ID A0A0R2CNJ7_9LACO Unreviewed; 306 AA.
AC A0A0R2CNJ7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=FC80_GL000562 {ECO:0000313|EMBL:KRM92810.1};
OS Liquorilactobacillus cacaonum DSM 21116.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Liquorilactobacillus.
OX NCBI_TaxID=1423729 {ECO:0000313|EMBL:KRM92810.1, ECO:0000313|Proteomes:UP000051131};
RN [1] {ECO:0000313|EMBL:KRM92810.1, ECO:0000313|Proteomes:UP000051131}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21116 {ECO:0000313|EMBL:KRM92810.1,
RC ECO:0000313|Proteomes:UP000051131};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRM92810.1}.
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DR EMBL; AYZE01000003; KRM92810.1; -; Genomic_DNA.
DR RefSeq; WP_057828185.1; NZ_AYZE01000003.1.
DR AlphaFoldDB; A0A0R2CNJ7; -.
DR STRING; 1423729.FC80_GL000562; -.
DR PATRIC; fig|1423729.3.peg.567; -.
DR OrthoDB; 9766150at2; -.
DR Proteomes; UP000051131; 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:UP000051131}.
FT DOMAIN 180..306
FT /note="DHHA2"
FT /evidence="ECO:0000259|SMART:SM01131"
FT BINDING 8
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00207"
FT BINDING 12
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="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00207"
FT BINDING 74
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00207"
FT BINDING 74
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00207"
FT BINDING 96
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00207"
FT BINDING 148
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00207"
SQ SEQUENCE 306 AA; 33446 MW; E54938F08E8309BB CRC64;
MKELVFGHKN PDTDAIVAAK AFAYLQNQLG GNVEAVALGT PNEETKFVLA NFAEDAPRVV
EKVSEEVEEV MLVDHNEAQQ SVDDIKDVTV THVVDHHRIA NFETSAPLYY YAEPVGCTST
IIFKLFKQNE VAVPAKLAGL MLSAIISDTL LFKSPTTTPA DELAVKELAK IAGVDYETYG
LEMLKAGTNL ASKSEKELIE ADAKSFEMGG KTVRIDQVNT VDLDEVFARE AALRSAIEEE
SAANGYDLFL LMVTNILDSN TRLLVVGEPK DVVEKAFDVK LNDDKAELPG VVSRKKQVVP
PLEKAF
//
