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Database: UniProt
Entry: A0A0G0J6J5_9BACT
LinkDB: A0A0G0J6J5_9BACT
Original site: A0A0G0J6J5_9BACT 
ID   A0A0G0J6J5_9BACT        Unreviewed;       309 AA.
AC   A0A0G0J6J5;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=inorganic diphosphatase {ECO:0000256|ARBA:ARBA00012146};
DE            EC=3.6.1.1 {ECO:0000256|ARBA:ARBA00012146};
DE   AltName: Full=Pyrophosphate phospho-hydrolase {ECO:0000256|ARBA:ARBA00032535};
GN   ORFNames=US82_C0003G0037 {ECO:0000313|EMBL:KKQ63088.1};
OS   Parcubacteria group bacterium GW2011_GWC1_38_22.
OC   Bacteria.
OX   NCBI_TaxID=1618897 {ECO:0000313|EMBL:KKQ63088.1, ECO:0000313|Proteomes:UP000034773};
RN   [1] {ECO:0000313|EMBL:KKQ63088.1, ECO:0000313|Proteomes:UP000034773}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(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};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
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:KKQ63088.1}.
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DR   EMBL; LBUL01000003; KKQ63088.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0J6J5; -.
DR   STRING; 1618897.US82_C0003G0037; -.
DR   PATRIC; fig|1618897.3.peg.146; -.
DR   Proteomes; UP000034773; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004427; F:inorganic diphosphate phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.310.20; DHHA2 domain; 1.
DR   Gene3D; 3.90.1640.10; inorganic pyrophosphatase (n-terminal core); 1.
DR   InterPro; IPR001667; DDH_dom.
DR   InterPro; IPR038763; DHH_sf.
DR   InterPro; IPR004097; DHHA2.
DR   InterPro; IPR038222; DHHA2_dom_sf.
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   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          180..307
FT                   /note="DHHA2"
FT                   /evidence="ECO:0000259|SMART:SM01131"
SQ   SEQUENCE   309 AA;  34709 MW;  151C3C3DC7E9BEDC CRC64;
     MSKIIIVGHK NPDTDSVVSS IAAQEYFEKV LGKESKAYCA GMLNNETKFI LEKLEVEIPK
     LFEKIEDDEC AAIVDHNQPS QIVDGLDYGK IEYIFDHHNL NIVTEKPIFV RVEPIGSTSS
     LIAKMFFEKG ITPSEVTSKL LLSGILSDML NFTSPTTTDE DRKLADKLNE IAKLDMQEFV
     TEMFKAKSSL EGISIEDVIT LDYKTFEMGS KNVGIGTWET TLPESVNIKK DEIFAALEKK
     KALENLDYMF FMVVDILQGN CQLYIIGDAE KELAEKVFGK EAENKLMTLP GVVSRKKQIV
     PQLTEELSK
//
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