NUDK_PECAS
ID NUDK_PECAS Reviewed; 193 AA.
AC Q6D8X4;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 97.
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=ECA0847;
OS Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia
OS carotovora subsp. atroseptica).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Pectobacterium.
OX NCBI_TaxID=218491;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCRI 1043 / ATCC BAA-672;
RX PubMed=15263089; DOI=10.1073/pnas.0402424101;
RA Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J.,
RA Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K.,
RA Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J.,
RA Fraser A., Hance Z., Hauser H., Jagels K., Moule S., Norbertczak H.,
RA Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S.,
RA Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K.;
RT "Genome sequence of the enterobacterial phytopathogen Erwinia carotovora
RT subsp. atroseptica and characterization of virulence factors.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(2004).
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; BX950851; CAG73760.1; -; Genomic_DNA.
DR RefSeq; WP_011092451.1; NC_004547.2.
DR AlphaFoldDB; Q6D8X4; -.
DR SMR; Q6D8X4; -.
DR STRING; 218491.ECA0847; -.
DR EnsemblBacteria; CAG73760; CAG73760; ECA0847.
DR GeneID; 57207592; -.
DR KEGG; eca:ECA0847; -.
DR PATRIC; fig|218491.5.peg.848; -.
DR eggNOG; COG0494; Bacteria.
DR HOGENOM; CLU_062658_6_0_6; -.
DR OMA; RTPAACI; -.
DR OrthoDB; 1831818at2; -.
DR Proteomes; UP000007966; 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..193
FT /note="GDP-mannose pyrophosphatase"
FT /id="PRO_0000342481"
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 193 AA; 21713 MW; 7EBC0C22AC2D1BC1 CRC64;
MSSPIDIVEK KLLSDHWFIL HKYVFDLKRK NGGVVRQIRE VYDRGDGATI LLYNRAKGTV
ILTRQFRIPT YVNGNESGML LEACAGLLDD YSPEECIRNE AIEETGYAVG NVEKLFDAYM
SPGGVTERLH FFAAEYDESL RDNSGGGVED EDIEVLELPF SEAIAMMNDG RIKDGKTIML
LQHAIIRGWF AKG
