ID A0A1S8MDE7_9CLOT Unreviewed; 310 AA.
AC A0A1S8MDE7;
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 ECO:0000313|EMBL:OOL85346.1};
GN ORFNames=CLAUR_008870 {ECO:0000313|EMBL:URZ00899.1}, CROST_021070
GN {ECO:0000313|EMBL:URZ11390.1}, CROST_36870
GN {ECO:0000313|EMBL:OOL85346.1};
OS Clostridium felsineum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=36839 {ECO:0000313|EMBL:OOL85346.1};
RN [1] {ECO:0000313|EMBL:OOL85346.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7320 {ECO:0000313|EMBL:OOL85346.1};
RA Poehlein A., Montoya Solano J.D., Flitsch S., Krabben P., Duerre P.,
RA Daniel R.;
RT "Microbial solvent formation.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:URZ11390.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 7320 {ECO:0000313|EMBL:URZ11390.1};
RA Poehlein A., Schoch T., Duerre P., Daniel R.;
RT "Genome sequence of C. roseum typestrain.";
RL Submitted (APR-2022) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:URZ00899.1, ECO:0000313|Proteomes:UP000190175}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 793 {ECO:0000313|EMBL:URZ00899.1,
RC ECO:0000313|Proteomes:UP000190175};
RA Poehlein A., Schoch T., Duerre P., Daniel R.;
RT "Genome sequence of Clostridium aurantibutyricum DSM 793.";
RL Submitted (APR-2022) 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; LZYV01000094; OOL85346.1; -; Genomic_DNA.
DR EMBL; CP096988; URZ00899.1; -; Genomic_DNA.
DR EMBL; CP096983; URZ11390.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S8MDE7; -.
DR STRING; 84029.CROST_36870; -.
DR KEGG; caun:CLAUR_008870; -.
DR KEGG; crw:CROST_021070; -.
DR Proteomes; UP000190175; Chromosome.
DR Proteomes; UP000190951; Chromosome.
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 10
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00207"
FT BINDING 14
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00207"
FT BINDING 16
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 310 AA; 34545 MW; 9672EF5331B5A465 CRC64;
MENIIYISGH KNPDTDSICS AIAYSELKNK LGFNTVPARL GNVSRETQFA LDYFKVDAPK
LVENLSENQD LILVDHNERS QSIDNLEALH LLEIIDHHRI ADIQTSYPIF FRNEPVGCSS
TIIGSMYFEK GITPSKEAAG LMCSAIISDT LLFRSPTTTD RDKEVLKKLA EIADIDPEKY
ASEMFKAGTS LKGKTVEEIF NSDYKVFNLG DKKVGVSQVT TMDIEGFDEY KKDMLAYMDK
KVKDESFNVV LLLLTDIIKE GSLLIATGED TAIVNKAFNV ELKDNSVYVP GILSRKKQVI
PPLTSAIEAK
//
