacteria; CAL11255; CAL11255; YE1161.
DR   KEGG; yen:YE1161; -.
DR   PATRIC; fig|393305.7.peg.1267; -.
DR   eggNOG; COG0494; Bacteria.
DR   HOGENOM; CLU_062658_6_0_6; -.
DR   OMA; RTPAACI; -.
DR   Proteomes; UP000000642; Chromosome.
DR   GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR004385; NDP_pyrophosphatase.
DR   InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR   InterPro; IPR000086; NUDIX_hydrolase_dom.
DR   Pfam; PF00293; NUDIX; 1.
DR   SUPFAM; SSF55811; SSF55811; 1.
DR   TIGRFAMs; TIGR00052; TIGR00052; 1.
DR   PROSITE; PS51462; NUDIX; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Magnesium; Metal-binding.
FT   CHAIN           1..191
FT                   /note="GDP-mannose pyrophosphatase"
FT                   /id="PRO_0000342505"
FT   DOMAIN          43..180
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT   MOTIF           86..106
FT                   /note="Nudix box"
FT   BINDING         38..40
FT                   /ligand="GDP-alpha-D-mannose"
FT                   /ligand_id="ChEBI:CHEBI:57527"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250|UniProtKB:P37128"
FT   BINDING         67
FT                   /ligand="GDP-alpha-D-mannose"
FT                   /ligand_id="ChEBI:CHEBI:57527"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250|UniProtKB:P37128"
FT   BINDING         85..87
FT                   /ligand="GDP-alpha-D-mannose"
FT                   /ligand_id="ChEBI:CHEBI:57527"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250|UniProtKB:P37128"
FT   BINDING         85
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P37128"
FT   BINDING         100
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P37128"
FT   BINDING         104
FT                   /ligand="GDP-alpha-D-mannose"
FT                   /ligand_id="ChEBI:CHEBI:57527"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250|UniProtKB:P37128"
FT   BINDING         104
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P37128"
FT   BINDING         104
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P37128"
FT   BINDING         127
FT                   /ligand="GDP-alpha-D-mannose"
FT                   /ligand_id="ChEBI:CHEBI:57527"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250|UniProtKB:P37128"
FT   BINDING         150..151
FT                   /ligand="GDP-alpha-D-mannose"
FT                   /ligand_id="ChEBI:CHEBI:57527"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250|UniProtKB:P37128"
FT   BINDING         151
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P37128"
FT   BINDING         176
FT                   /ligand="GDP-alpha-D-mannose"
FT                   /ligand_id="ChEBI:CHEBI:57527"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250|UniProtKB:P37128"
SQ   SEQUENCE   191 AA;  21596 MW;  4B45BC687E7FB3F5 CRC64;
     MSVKIENIRS ELLSKNWFKL HKYTFDLIDD NGTSVQQIRE VYDRGNGATI LLYNRPNGTV
     LLINQFRMPT YVNGNPDGML LETCAGLLDN DSPEECIRRE AMEETGYQVD SVQKLFEAYM
     SPGGVTEIIH FFAAEYHADQ KVTDDVGVED EVIEVVELPF TEAIAMIADG RIKDGKTIML
     LQYAQIHGLL K
 
 
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