ID A0A549YIG0_9BACI Unreviewed; 315 AA.
AC A0A549YIG0; A0A5S3QLX7;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 18-JUN-2025, entry version 18.
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=FFL34_12880 {ECO:0000313|EMBL:TMN22880.1}, FH966_08230
GN {ECO:0000313|EMBL:TRM11671.1};
OS Lentibacillus cibarius.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC Lentibacillus.
OX NCBI_TaxID=2583219 {ECO:0000313|EMBL:TRM11671.1, ECO:0000313|Proteomes:UP000319280};
RN [1] {ECO:0000313|EMBL:TMN22880.1, ECO:0000313|Proteomes:UP000306980}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NKC220-2 {ECO:0000313|EMBL:TMN22880.1,
RC ECO:0000313|Proteomes:UP000306980};
RA Oh Y.J.;
RT "Genomic analysis of Lentibacillus sp. NKC220-2.";
RL Submitted (MAY-2019) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:TRM11671.1, ECO:0000313|Proteomes:UP000319280}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NKC851-2 {ECO:0000313|EMBL:TRM11671.1,
RC ECO:0000313|Proteomes:UP000319280};
RA Oh Y.J.;
RT "Genomic analysis of Lentibacillus sp. NKC851-2.";
RL Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=diphosphate + H2O = 2 phosphate + H(+); 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:ARBA00047820, 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:TRM11671.1}.
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; VCIA01000001; TMN22880.1; -; Genomic_DNA.
DR EMBL; VJMZ01000001; TRM11671.1; -; Genomic_DNA.
DR RefSeq; WP_138603776.1; NZ_VCIA01000001.1.
DR AlphaFoldDB; A0A549YIG0; -.
DR OrthoDB; 9766150at2; -.
DR Proteomes; UP000306980; Unassembled WGS sequence.
DR Proteomes; UP000319280; 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 FunFam; 3.10.310.20:FF:000001; Probable manganese-dependent inorganic pyrophosphatase; 1.
DR FunFam; 3.90.1640.10:FF:000001; Probable manganese-dependent inorganic pyrophosphatase; 1.
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 NCBIfam; NF003877; PRK05427.1; 1.
DR PANTHER; PTHR12112; BNIP - RELATED; 1.
DR PANTHER; PTHR12112:SF22; MANGANESE-DEPENDENT INORGANIC PYROPHOSPHATASE-RELATED; 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:UP000319280}.
FT DOMAIN 181..308
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 315 AA; 34687 MW; 122203CD0E4370B4 CRC64;
MDKTLIFGHK SPDTDSICSA LVYADLKKEL GVNAHPARLG EVNKETQFAL DYFGVEVPPL
IKKVDDDVKN VILVDHNEFQ QSVDNIQDVR ISEVIDHHRV SNFETKEPLY FRSEPVGCTA
TILNKMHKES GVIVSKKNAG LLLSAIISDS LLLKSPTCTQ VDIDAAHELA EIAGVDLETY
GLEMLKAGAD LSDKSAHDLI TMDAKEFTMG DAKVQIAQVN AVDTNQIYAS QAAIEKEMEQ
FISDKNLDLF LFVATDILNN DSDALALGSA KDNVEKAFDV TLDDNNRALL KGVVSRKKQI
VTKLTETFLS KTFTK
//
