IPYR_HELPY
ID IPYR_HELPY Reviewed; 173 AA.
AC P56153;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 126.
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=HP_0620;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=PP34A2;
RA Dailide G., Ogura M., Dailidiene D., Berg D.E.;
RT "Geographic partioning in Helicobacter pylori: gene pools of Spain and Peru
RT are closely related, and distinct from those of Japan.";
RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
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; AY153259; AAN74434.1; -; Genomic_DNA.
DR EMBL; AE000511; AAD07684.1; -; Genomic_DNA.
DR PIR; D64597; D64597.
DR RefSeq; NP_207414.1; NC_000915.1.
DR RefSeq; WP_001047373.1; NC_018939.1.
DR PDB; 1YGZ; X-ray; 2.60 A; A/B/C/D/E/F=1-173.
DR PDB; 2BQX; X-ray; 1.90 A; A=1-173.
DR PDB; 2BQY; X-ray; 2.30 A; A=1-173.
DR PDBsum; 1YGZ; -.
DR PDBsum; 2BQX; -.
DR PDBsum; 2BQY; -.
DR AlphaFoldDB; P56153; -.
DR SMR; P56153; -.
DR DIP; DIP-3464N; -.
DR IntAct; P56153; 2.
DR MINT; P56153; -.
DR STRING; 85962.C694_03210; -.
DR PaxDb; P56153; -.
DR EnsemblBacteria; AAD07684; AAD07684; HP_0620.
DR KEGG; hpy:HP_0620; -.
DR PATRIC; fig|85962.47.peg.669; -.
DR eggNOG; COG0221; Bacteria.
DR OMA; DEPTFPG; -.
DR PhylomeDB; P56153; -.
DR BRENDA; 3.6.1.1; 2604.
DR EvolutionaryTrace; P56153; -.
DR Proteomes; UP000000429; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004427; F:inorganic diphosphatase activity; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central.
DR GO; GO:0006796; P:phosphate-containing compound metabolic process; IBA:GO_Central.
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..173
FT /note="Inorganic pyrophosphatase"
FT /id="PRO_0000137501"
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 140
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00209"
FT HELIX 3..5
FT /evidence="ECO:0007829|PDB:1YGZ"
FT STRAND 14..21
FT /evidence="ECO:0007829|PDB:2BQX"
FT STRAND 26..31
FT /evidence="ECO:0007829|PDB:2BQX"
FT TURN 33..35
FT /evidence="ECO:0007829|PDB:2BQX"
FT STRAND 38..43
FT /evidence="ECO:0007829|PDB:2BQX"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:2BQX"
FT STRAND 51..56
FT /evidence="ECO:0007829|PDB:2BQX"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:2BQX"
FT STRAND 83..96
FT /evidence="ECO:0007829|PDB:2BQX"
FT STRAND 99..108
FT /evidence="ECO:0007829|PDB:2BQX"
FT TURN 110..112
FT /evidence="ECO:0007829|PDB:2BQX"
FT TURN 115..118
FT /evidence="ECO:0007829|PDB:2BQX"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:2BQX"
FT HELIX 127..139
FT /evidence="ECO:0007829|PDB:2BQX"
FT TURN 140..143
FT /evidence="ECO:0007829|PDB:2BQX"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:1YGZ"
FT STRAND 149..156
FT /evidence="ECO:0007829|PDB:2BQX"
FT HELIX 157..171
FT /evidence="ECO:0007829|PDB:2BQX"
SQ SEQUENCE 173 AA; 19272 MW; 23A51C685A6EC7F2 CRC64;
MNLEKLEVSH DADSLCVVIE ISKHSNIKYE LDKESGALMV DRVLYGAQNY PANYGFVPNT
LGSDGDPVDA LVLSDVAFQA GSVVKARLVG VLNMEDESGM DEKLIALPID KIDPTHSYVK
DIDDLSKHTL DKIKHFFETY KDLEPNKWVK VKGFENKESA IKVLEKAIKA YQG
