IPYR_RICFE
ID IPYR_RICFE Reviewed; 173 AA.
AC Q4UKW0;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 83.
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=RF_0962;
OS Rickettsia felis (strain ATCC VR-1525 / URRWXCal2) (Rickettsia azadi).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=315456;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-1525 / URRWXCal2;
RX PubMed=15984913; DOI=10.1371/journal.pbio.0030248;
RA Ogata H., Renesto P., Audic S., Robert C., Blanc G., Fournier P.-E.,
RA Parinello H., Claverie J.-M., Raoult D.;
RT "The genome sequence of Rickettsia felis identifies the first putative
RT conjugative plasmid in an obligate intracellular parasite.";
RL PLoS Biol. 3:1-12(2005).
CC -!- FUNCTION: Catalyzes the hydrolysis of inorganic pyrophosphate (PPi)
CC forming two phosphate ions. {ECO:0000255|HAMAP-Rule:MF_00209}.
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};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00209};
CC -!- SUBUNIT: Homohexamer. {ECO:0000255|HAMAP-Rule:MF_00209}.
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 -!- SEQUENCE CAUTION:
CC Sequence=AAY61813.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000053; AAY61813.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_011271285.1; NC_007109.1.
DR AlphaFoldDB; Q4UKW0; -.
DR SMR; Q4UKW0; -.
DR STRING; 315456.RF_0962; -.
DR EnsemblBacteria; AAY61813; AAY61813; RF_0962.
DR KEGG; rfe:RF_0962; -.
DR eggNOG; COG0221; Bacteria.
DR HOGENOM; CLU_073198_1_0_5; -.
DR OrthoDB; 1767807at2; -.
DR Proteomes; UP000008548; 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 Cytoplasm; Hydrolase; Magnesium; Metal-binding.
FT CHAIN 1..173
FT /note="Inorganic pyrophosphatase"
FT /id="PRO_0000278036"
FT BINDING 29
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT BINDING 43
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT BINDING 55
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT BINDING 65
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT BINDING 70
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT BINDING 70
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT BINDING 102
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT BINDING 141
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
SQ SEQUENCE 173 AA; 19551 MW; 50C73DDA61C42B4B CRC64;
MFIDKIKAKA NNDEINVIIE IPMNIGPIKY EFDKESGAVF VDRFMQTTMS YPCNYGFIPH
TLSNDGDPVD VLVVAHHPVV PGSVIKCRAV GVLMMEDESG LDEKIIAVPT SKLDITFDHI
KELDDLCEML KKRIVHFFEH YKDLEKGKWV KVTGWENKAK ANALINEGID RAS
