ID A0A223CZR4_9BACL Unreviewed; 160 AA. AC A0A223CZR4; DT 25-OCT-2017, integrated into UniProtKB/TrEMBL. DT 25-OCT-2017, sequence version 1. DT 20-DEC-2017, entry version 3. 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 ORFNames=CIG75_07465 {ECO:0000313|EMBL:ASS74832.1}; OS Tumebacillus algifaecis. OC Bacteria; Firmicutes; Bacilli; Bacillales; Alicyclobacillaceae; OC Tumebacillus. OX NCBI_TaxID=1214604 {ECO:0000313|EMBL:ASS74832.1, ECO:0000313|Proteomes:UP000214688}; RN [1] {ECO:0000313|EMBL:ASS74832.1, ECO:0000313|Proteomes:UP000214688} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=THMBR28 {ECO:0000313|EMBL:ASS74832.1, RC ECO:0000313|Proteomes:UP000214688}; RX PubMed=25858243; DOI=10.1099/ijs.0.000240; RA Wu Y.F., Zhang B., Xing P., Wu Q.L., Liu S.J.; RT "Tumebacillus algifaecis sp. nov., isolated from decomposing algal RT scum."; RL Int. J. Syst. Evol. Microbiol. 65:2194-2198(2015). 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP022657; ASS74832.1; -; Genomic_DNA. DR Proteomes; UP000214688; 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; KW Complete proteome {ECO:0000313|Proteomes:UP000214688}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00209}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00209}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00209}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00209}; KW Reference proteome {ECO:0000313|Proteomes:UP000214688}. 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 91 91 Magnesium 1. {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 160 AA; 18246 MW; C89D20EE4B07604A CRC64; MAMIVNAFIE IPTGSQNKYE YDKENNRFML DRVLFSPMHY PTEYGYIDNT LAEDGDPLDI LVVTSFPTFP GCVIESRVVG VLIMTDDKGK DEKLLAVPTQ DPRFANVHTL DDVAPHVLKE ISHFFQVYKD LENKQVQIDG WEGVETAQRL LDESTARYAK //