ID A0A176JA18_9BACI Unreviewed; 312 AA.
AC A0A176JA18;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=AS29_004315 {ECO:0000313|EMBL:KZZ85820.1};
OS Bacillus sp. SJS.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1423321 {ECO:0000313|EMBL:KZZ85820.1, ECO:0000313|Proteomes:UP000028527};
RN [1] {ECO:0000313|EMBL:KZZ85820.1, ECO:0000313|Proteomes:UP000028527}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SJS {ECO:0000313|EMBL:KZZ85820.1,
RC ECO:0000313|Proteomes:UP000028527};
RA Newman J.D., Stropko S.J., Pipes S.E.;
RT "Bacillus sp. SJS genome.";
RL Submitted (APR-2016) 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:KZZ85820.1}.
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DR EMBL; JAQV02000007; KZZ85820.1; -; Genomic_DNA.
DR RefSeq; WP_035409850.1; NZ_JAQV02000007.1.
DR AlphaFoldDB; A0A176JA18; -.
DR STRING; 1423321.AS29_004315; -.
DR eggNOG; COG1227; Bacteria.
DR OrthoDB; 9766150at2; -.
DR Proteomes; UP000028527; 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:UP000028527}.
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 312 AA; 34224 MW; FDCFB3D89B82A7CF CRC64;
MEKVLVFGHK NPDTDTICSS IAYAELKNKL GMNAEPVRLG SINGETQYAL DTFNKQAPRL
VEKVAAEVNH VILVDHNERQ QSADDITEVS VLEVIDHHRI ANFETSDPLY YRAEPVGCTT
TILNKMYKEN GVEIEKDTAG LMLSAIISDS LLFKSPTCTE QDIAAAKELA EIAGVNLESY
GLEMLKAGAD LSSKTVEELI SLDAKEFQMG TRRVEIAQVN AVDPNDILVR QSEIEAAIAH
VVAEKGLDLF LFVVTDILES DSIALASGRE VEAVERAYNV KIEDSRALLK GVVSRKKQIV
PILTETFSST NS
//
