IPYR_RICPR
ID IPYR_RICPR Reviewed; 172 AA.
AC Q9ZCW5;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 110.
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=RP589;
OS Rickettsia prowazekii (strain Madrid E).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX NCBI_TaxID=272947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Madrid E;
RX PubMed=9823893; DOI=10.1038/24094;
RA Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA Kurland C.G.;
RT "The genome sequence of Rickettsia prowazekii and the origin of
RT mitochondria.";
RL Nature 396:133-140(1998).
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 ---------------------------------------------------------------------------
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; AJ235272; CAA15034.1; -; Genomic_DNA.
DR PIR; H71663; H71663.
DR RefSeq; NP_220958.1; NC_000963.1.
DR RefSeq; WP_004597914.1; NC_000963.1.
DR PDB; 3D53; X-ray; 2.20 A; A/B/C/D/E/F=1-172.
DR PDB; 3EMJ; X-ray; 2.20 A; A/B/C/D/E/F/G/H/I/J/K/L=1-172.
DR PDBsum; 3D53; -.
DR PDBsum; 3EMJ; -.
DR AlphaFoldDB; Q9ZCW5; -.
DR SMR; Q9ZCW5; -.
DR STRING; 272947.RP589; -.
DR EnsemblBacteria; CAA15034; CAA15034; CAA15034.
DR GeneID; 57569715; -.
DR KEGG; rpr:RP589; -.
DR PATRIC; fig|272947.5.peg.606; -.
DR eggNOG; COG0221; Bacteria.
DR HOGENOM; CLU_073198_1_0_5; -.
DR OMA; DEPTFPG; -.
DR EvolutionaryTrace; Q9ZCW5; -.
DR Proteomes; UP000002480; 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 3D-structure; Cytoplasm; Hydrolase; Magnesium; Metal-binding;
KW Reference proteome.
FT CHAIN 1..172
FT /note="Inorganic pyrophosphatase"
FT /id="PRO_0000137529"
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"
FT HELIX 3..5
FT /evidence="ECO:0007829|PDB:3D53"
FT STRAND 15..21
FT /evidence="ECO:0007829|PDB:3D53"
FT STRAND 27..32
FT /evidence="ECO:0007829|PDB:3D53"
FT TURN 34..36
FT /evidence="ECO:0007829|PDB:3D53"
FT STRAND 39..44
FT /evidence="ECO:0007829|PDB:3D53"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:3EMJ"
FT STRAND 52..57
FT /evidence="ECO:0007829|PDB:3D53"
FT STRAND 70..73
FT /evidence="ECO:0007829|PDB:3D53"
FT STRAND 84..97
FT /evidence="ECO:0007829|PDB:3D53"
FT STRAND 100..109
FT /evidence="ECO:0007829|PDB:3D53"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:3D53"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:3D53"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:3D53"
FT HELIX 128..140
FT /evidence="ECO:0007829|PDB:3D53"
FT TURN 141..144
FT /evidence="ECO:0007829|PDB:3D53"
FT STRAND 150..156
FT /evidence="ECO:0007829|PDB:3D53"
FT HELIX 158..170
FT /evidence="ECO:0007829|PDB:3D53"
SQ SEQUENCE 172 AA; 19515 MW; 60248645842A13C5 CRC64;
MFIKKIKAKA NNNEINVIIE IPMNSGPIKY EFDKESGALF VDRFMQTTMS YPCNYGFIPD
TLSNDGDPVD VLVVAHHPVV PGSVIKCRAI GVLMMEDESG LDEKIIAVPT SKLDITFDHI
KELDDLCEML KKRIVHFFEH YKDLEKGKWV KVTGWGDKVK AETLIKEGID RN
