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PPAC_LACDA
ID   PPAC_LACDA              Reviewed;         311 AA.
AC   Q1GAB5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Probable manganese-dependent inorganic pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_00207};
DE            EC=3.6.1.1 {ECO:0000255|HAMAP-Rule:MF_00207};
DE   AltName: Full=Pyrophosphate phospho-hydrolase {ECO:0000255|HAMAP-Rule:MF_00207};
DE            Short=PPase {ECO:0000255|HAMAP-Rule:MF_00207};
GN   Name=ppaC {ECO:0000255|HAMAP-Rule:MF_00207}; OrderedLocusNames=Ldb0995;
OS   Lactobacillus delbrueckii subsp. bulgaricus (strain ATCC 11842 / DSM 20081
OS   / BCRC 10696 / JCM 1002 / NBRC 13953 / NCIMB 11778 / NCTC 12712 / WDCM
OS   00102 / Lb 14).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=390333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11842 / DSM 20081 / BCRC 10696 / JCM 1002 / NBRC 13953 / NCIMB
RC   11778 / NCTC 12712 / WDCM 00102 / Lb 14;
RX   PubMed=16754859; DOI=10.1073/pnas.0603024103;
RA   van de Guchte M., Penaud S., Grimaldi C., Barbe V., Bryson K., Nicolas P.,
RA   Robert C., Oztas S., Mangenot S., Couloux A., Loux V., Dervyn R., Bossy R.,
RA   Bolotin A., Batto J.-M., Walunas T., Gibrat J.-F., Bessieres P.,
RA   Weissenbach J., Ehrlich S.D., Maguin E.;
RT   "The complete genome sequence of Lactobacillus bulgaricus reveals extensive
RT   and ongoing reductive evolution.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:9274-9279(2006).
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00207};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00207};
CC       Note=Binds 2 manganese ions per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00207};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00207}.
CC   -!- SIMILARITY: Belongs to the PPase class C family. {ECO:0000255|HAMAP-
CC       Rule:MF_00207}.
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DR   EMBL; CR954253; CAI97797.1; -; Genomic_DNA.
DR   RefSeq; WP_003620120.1; NZ_JQAV01000012.1.
DR   AlphaFoldDB; Q1GAB5; -.
DR   SMR; Q1GAB5; -.
DR   STRING; 390333.Ldb0995; -.
DR   EnsemblBacteria; CAI97797; CAI97797; Ldb0995.
DR   GeneID; 66399908; -.
DR   KEGG; ldb:Ldb0995; -.
DR   PATRIC; fig|390333.13.peg.591; -.
DR   eggNOG; COG1227; Bacteria.
DR   HOGENOM; CLU_025243_0_1_9; -.
DR   OMA; IMLCAIL; -.
DR   BioCyc; LDEL390333:LDB_RS04345-MON; -.
DR   Proteomes; UP000001259; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004427; F:inorganic diphosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.10.310.20; -; 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   Pfam; PF01368; DHH; 1.
DR   Pfam; PF02833; DHHA2; 1.
DR   SMART; SM01131; DHHA2; 1.
DR   SUPFAM; SSF64182; SSF64182; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Hydrolase; Manganese; Metal-binding; Reference proteome.
FT   CHAIN           1..311
FT                   /note="Probable manganese-dependent inorganic
FT                   pyrophosphatase"
FT                   /id="PRO_1000012313"
FT   BINDING         9
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00207"
FT   BINDING         13
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00207"
FT   BINDING         15
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00207"
FT   BINDING         75
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00207"
FT   BINDING         75
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00207"
FT   BINDING         97
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00207"
FT   BINDING         149
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00207"
SQ   SEQUENCE   311 AA;  34282 MW;  21515C36173C901D CRC64;
     MEKELIFGHR NPDTDAIGTA IAYSYFQNQH GYNTEAVALG EANDETSFAL KKFGFEAPRV
     VKTVANEVKA IMLVDHNEPQ QSVEDRDQVK VTHVIDHHRI SNFATIDPLF YRAEPVGCTS
     TVLWEMFKEQ NMEIPANIAG IMLSAIISDT LLLKSPTTTD IDKEAVEELA KIAGVDYKEY
     GLELLKAGTN IAAKSVEELI DLDAKSFELG SKTARIAQVN VVDVPEALER KDAFLAAMEK
     DAKANGYDLF MLVITNVLDS DSEVLFIGDD ESKSVFAKAF GKELVDSEAH LPGVVSRKKQ
     IVPPLTRAFE A
 
 
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