(data stored in SCRATCH zone)

SWISSPROT: C0ZNS3_RHOE4

ID   C0ZNS3_RHOE4            Unreviewed;       163 AA.
AC   C0ZNS3;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   08-MAY-2019, entry version 56.
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   ECO:0000313|EMBL:BAH31325.1};
GN   OrderedLocusNames=RER_06170 {ECO:0000313|EMBL:BAH31325.1};
OS   Rhodococcus erythropolis (strain PR4 / NBRC 100887).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=234621 {ECO:0000313|EMBL:BAH31325.1, ECO:0000313|Proteomes:UP000002204};
RN   [1] {ECO:0000313|Proteomes:UP000002204}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204};
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus
RT   erythropolis PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:BAH31325.1, ECO:0000313|Proteomes:UP000002204}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204};
RX   PubMed=16423019; DOI=10.1111/j.1462-2920.2005.00899.x;
RA   Sekine M., Tanikawa S., Omata S., Saito M., Fujisawa T., Tsukatani N.,
RA   Tajima T., Sekigawa T., Kosugi H., Matsuo Y., Nishiko R., Imamura K.,
RA   Ito M., Narita H., Tago S., Fujita N., Harayama S.;
RT   "Sequence analysis of three plasmids harboured in Rhodococcus
RT   erythropolis strain PR4.";
RL   Environ. Microbiol. 8:334-346(2006).
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; AP008957; BAH31325.1; -; Genomic_DNA.
DR   RefSeq; WP_003941181.1; NC_012490.1.
DR   STRING; 234621.RER_06170; -.
DR   EnsemblBacteria; BAH31325; BAH31325; RER_06170.
DR   KEGG; rer:RER_06170; -.
DR   PATRIC; fig|234621.6.peg.1064; -.
DR   eggNOG; ENOG4105F0N; Bacteria.
DR   eggNOG; COG0221; LUCA.
DR   HOGENOM; HOG000236473; -.
DR   KO; K01507; -.
DR   OMA; DEPTFPG; -.
DR   Proteomes; UP000002204; 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; C0ZNS3.
DR   SWISS-2DPAGE; C0ZNS3.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002204};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00209};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00209,
KW   ECO:0000313|EMBL:BAH31325.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00209};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00209}.
FT   ACT_SITE     89     89       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00209}.
FT   METAL         8      8       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00209}.
FT   METAL        52     52       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00209}.
FT   METAL        57     57       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00209}.
FT   METAL        57     57       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00209}.
FT   METAL        84     84       Magnesium 3. {ECO:0000256|HAMAP-Rule:
FT                                MF_00209}.
FT   METAL        89     89       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00209}.
FT   METAL        89     89       Magnesium 3. {ECO:0000256|HAMAP-Rule:
FT                                MF_00209}.
FT   BINDING      16     16       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00209}.
FT   BINDING      30     30       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00209}.
FT   BINDING      42     42       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00209}.
FT   BINDING     126    126       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00209}.
SQ   SEQUENCE   163 AA;  18177 MW;  87D40F028036F653 CRC64;
     MEFDVTIEIP KGQRNKYEVD HVTGRVKLDR YLYTAFGYPA DYGFIENTLG EDGDPLDAMV
     LLPESVFPGV IVEARAVAMF KMVDEAGGDD KVLCVPAGDP RWDHIQDLGD ISQFELDAIK
     HFFVHYKDLE PNKHVEAANW VGRAEAEAEI EASIKRLAAN GGH
//

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