ID IPYR_NOSS1 Reviewed; 169 AA. AC P80562; Q8YR78; DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot. DT 11-FEB-2002, sequence version 1. DT 10-JUN-2026, entry version 113. DE RecName: Full=Inorganic pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_00209}; DE EC=3.6.1.1 {ECO:0000255|HAMAP-Rule:MF_00209}; DE AltName: Full=Pyrophosphate phospho-hydrolase {ECO:0000255|HAMAP-Rule:MF_00209}; DE Short=PPase {ECO:0000255|HAMAP-Rule:MF_00209}; GN Name=ppa {ECO:0000255|HAMAP-Rule:MF_00209}; OrderedLocusNames=all3570; OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576). OC Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales; OC Nostocaceae; Nostoc. OX NCBI_TaxID=103690; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-23, CATALYTIC RP ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND FORMYLATION RP AT MET-1. RX PubMed=17635582; DOI=10.1111/j.1742-4658.2007.05927.x; RA Gomez-Garcia M.R., Losada M., Serrano A.; RT "Comparative biochemical and functional studies of family I soluble RT inorganic pyrophosphatases from photosynthetic bacteria."; RL FEBS J. 274:3948-3959(2007). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576; RX PubMed=11759840; DOI=10.1093/dnares/8.5.205; RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A., RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M., RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M., RA Takazawa M., Yamada M., Yasuda M., Tabata S.; RT "Complete genomic sequence of the filamentous nitrogen-fixing RT cyanobacterium Anabaena sp. strain PCC 7120."; RL DNA Res. 8:205-213(2001). CC -!- FUNCTION: Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) CC forming two phosphate ions. {ECO:0000255|HAMAP-Rule:MF_00209, CC ECO:0000269|PubMed:17635582}. CC -!- CATALYTIC ACTIVITY: CC Reaction=diphosphate + H2O = 2 phosphate + H(+); Xref=Rhea:RHEA:24576, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:43474; EC=3.6.1.1; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00209, ECO:0000269|PubMed:17635582}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00209, ECO:0000269|PubMed:17635582}; CC Note=In the presence of Zn(2+), Mn(2+), Cu(2+), Fe(2+) or Co(2+) ions, CC activity is very low. In the absence of metal ions, there is no CC activity. {ECO:0000269|PubMed:17635582}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=3 uM for PPi {ECO:0000269|PubMed:17635582}; CC -!- SUBUNIT: Homohexamer. {ECO:0000255|HAMAP-Rule:MF_00209, CC ECO:0000269|PubMed:17635582}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00209}. CC -!- SIMILARITY: Belongs to the PPase family. {ECO:0000255|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; AJ252206; CAC81009.2; -; Genomic_DNA. DR EMBL; BA000019; BAB75269.1; -; Genomic_DNA. DR PIR; AC2252; AC2252. DR RefSeq; WP_010997720.1; NC_003272.1. DR AlphaFoldDB; P80562; -. DR SMR; P80562; -. DR STRING; 103690.gene:10495611; -. DR KEGG; ana:all3570; -. DR eggNOG; COG0221; Bacteria. DR OrthoDB; 5187599at2; -. DR BRENDA; 3.6.1.1; 319. DR SABIO-RK; P80562; -. DR Proteomes; UP000002483; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004427; F:inorganic diphosphate phosphatase 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 FunFam; 3.90.80.10:FF:000003; Inorganic pyrophosphatase; 1. DR Gene3D; 3.90.80.10; Inorganic pyrophosphatase; 1. DR HAMAP; MF_00209; Inorganic_PPase; 1. DR InterPro; IPR008162; Pyrophosphatase. DR InterPro; IPR036649; Pyrophosphatase_sf. DR PANTHER; PTHR10286; INORGANIC PYROPHOSPHATASE; 1. DR Pfam; PF00719; Pyrophosphatase; 1. DR SUPFAM; SSF50324; Inorganic pyrophosphatase; 1. DR PROSITE; PS00387; PPASE; 1. PE 1: Evidence at protein level; KW Cytoplasm; Direct protein sequencing; Formylation; Hydrolase; Magnesium; KW Metal-binding; Reference proteome. FT CHAIN 1..169 FT /note="Inorganic pyrophosphatase" FT /id="PRO_0000137474" FT BINDING 28 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00209" FT BINDING 42 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00209" FT BINDING 54 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00209" FT BINDING 64 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00209" FT BINDING 69 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00209" FT BINDING 69 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00209" FT BINDING 101 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00209" FT BINDING 138 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00209" FT MOD_RES 1 FT /note="N-formylmethionine" FT /evidence="ECO:0000269|PubMed:17635582" FT CONFLICT 117 FT /note="V -> R (in Ref. 1; CAC81009)" FT /evidence="ECO:0000305" FT CONFLICT 148..149 FT /note="IL -> SV (in Ref. 1; CAC81009)" FT /evidence="ECO:0000305" FT CONFLICT 163..165 FT /note="QSI -> HPV (in Ref. 1; CAC81009)" FT /evidence="ECO:0000305" FT CONFLICT 169 FT /note="K -> T (in Ref. 1; CAC81009)" FT /evidence="ECO:0000305" SQ SEQUENCE 169 AA; 18961 MW; 17A027E16C2289D3 CRC64; MDLSRIPAQP KPGVINILIE IAGGSQNKYE FDKDLEAFAL DRVLYSSVKY PYDYGFVPNT LADDGDPLDG MVIIDEPTFP GCVIAARPIG FLEMIDGGDR DEKILAVPDK DPRYAHVKSL NDVAPHRLDE IAEFFRSYKN LEKKVTQILG WQDVDQVKAL VDQSIKAYK //