ID D8MJJ7_ERWBE Unreviewed; 302 AA.
AC D8MJJ7;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 65.
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 OrderedLocusNames=EbC_pEb10201070 {ECO:0000313|EMBL:CAX53385.1};
OS Erwinia billingiae (strain Eb661).
OG Plasmid pEB102 {ECO:0000313|EMBL:CAX53385.1,
OG ECO:0000313|Proteomes:UP000008793}.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=634500 {ECO:0000313|Proteomes:UP000008793};
RN [1] {ECO:0000313|EMBL:CAX53385.1, ECO:0000313|Proteomes:UP000008793}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Eb661 {ECO:0000313|EMBL:CAX53385.1,
RC ECO:0000313|Proteomes:UP000008793};
RC PLASMID=pEB102 {ECO:0000313|EMBL:CAX53385.1};
RX PubMed=20565991; DOI=10.1186/1471-2164-11-393;
RA Kube M., Migdoll A.M., Gehring I., Heitmann K., Mayer Y., Kuhl H.,
RA Knaust F., Geider K., Reinhardt R.;
RT "Genome comparison of the epiphytic bacteria Erwinia billingiae and E.
RT tasmaniensis with the pear pathogen E. pyrifoliae.";
RL BMC Genomics 11:393-393(2010).
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};
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DR EMBL; FP236826; CAX53385.1; -; Genomic_DNA.
DR RefSeq; WP_010260815.1; NC_014304.1.
DR AlphaFoldDB; D8MJJ7; -.
DR KEGG; ebi:EbC_pEb10201070; -.
DR eggNOG; COG1227; Bacteria.
DR HOGENOM; CLU_025243_0_1_6; -.
DR Proteomes; UP000008793; Plasmid pEB102.
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};
KW Plasmid {ECO:0000313|EMBL:CAX53385.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008793}.
FT DOMAIN 179..295
FT /note="DHHA2"
FT /evidence="ECO:0000259|SMART:SM01131"
SQ SEQUENCE 302 AA; 32719 MW; 840E490157D2F7E6 CRC64;
MIHVFGHINP DSDAICTAFV TAHWLTGRGM DARAWRLGEA NRETHFIFDT AGLTLPPRLD
IPLQDERVWL VDFTEPAQGP DDLLRSNIVG ITDHHRLGGL ITQLPPEVHI RPLGSSATLL
WLLMNAEARR TLPPTLAILL LGALLSDTVN LRSPTTTEDD IRSATELGVL SGVNRRAFAR
DLLTAKTDVS GLSAQLLLDR DLKAFVIAGT DVRIAQIEVS SPSQVATVMD DLLAALAYLA
DQSGAGLAVL MLTDIRAGFS TLYFAGRESV NAASCSVPGM LSRKKQLLPW LESRLNQNGS
SL
//
