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Database: UniProt
Entry: A0A3E2J7Y3_9BACI
LinkDB: A0A3E2J7Y3_9BACI
Original site: A0A3E2J7Y3_9BACI 
ID   A0A3E2J7Y3_9BACI        Unreviewed;       310 AA.
AC   A0A3E2J7Y3;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   27-MAR-2024, entry version 16.
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=D0463_14575 {ECO:0000313|EMBL:RFU61730.1};
OS   Bacillus sp. V59.32b.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1758642 {ECO:0000313|EMBL:RFU61730.1, ECO:0000313|Proteomes:UP000258625};
RN   [1] {ECO:0000313|EMBL:RFU61730.1, ECO:0000313|Proteomes:UP000258625}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=V59.32a {ECO:0000313|EMBL:RFU61730.1,
RC   ECO:0000313|Proteomes:UP000258625};
RA   Seuylemezian A., Vaishampayan P.;
RT   "Bacillus chawlae sp. nov., Bacillus glennii sp. nov., and Bacillus saganii
RT   sp. nov. Isolated from the Vehicle Assembly Building at Kennedy Space
RT   Center where the Viking Spacecraft were Assembled.";
RL   Submitted (AUG-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:RFU61730.1}.
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DR   EMBL; QVTC01000061; RFU61730.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3E2J7Y3; -.
DR   OrthoDB; 9766150at2; -.
DR   Proteomes; UP000258625; 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}; Reference proteome {ECO:0000313|Proteomes:UP000258625}.
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="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         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   310 AA;  33766 MW;  04F170ACA9352B72 CRC64;
     MEKVLVFGHK NPDTDTICSA IAYAELKTKL GIDAEPVRLG QINGETQYAL DYFKAEAPRL
     VETVANEVDG VILVDHNERQ QSVSDLEKVQ VLEVIDHHRI ANFETSDPLY YRAEPVGCTA
     TILNKLYKEK GIEISKATAG LMLSAIISDS LLFKSPTCTD EDIQAARELA EIAGVDSESY
     GLEMLKAGAD LSDKTAKDLI SLDAKEFSMG SKKVEIAQVN AVDTNEVLAH QEELETVIAS
     VIAEKNLDLF LFVVTDILTN DSVALALGNA TQAVEKAYNV QLSNHTAVLK GVVSRKKQIV
     PVLTETFNAL
//
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