(data stored in SCRATCH zone)

SWISSPROT: E3J7C3_FRAIE

ID   E3J7C3_FRAIE            Unreviewed;       182 AA.
AC   E3J7C3;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   08-MAY-2019, entry version 45.
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=FraEuI1c_0310 {ECO:0000313|EMBL:ADP78396.1};
OS   Frankia inefficax (strain DSM 45817 / CECT 9037 / EuI1c).
OC   Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=298654 {ECO:0000313|EMBL:ADP78396.1, ECO:0000313|Proteomes:UP000002484};
RN   [1] {ECO:0000313|EMBL:ADP78396.1, ECO:0000313|Proteomes:UP000002484}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45817 / CECT 9037 / EuI1c
RC   {ECO:0000313|Proteomes:UP000002484};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N.,
RA   Beauchemin N., Sen A., Sur S.A., Gtari M., Wall L., Tisa L., Woyke T.;
RT   "Complete sequence of Frankia sp. EuI1c.";
RL   Submitted (OCT-2010) 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:
CC       Reaction=diphosphate + H2O = H(+) + 2 phosphate;
CC         Xref=Rhea:RHEA:24576, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:43474; EC=3.6.1.1;
CC         Evidence={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; CP002299; ADP78396.1; -; Genomic_DNA.
DR   RefSeq; WP_013421519.1; NC_014666.1.
DR   STRING; 298654.FraEuI1c_0310; -.
DR   EnsemblBacteria; ADP78396; ADP78396; FraEuI1c_0310.
DR   KEGG; fri:FraEuI1c_0310; -.
DR   eggNOG; ENOG4105F0N; Bacteria.
DR   eggNOG; COG0221; LUCA.
DR   HOGENOM; HOG000236473; -.
DR   KO; K01507; -.
DR   OMA; DEPTFPG; -.
DR   OrthoDB; 1767807at2; -.
DR   BioCyc; FSP298654:G1GOT-310-MONOMER; -.
DR   Proteomes; UP000002484; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004427; F:inorganic diphosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
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   InterPro; IPR036649; Pyrophosphatase_sf.
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; E3J7C3.
DR   SWISS-2DPAGE; E3J7C3.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002484};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00209};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00209,
KW   ECO:0000313|EMBL:ADP78396.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00209};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00209};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002484}.
FT   ACT_SITE     91     91       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00209}.
FT   METAL        10     10       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00209}.
FT   METAL        54     54       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00209}.
FT   METAL        59     59       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00209}.
FT   METAL        59     59       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00209}.
FT   METAL        86     86       Magnesium 3. {ECO:0000256|HAMAP-Rule:
FT                                MF_00209}.
FT   METAL        91     91       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00209}.
FT   METAL        91     91       Magnesium 3. {ECO:0000256|HAMAP-Rule:
FT                                MF_00209}.
FT   BINDING      18     18       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00209}.
FT   BINDING      32     32       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00209}.
FT   BINDING      44     44       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00209}.
FT   BINDING     128    128       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00209}.
SQ   SEQUENCE   182 AA;  20786 MW;  878E7D66E96E0701 CRC64;
     MDLEFDVTIE IPKGQRNKYE MDHHTGRIRL DRMLFTSTHY PSDYGFIEGT LGRDGDPLDA
     LVLLEEPTFP GCLVRCRTIG MFQMTDEKGP DDKVLCVPVA DIRQEHLRDI RHLPEFDRLE
     IQHFFEVYKD LEPGKSVEGA SWVGRADAER EILASIKRLE TDGAEHAPVV DEVETEAETE
     TA
//

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