ID   A0A418SWQ7_9RHOB        Unreviewed;       305 AA.
AC   A0A418SWQ7;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 12.
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=D3P04_10310 {ECO:0000313|EMBL:RJE85397.1};
OS   Paracoccus onubensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Paracoccus.
OX   NCBI_TaxID=1675788 {ECO:0000313|EMBL:RJE85397.1, ECO:0000313|Proteomes:UP000284202};
RN   [1] {ECO:0000313|Proteomes:UP000284202}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1011MAR3C25 {ECO:0000313|Proteomes:UP000284202};
RA   Jurado V., Gutierrez-Patricio S., Gonzalez-Pimentel J.L., Miller A.Z.,
RA   Laiz L., Saiz-Jimenez C.;
RT   "Acidovorax cavernicola nov. sp. isolated from Gruta de las Maravillas
RT   (Aracena, Spain).";
RL   Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
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:RJE85397.1}.
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DR   EMBL; QZCG01000006; RJE85397.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A418SWQ7; -.
DR   OrthoDB; 9766150at2; -.
DR   Proteomes; UP000284202; 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, ECO:0000313|EMBL:RJE85397.1};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000284202}.
FT   DOMAIN          180..305
FT                   /note="DHHA2"
FT                   /evidence="ECO:0000259|SMART:SM01131"
SQ   SEQUENCE   305 AA;  33333 MW;  4CE598515A4CDD02 CRC64;
     MIKVFGHIAP DTDSTGSPII WAWYLNEIRQ TPAKAVLQGE PNTEAAWMLE RWGLDKPEII
     TDVAAGEQCV IVDTNNPAEL PASINEAEVI EIIDHHMLAG GVKTRTPINI TIRPLACTAT
     IMHDLIGEDL AKAPEGVKGA MLTCILSDTL EFRSPTTTPH DREVAEKIAR ELGIIISEYA
     AEMFAAKSDV SVFSEEELLR MDSKEFEIDG RKLRISVLET TAPQVLLDRK QALMDAMPGV
     AESDGADEVI LFIIDILKEE ATLLVPNDAV KEIAEKSFDV TVNGDSIVLP GVMSRKKQII
     PVLAV
//