NUDK_SHIDS
ID NUDK_SHIDS Reviewed; 191 AA.
AC Q32DA4;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 87.
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=SDY_2650;
OS Shigella dysenteriae serotype 1 (strain Sd197).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300267;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sd197;
RX PubMed=16275786; DOI=10.1093/nar/gki954;
RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA Jin Q.;
RT "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT bacillary dysentery.";
RL Nucleic Acids Res. 33:6445-6458(2005).
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; CP000034; ABB62701.1; -; Genomic_DNA.
DR RefSeq; WP_001301627.1; NC_007606.1.
DR RefSeq; YP_404192.1; NC_007606.1.
DR AlphaFoldDB; Q32DA4; -.
DR SMR; Q32DA4; -.
DR STRING; 300267.SDY_2650; -.
DR EnsemblBacteria; ABB62701; ABB62701; SDY_2650.
DR KEGG; sdy:SDY_2650; -.
DR PATRIC; fig|300267.13.peg.3196; -.
DR HOGENOM; CLU_062658_6_0_6; -.
DR OMA; RTPAACI; -.
DR Proteomes; UP000002716; 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_0000342501"
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; 21745 MW; B88E6371E2B57E72 CRC64;
MTQQITLIKD KILSDNYFTL HNITYDLTRK DGEVIRHKRE VYDRGNGATI LLYNAKKKTV
VLIRQFRVAT WVNGNESGQL IETCAGLLDN DEPEVCIRKE AIEETGYEVG EVRKLFELYM
SPGGVTELIH FFIAEYSDNQ RANAGGGVED EDIEVLELPF SQALEMIKTG EIRDGKTVLL
LNYLQMSHLI D
