PPAC_BACC7
ID PPAC_BACC7 Reviewed; 309 AA.
AC B7HUD5;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Probable manganese-dependent inorganic pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_00207};
DE EC=3.6.1.1 {ECO:0000255|HAMAP-Rule:MF_00207};
DE AltName: Full=Pyrophosphate phospho-hydrolase {ECO:0000255|HAMAP-Rule:MF_00207};
DE Short=PPase {ECO:0000255|HAMAP-Rule:MF_00207};
GN Name=ppaC {ECO:0000255|HAMAP-Rule:MF_00207};
GN OrderedLocusNames=BCAH187_A2875;
OS Bacillus cereus (strain AH187).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=405534;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AH187;
RA Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Kolsto A.B.,
RA Okstad O.A., Ravel J., Sutton G.;
RT "Genome sequence of Bacillus cereus AH187.";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
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_00207};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00207};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00207};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00207}.
CC -!- SIMILARITY: Belongs to the PPase class C family. {ECO:0000255|HAMAP-
CC Rule:MF_00207}.
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DR EMBL; CP001177; ACJ81335.1; -; Genomic_DNA.
DR RefSeq; WP_000416843.1; NC_011658.1.
DR AlphaFoldDB; B7HUD5; -.
DR SMR; B7HUD5; -.
DR EnsemblBacteria; ACJ81335; ACJ81335; BCAH187_A2875.
DR KEGG; bcr:BCAH187_A2875; -.
DR HOGENOM; CLU_025243_0_1_9; -.
DR OMA; IMLCAIL; -.
DR OrthoDB; 732679at2; -.
DR Proteomes; UP000002214; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004427; F:inorganic diphosphatase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR Gene3D; 3.10.310.20; -; 1.
DR HAMAP; MF_00207; PPase_C; 1.
DR InterPro; IPR001667; DDH_dom.
DR InterPro; IPR038763; DHH_sf.
DR InterPro; IPR004097; DHHA2.
DR InterPro; IPR038222; DHHA2_dom_sf.
DR InterPro; IPR022934; Mn-dep_inorganic_PyrPase.
DR Pfam; PF01368; DHH; 1.
DR Pfam; PF02833; DHHA2; 1.
DR SMART; SM01131; DHHA2; 1.
DR SUPFAM; SSF64182; SSF64182; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Hydrolase; Manganese; Metal-binding.
FT CHAIN 1..309
FT /note="Probable manganese-dependent inorganic
FT pyrophosphatase"
FT /id="PRO_1000192513"
FT BINDING 9
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00207"
FT BINDING 13
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00207"
FT BINDING 15
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00207"
FT BINDING 75
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00207"
FT BINDING 75
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00207"
FT BINDING 97
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00207"
FT BINDING 149
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00207"
SQ SEQUENCE 309 AA; 33763 MW; CC781E0E7F20DE1F CRC64;
MEKVLVFGHK NPDTDAICSA IAYAELKKEL GMNAEPVRLG EISGETQFAL DYFKVEGPRF
VETVANEVDN VILVDHNERQ QSANDIESVR VLEVIDHHRI ANFETSDPIY YRCEPVGCTA
TILNKMYKEN GITIRKEVAG LMLSAIISDS LLFKSPTCTE QDVAAARELA EIAGVDADKY
GLEMLKAGAD LSGKTMEQLI SLDAKEFQMG NAKVEIAQVN AVDTNDVLVH QAELEKVISA
VVEEKGLDLF LFVVTDILTN DSVGLAIGKA ANIVEKAYNV SLENNTATLK GVVSRKKQIV
PVLTEAFQA
