ID A0A1T4K7S9_9ENTE Unreviewed; 312 AA.
AC A0A1T4K7S9;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, 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=SAMN02745116_00134 {ECO:0000313|EMBL:SJZ38397.1};
OS Pilibacter termitis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae; Pilibacter.
OX NCBI_TaxID=263852 {ECO:0000313|EMBL:SJZ38397.1, ECO:0000313|Proteomes:UP000190328};
RN [1] {ECO:0000313|EMBL:SJZ38397.1, ECO:0000313|Proteomes:UP000190328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1030 {ECO:0000313|EMBL:SJZ38397.1,
RC ECO:0000313|Proteomes:UP000190328};
RA Peterson S.W.;
RL Submitted (FEB-2017) 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}.
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DR EMBL; FUXI01000001; SJZ38397.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T4K7S9; -.
DR STRING; 263852.SAMN02745116_00134; -.
DR OrthoDB; 9766150at2; -.
DR Proteomes; UP000190328; 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:UP000190328}.
FT DOMAIN 183..309
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 77
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00207"
FT BINDING 77
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00207"
FT BINDING 99
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00207"
FT BINDING 151
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; 34064 MW; 1EE76391E3F8C331 CRC64;
MSKIFVFGHQ NPDTDAIASS MAFAYLKAKE NNLPTEAVAL GEVNEETAFA LNYFDLTAPR
VVKRAKDEGV ETVILTDHNE FQQSIEDIEE LRILGVVDHH RIANFQTAEP LFYRAEPVGS
ASSIVYRMFK ETGIALPKNL AGMLLSGLIS DTLLLKSPTT HPTDLQVAKD LAEIAGVELE
KYGLEMLKAG TNLSTKSEEE LIDLDAKSFP LADKTVRVAQ VNTVDIEEVM TRQSALESAM
TSASAANGYD DFLLVVTDIV NSNSELLHVG QNGSLVEKAF NTTLANNRAF LEGVVSRKKQ
VVPQLTEAFG KV
//
