ID C0Q6I5_SALPC Unreviewed; 176 AA.
AC C0Q6I5;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 01-MAY-2013, entry version 27.
DE RecName: Full=Inorganic pyrophosphatase;
DE EC=3.6.1.1;
DE AltName: Full=Pyrophosphate phospho-hydrolase;
GN Name=ppa; OrderedLocusNames=SPC_4565;
OS Salmonella paratyphi C (strain RKS4594).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=476213;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RKS4594;
RX PubMed=19229335; DOI=10.1371/journal.pone.0004510;
RA Liu W.Q., Feng Y., Wang Y., Zou Q.H., Chen F., Guo J.T., Peng Y.H.,
RA Jin Y., Li Y.G., Hu S.N., Johnston R.N., Liu G.R., Liu S.L.;
RT "Salmonella paratyphi C: genetic divergence from Salmonella
RT choleraesuis and pathogenic convergence with Salmonella typhi.";
RL PLoS ONE 4:E4510-E4510(2009).
CC -!- CATALYTIC ACTIVITY: Diphosphate + H(2)O = 2 phosphate.
CC -!- COFACTOR: Binds 4 magnesium ions per subunit. Other metal ions can
CC support activity, but at a lower rate. Two magnesium ions are
CC required for the activation of the enzyme and are present before
CC substrate binds, two additional magnesium ions form complexes with
CC substrate and product (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the PPase family.
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DR EMBL; CP000857; ACN48615.1; -; Genomic_DNA.
DR RefSeq; YP_002640056.1; NC_012125.1.
DR ProteinModelPortal; C0Q6I5; -.
DR SMR; C0Q6I5; 2-176.
DR STRING; 476213.SPC_4565; -.
DR STRING; C0Q6I5; -.
DR PRIDE; C0Q6I5; -.
DR EnsemblBacteria; ACN48615; ACN48615; SPC_4565.
DR GeneID; 7557140; -.
DR KEGG; sei:SPC_4565; -.
DR PATRIC; 32368103; VBISalEnt12305_4600.
DR eggNOG; COG0221; -.
DR HOGENOM; HOG000236473; -.
DR KO; K01507; -.
DR OMA; GVANYKK; -.
DR ProtClustDB; PRK01250; -.
DR BioCyc; SENT476213:GH8J-4656-MONOMER; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004427; F:inorganic diphosphatase activity; IEA:HAMAP.
DR GO; GO:0000287; F:magnesium ion binding; IEA:HAMAP.
DR GO; GO:0006796; P:phosphate-containing compound metabolic process; IEA:InterPro.
DR Gene3D; 3.90.80.10; -; 1.
DR HAMAP; MF_00209; Inorganic_PPase; 1; -.
DR InterPro; IPR008162; Pyrophosphatase.
DR PANTHER; PTHR10286; PTHR10286; 1.
DR Pfam; PF00719; Pyrophosphatase; 1.
DR SUPFAM; SSF50324; Pyrophosphatase; 1.
DR PROSITE; PS00387; PPASE; 1.
PE 3: Inferred from homology;
KW Complete proteome; Cytoplasm; Hydrolase; Magnesium; Metal-binding.
FT METAL 66 66 Magnesium 1 (By similarity).
FT METAL 71 71 Magnesium 1 (By similarity).
FT METAL 71 71 Magnesium 2 (By similarity).
FT METAL 103 103 Magnesium 1 (By similarity).
SQ SEQUENCE 176 AA; 19677 MW; 3C00EC5AA02B1BB2 CRC64;
MSLLNVPAGK ELPEDIYVVI EIPANADPIK YEVDKESGAL FVDRFMSTAM FYPCNYGYIN
HTLSLDGDPV DVLVPTPYPL QPGAVIRCRP VGVLKMTDES GEDAKLVAVP HTKLSKEYDH
IKDVNDLPEL LKAQITHFFE HYKDLEKGKW VKVDGWDNAE AAKAEIVASF ERAAKK
//
