IPYR_NOSS1
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 03-AUG-2022, entry version 101.
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; Cyanobacteria; Nostocales; 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 = H(+) + 2 phosphate; 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;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00209,
CC 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; NZ_RSCN01000034.1.
DR AlphaFoldDB; P80562; -.
DR SMR; P80562; -.
DR STRING; 103690.17132703; -.
DR EnsemblBacteria; BAB75269; BAB75269; BAB75269.
DR KEGG; ana:all3570; -.
DR eggNOG; COG0221; Bacteria.
DR OMA; DEPTFPG; -.
DR OrthoDB; 1767807at2; -.
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 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 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
