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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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