PPAC_STRA3
ID PPAC_STRA3 Reviewed; 311 AA.
AC Q8E4D4;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=gbs1467;
OS Streptococcus agalactiae serotype III (strain NEM316).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=211110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEM316;
RX PubMed=12354221; DOI=10.1046/j.1365-2958.2002.03126.x;
RA Glaser P., Rusniok C., Buchrieser C., Chevalier F., Frangeul L., Msadek T.,
RA Zouine M., Couve E., Lalioui L., Poyart C., Trieu-Cuot P., Kunst F.;
RT "Genome sequence of Streptococcus agalactiae, a pathogen causing invasive
RT neonatal disease.";
RL Mol. Microbiol. 45:1499-1513(2002).
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; AL766851; CAD47126.1; -; Genomic_DNA.
DR RefSeq; WP_000036015.1; NC_004368.1.
DR AlphaFoldDB; Q8E4D4; -.
DR SMR; Q8E4D4; -.
DR STRING; 211110.gbs1467; -.
DR EnsemblBacteria; CAD47126; CAD47126; CAD47126.
DR KEGG; san:gbs1467; -.
DR eggNOG; COG1227; Bacteria.
DR HOGENOM; CLU_025243_0_1_9; -.
DR OMA; IMLCAIL; -.
DR Proteomes; UP000000823; 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.
FT CHAIN 1..311
FT /note="Probable manganese-dependent inorganic
FT pyrophosphatase"
FT /id="PRO_0000158587"
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 77
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00207"
FT BINDING 77
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00207"
FT BINDING 99
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00207"
FT BINDING 151
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; 33597 MW; 5EAE5E0A9245EAB4 CRC64;
MSKILVFGHQ NPDSDAIGSS VAFAYLAKEA WGLDTEAVAL GTPNEETAYV LDYFGVQAPR
VVESAKAEGV ETVILTDHNE FQQSISDIKD VTVYGVVDHH RVANFETANP LYMRLEPVGS
ASSIVYRMFK ENGVSVPKEL AGLLLSGLIS DTLLLKSPTT HASDIPVAKE LAEIAGVNLE
EYGLEMLKAG TNLSSKTAAE LIDIDAKTFE LNGEAVRVAQ VNTVDINDIL ARQEEIEVAI
QEAIVTEGYS DFVLMITDIV NSNSEILALG SNMAKVEAAF EFTLENNHAF LAGAVSRKKQ
VVPQLTESYN A