位置:首页 > 蛋白库 > NUDK_SHIFL
NUDK_SHIFL
ID   NUDK_SHIFL              Reviewed;         191 AA.
AC   Q83K58; Q7C0J4;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 119.
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=SF2509, S2660;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA   Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA   Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA   Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA   Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA   Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella flexneri
RT   serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
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}.
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; AE005674; AAN44013.1; -; Genomic_DNA.
DR   EMBL; AE014073; AAP17828.1; -; Genomic_DNA.
DR   RefSeq; NP_708306.1; NC_004337.2.
DR   RefSeq; WP_001325569.1; NZ_WPGW01000011.1.
DR   AlphaFoldDB; Q83K58; -.
DR   SMR; Q83K58; -.
DR   STRING; 198214.SF2509; -.
DR   EnsemblBacteria; AAN44013; AAN44013; SF2509.
DR   EnsemblBacteria; AAP17828; AAP17828; S2660.
DR   GeneID; 1025501; -.
DR   KEGG; sfl:SF2509; -.
DR   KEGG; sfx:S2660; -.
DR   PATRIC; fig|198214.7.peg.2999; -.
DR   HOGENOM; CLU_062658_6_0_6; -.
DR   OMA; RTPAACI; -.
DR   OrthoDB; 1831818at2; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; 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; Reference proteome.
FT   CHAIN           1..191
FT                   /note="GDP-mannose pyrophosphatase"
FT                   /id="PRO_0000342502"
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;  B888A5AAE07E7A62 CRC64;
     MTQQITLIKD KILSDNYFTL HNITYDLTRK DGEVIRHKRE VYDRGNGATI LLYNAKKKSV
     VLIRQFRVAT WVNGNESGQL IETCAGLLDN DEPEVCIRKE AIEETGYEVG EVRKLFELYM
     SPGGVTELIH FFIAEYSDNQ RANAGGGVED EDIEVLELPF SQALEMIKTG EIRDGKTVLL
     LNYLQMSHLM D
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024