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NUDK_ECODH
ID   NUDK_ECODH              Reviewed;         191 AA.
AC   B1XAD8;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 73.
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=ECDH10B_2632;
OS   Escherichia coli (strain K12 / DH10B).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=316385;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / DH10B;
RX   PubMed=18245285; DOI=10.1128/jb.01695-07;
RA   Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B.,
RA   Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B.,
RA   Posfai G., Weinstock G.M., Blattner F.R.;
RT   "The complete genome sequence of Escherichia coli DH10B: insights into the
RT   biology of a laboratory workhorse.";
RL   J. Bacteriol. 190:2597-2606(2008).
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; CP000948; ACB03618.1; -; Genomic_DNA.
DR   RefSeq; WP_001300814.1; NC_010473.1.
DR   AlphaFoldDB; B1XAD8; -.
DR   SMR; B1XAD8; -.
DR   KEGG; ecd:ECDH10B_2632; -.
DR   HOGENOM; CLU_062658_6_0_6; -.
DR   OMA; RTPAACI; -.
DR   BioCyc; ECOL316385:ECDH10B_RS13375-MON; -.
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_0000342483"
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         17
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         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;  21749 MW;  13880625B41233C5 CRC64;
     MTQQITLIKD KILSDNYFTL HNITYDLTRK DGEVIRHKRE VYDRGNGATI LLYNTKKKTV
     VLIRQFRVAT WVNGNESGQL IESCAGLLDN DEPEVCIRKE AIEETGYEVG EVRKLFELYM
     SPGGVTELIH FFIAEYSDNQ RANAGGGVED EDIEVLELPF SQALEMIKTG EIRDGKTVLL
     LNYLQTSHLM D
 
 
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