(data stored in ACNUC1104 zone)

SWISSPROT: D5USC5_TSUPD

ID   D5USC5_TSUPD            Unreviewed;       166 AA.
AC   D5USC5;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   08-MAY-2019, entry version 50.
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=Tpau_0552 {ECO:0000313|EMBL:ADG77192.1};
OS   Tsukamurella paurometabola (strain ATCC 8368 / DSM 20162 / JCM 10117 /
OS   NBRC 16120 / NCTC 13040) (Corynebacterium paurometabolum).
OC   Bacteria; Actinobacteria; Corynebacteriales; Tsukamurellaceae;
OC   Tsukamurella.
OX   NCBI_TaxID=521096 {ECO:0000313|EMBL:ADG77192.1, ECO:0000313|Proteomes:UP000001213};
RN   [1] {ECO:0000313|Proteomes:UP000001213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8368 / DSM 20162 / JCM 10117 / NBRC 16120 / NCTC 13040
RC   {ECO:0000313|Proteomes:UP000001213};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K.,
RA   Ivanova N., Mikhailova N., Munk A.C., Brettin T., Detter J.C.,
RA   Tapia R., Han C., Larimer F., Land M., Hauser L., Markowitz V.,
RA   Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Jando M., Brambilla E.,
RA   Klenk H.-P., Eisen J.A.;
RT   "The complete chromosome of Tsukamurella paurometabola DSM 20162.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADG77192.1, ECO:0000313|Proteomes:UP000001213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8368 / DSM 20162 / JCM 10117 / NBRC 16120 / NCTC 13040
RC   {ECO:0000313|Proteomes:UP000001213};
RX   PubMed=21886861;
RA   Munk A.C., Lapidus A., Lucas S., Nolan M., Tice H., Cheng J.F.,
RA   Del Rio T.G., Goodwin L., Pitluck S., Liolios K., Huntemann M.,
RA   Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA   Palaniappan K., Tapia R., Han C., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Brettin T., Yasawong M., Brambilla E.M., Rohde M.,
RA   Sikorski J., Goker M., Detter J.C., Woyke T., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Tsukamurella paurometabola type strain
RT   (no. 33).";
RL   Stand. Genomic Sci. 4:342-351(2011).
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; CP001966; ADG77192.1; -; Genomic_DNA.
DR   RefSeq; WP_013125234.1; NC_014158.1.
DR   STRING; 521096.Tpau_0552; -.
DR   EnsemblBacteria; ADG77192; ADG77192; Tpau_0552.
DR   KEGG; tpr:Tpau_0552; -.
DR   eggNOG; ENOG4105F0N; Bacteria.
DR   eggNOG; COG0221; LUCA.
DR   HOGENOM; HOG000236473; -.
DR   KO; K01507; -.
DR   OMA; DEPTFPG; -.
DR   OrthoDB; 1767807at2; -.
DR   BioCyc; TPAU521096:G1GKO-535-MONOMER; -.
DR   Proteomes; UP000001213; 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; D5USC5.
DR   SWISS-2DPAGE; D5USC5.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001213};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00209};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00209,
KW   ECO:0000313|EMBL:ADG77192.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00209};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00209};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001213}.
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   166 AA;  18446 MW;  6D7B7C33E1699281 CRC64;
     MEFEVTVEIA KGSRNKYEVD HKSGRLKLDR YLYTSFGYPT DYGYIEDTLG EDGDPLDALV
     LLPESVIPGS LVDCRAIGMF KMEDEKGGDD KVLVVPAGDP RWDAIQDLEH IDKFELDAIE
     HFFVHYKDLE PGKFVKGSTW VGKAEAEKEI AASIARAEAA AEGIDS
//

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