NUDK_YERP3
ID NUDK_YERP3 Reviewed; 198 AA.
AC A7FG78;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 82.
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=YpsIP31758_1276;
OS Yersinia pseudotuberculosis serotype O:1b (strain IP 31758).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=349747;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IP 31758;
RX PubMed=17784789; DOI=10.1371/journal.pgen.0030142;
RA Eppinger M., Rosovitz M.J., Fricke W.F., Rasko D.A., Kokorina G.,
RA Fayolle C., Lindler L.E., Carniel E., Ravel J.;
RT "The complete genome sequence of Yersinia pseudotuberculosis IP31758, the
RT causative agent of Far East scarlet-like fever.";
RL PLoS Genet. 3:1508-1523(2007).
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; CP000720; ABS46771.1; -; Genomic_DNA.
DR RefSeq; WP_002208529.1; NC_009708.1.
DR AlphaFoldDB; A7FG78; -.
DR SMR; A7FG78; -.
DR EnsemblBacteria; ABS46771; ABS46771; YpsIP31758_1276.
DR GeneID; 66844817; -.
DR KEGG; ypi:YpsIP31758_1276; -.
DR HOGENOM; CLU_062658_6_0_6; -.
DR OMA; RTPAACI; -.
DR Proteomes; UP000002412; 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..198
FT /note="GDP-mannose pyrophosphatase"
FT /id="PRO_0000342510"
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 198 AA; 22472 MW; 8CEB6975DAE1A14B CRC64;
MSVKIENIQC ELLSKNWFKL HKYTFDLKTD EGTSVQQIRE VYDRGNGATI LLYNRQQGTV
VLIEQFRMPT YVNGNASGML LEACAGLLDN DSPEACIRRE AMEETGYQVD KVQKLFEAYM
SPGGVTELVY FFAAEYHPDQ KITDEVGVED EVIEVVELPF HDALAMVADG RIKDGKTIML
LQYAQIHFFP SSLTPQRC
