PPAC_LISMC
ID PPAC_LISMC Reviewed; 308 AA.
AC C1KV95;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 58.
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=Lm4b_01458;
OS Listeria monocytogenes serotype 4b (strain CLIP80459).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=568819;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIP80459;
RX PubMed=22530965; DOI=10.1186/1471-2164-13-144;
RA Hain T., Ghai R., Billion A., Kuenne C.T., Steinweg C., Izar B.,
RA Mohamed W., Mraheil M., Domann E., Schaffrath S., Karst U., Goesmann A.,
RA Oehm S., Puhler A., Merkl R., Vorwerk S., Glaser P., Garrido P.,
RA Rusniok C., Buchrieser C., Goebel W., Chakraborty T.;
RT "Comparative genomics and transcriptomics of lineages I, II, and III
RT strains of Listeria monocytogenes.";
RL BMC Genomics 13:144-144(2012).
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; FM242711; CAS05220.1; -; Genomic_DNA.
DR RefSeq; WP_003727434.1; NC_012488.1.
DR AlphaFoldDB; C1KV95; -.
DR SMR; C1KV95; -.
DR KEGG; lmc:Lm4b_01458; -.
DR HOGENOM; CLU_025243_0_1_9; -.
DR OMA; IMLCAIL; -.
DR BioCyc; LMON568819:LM4B_RS07270-MON; -.
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.
FT CHAIN 1..308
FT /note="Probable manganese-dependent inorganic
FT pyrophosphatase"
FT /id="PRO_1000204161"
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 308 AA; 33761 MW; D367C1C23FE54DD3 CRC64;
MTKTLVFGHK NPDTDTICSA ISYAELKKAQ GADIEAVRLG ELNSETAFVL DYFQVTAPRL
VQTVANEVSE VALVDHNERQ QSVDDIDDVT VTAVVDHHRI ANFETSDPLY YRAEPVGCTT
TILLKMFREN EVEVSKTVAG LMLSAIISDT LLFQSPTCTE EDKVAAQKLA QIADVDIQSY
GMEMLKAGAD VSKKTVAELL LDAKEFNMND NKVEIAQINV VDVNDVLSRR AEVEALMTQN
IVDKGLDLYL FVITNILTND SVGIAIGSKT AVVEEAYGVK FVENQAPLKG VVSRKKQVVP
ILTDTFAK
