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Database: UniProt
Entry: A0A2P8G493_9BACL
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ID   A0A2P8G493_9BACL        Unreviewed;       308 AA.
AC   A0A2P8G493;
DT   23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Probable manganese-dependent inorganic pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_00207};
DE            EC=3.6.1.1 {ECO:0000256|HAMAP-Rule:MF_00207};
DE   AltName: Full=Pyrophosphate phospho-hydrolase {ECO:0000256|HAMAP-Rule:MF_00207};
DE            Short=PPase {ECO:0000256|HAMAP-Rule:MF_00207};
GN   Name=ppaC {ECO:0000256|HAMAP-Rule:MF_00207};
GN   ORFNames=B0H99_1152 {ECO:0000313|EMBL:PSL28789.1};
OS   Planomicrobium soli.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Planomicrobium.
OX   NCBI_TaxID=1176648 {ECO:0000313|EMBL:PSL28789.1, ECO:0000313|Proteomes:UP000242682};
RN   [1] {ECO:0000313|EMBL:PSL28789.1, ECO:0000313|Proteomes:UP000242682}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.12259 {ECO:0000313|EMBL:PSL28789.1,
RC   ECO:0000313|Proteomes:UP000242682};
RA   Whitman W.;
RT   "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT   soil and plant-associated and newly described type strains.";
RL   Submitted (MAR-2018) 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;
CC         Evidence={ECO:0000256|ARBA:ARBA00000926, ECO:0000256|HAMAP-
CC         Rule:MF_00207};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00207};
CC       Note=Binds 2 manganese ions per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00207};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_00207}.
CC   -!- SIMILARITY: Belongs to the PPase class C family.
CC       {ECO:0000256|ARBA:ARBA00007350, ECO:0000256|HAMAP-Rule:MF_00207}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PSL28789.1}.
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DR   EMBL; PYAT01000015; PSL28789.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2P8G493; -.
DR   OrthoDB; 9766150at2; -.
DR   Proteomes; UP000242682; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004427; F:inorganic diphosphate phosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.10.310.20; DHHA2 domain; 1.
DR   Gene3D; 3.90.1640.10; inorganic pyrophosphatase (n-terminal core); 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   PANTHER; PTHR12112; BNIP - RELATED; 1.
DR   PANTHER; PTHR12112:SF22; MANGANESE-DEPENDENT INORGANIC PYROPHOSPHATASE; 1.
DR   Pfam; PF01368; DHH; 1.
DR   Pfam; PF02833; DHHA2; 1.
DR   SMART; SM01131; DHHA2; 1.
DR   SUPFAM; SSF64182; DHH phosphoesterases; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00207};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00207};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_00207};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00207}.
FT   DOMAIN          181..307
FT                   /note="DHHA2"
FT                   /evidence="ECO:0000259|SMART:SM01131"
FT   BINDING         9
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00207"
FT   BINDING         13
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00207"
FT   BINDING         15
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00207"
FT   BINDING         75
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00207"
FT   BINDING         75
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00207"
FT   BINDING         97
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00207"
FT   BINDING         149
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00207"
SQ   SEQUENCE   308 AA;  33685 MW;  DD892E050D5A3C0E CRC64;
     MSKIFVLGHK NPDTDSICSA ISYAYLKNEI GMDVEPIRLG ELNNETLYAL EQFNFEHPRL
     VTRVSAEASQ VILVDHNERQ QSAEDINEVQ VIEVIDHHRI ANFETVDPLY FRAEPVGCTA
     TILLKLFKEN GVAVPANIAG LMLSAIISDS LLFKSPTCTQ QDIHAARELA ELAGVDAAEY
     GLAMLKAGAD LSNKTLEDLM SLDSKEFEAG AHHFEVAQVN AIGVDDVISR QKELEVLMEQ
     VITKKGLSLF LFVVTDILNN DSVGIVLGEQ AGIVESAFKS SVVDNRVLLP GVVSRKKQIV
     PVITEALS
//
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