(data stored in ACNUC7421 zone)

SWISSPROT: C5BF92_EDWI9

ID   C5BF92_EDWI9            Unreviewed;       176 AA.
AC   C5BF92;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 47.
DE   RecName: Full=Inorganic pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_00209};
DE            EC=3.6.1.1 {ECO:0000256|HAMAP-Rule:MF_00209};
DE   AltName: Full=Pyrophosphate phospho-hydrolase {ECO:0000256|HAMAP-Rule:MF_00209};
DE            Short=PPase {ECO:0000256|HAMAP-Rule:MF_00209};
GN   Name=ppa {ECO:0000256|HAMAP-Rule:MF_00209};
GN   OrderedLocusNames=NT01EI_0440 {ECO:0000313|EMBL:ACR67678.1};
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR67678.1, ECO:0000313|Proteomes:UP000001485};
RN   [1] {ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|Proteomes:UP000001485};
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the hydrolysis of inorganic pyrophosphate
CC       (PPi) forming two phosphate ions. {ECO:0000256|HAMAP-
CC       Rule:MF_00209}.
CC   -!- CATALYTIC ACTIVITY: Diphosphate + H(2)O = 2 phosphate.
CC       {ECO:0000256|HAMAP-Rule:MF_00209}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00209};
CC   -!- SUBUNIT: Homohexamer. {ECO:0000256|HAMAP-Rule:MF_00209}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00209}.
CC   -!- SIMILARITY: Belongs to the PPase family. {ECO:0000256|HAMAP-
CC       Rule:MF_00209}.
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DR   EMBL; CP001600; ACR67678.1; -; Genomic_DNA.
DR   RefSeq; WP_015869881.1; NC_012779.2.
DR   STRING; 634503.NT01EI_0440; -.
DR   EnsemblBacteria; ACR67678; ACR67678; NT01EI_0440.
DR   GeneID; 7961265; -.
DR   KEGG; eic:NT01EI_0440; -.
DR   PATRIC; fig|634503.3.peg.400; -.
DR   eggNOG; ENOG4105F0N; Bacteria.
DR   eggNOG; COG0221; LUCA.
DR   HOGENOM; HOG000236473; -.
DR   KO; K01507; -.
DR   OMA; DEPTFPG; -.
DR   OrthoDB; POG091H05Q5; -.
DR   Proteomes; UP000001485; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004427; F:inorganic diphosphatase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006796; P:phosphate-containing compound metabolic process; IEA:InterPro.
DR   CDD; cd00412; pyrophosphatase; 1.
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; SSF50324; 1.
DR   PROSITE; PS00387; PPASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; C5BF92.
DR   SWISS-2DPAGE; C5BF92.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001485};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00209};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00209,
KW   ECO:0000313|EMBL:ACR67678.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00209};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00209};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001485}.
FT   METAL        66     66       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00209}.
FT   METAL        71     71       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00209}.
FT   METAL        71     71       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00209}.
FT   METAL       103    103       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00209}.
FT   BINDING      30     30       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00209}.
FT   BINDING      44     44       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00209}.
FT   BINDING      56     56       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00209}.
FT   BINDING     142    142       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00209}.
SQ   SEQUENCE   176 AA;  19677 MW;  792136AA0243AC63 CRC64;
     MSLINVPAGK DMPEDIYVVI EIPANADPIK YEIDKETGAL FVDRFMSTAM FYPCNYGYIN
     HTLSLDGDPV DVLVPTPYPL QPGSVIRCRP VGVLKMTDEA GEDAKLVAVP HSKLTKEYDH
     IQDVNDLPEL LRAQIAHFFE HYKDLEKGKW VKVEGWADAA AAKAEIIASF ERAKNK
//

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