ID Q72BJ9_DESVH Unreviewed; 306 AA.
AC Q72BJ9;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 111.
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 Name=ppaC {ECO:0000313|EMBL:AAS96114.1};
GN OrderedLocusNames=DVU_1636 {ECO:0000313|EMBL:AAS96114.1};
OS Desulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / NCIMB 8303 / VKM
OS B-1760 / Hildenborough).
OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC Desulfovibrionaceae; Nitratidesulfovibrio.
OX NCBI_TaxID=882 {ECO:0000313|EMBL:AAS96114.1, ECO:0000313|Proteomes:UP000002194};
RN [1] {ECO:0000313|EMBL:AAS96114.1, ECO:0000313|Proteomes:UP000002194}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough
RC {ECO:0000313|Proteomes:UP000002194};
RX PubMed=15077118; DOI=10.1038/nbt959;
RA Heidelberg J.F., Seshadri R., Haveman S.A., Hemme C.L., Paulsen I.T.,
RA Kolonay J.F., Eisen J.A., Ward N., Methe B., Brinkac L.M., Daugherty S.C.,
RA Deboy R.T., Dodson R.J., Durkin A.S., Madupu R., Nelson W.C.,
RA Sullivan S.A., Fouts D., Haft D.H., Selengut J., Peterson J.D.,
RA Davidsen T.M., Zafar N., Zhou L., Radune D., Dimitrov G., Hance M.,
RA Tran K., Khouri H., Gill J., Utterback T.R., Feldblyum T.V., Wall J.D.,
RA Voordouw G., Fraser C.M.;
RT "The genome sequence of the anaerobic, sulfate-reducing bacterium
RT Desulfovibrio vulgaris Hildenborough.";
RL Nat. Biotechnol. 22:554-559(2004).
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; AE017285; AAS96114.1; -; Genomic_DNA.
DR RefSeq; WP_010938927.1; NZ_CABHLV010000001.1.
DR RefSeq; YP_010855.1; NC_002937.3.
DR AlphaFoldDB; Q72BJ9; -.
DR SMR; Q72BJ9; -.
DR STRING; 882.DVU_1636; -.
DR PaxDb; 882-DVU_1636; -.
DR EnsemblBacteria; AAS96114; AAS96114; DVU_1636.
DR KEGG; dvu:DVU_1636; -.
DR PATRIC; fig|882.5.peg.1511; -.
DR eggNOG; COG1227; Bacteria.
DR HOGENOM; CLU_025243_0_1_7; -.
DR OrthoDB; 9766150at2; -.
DR PhylomeDB; Q72BJ9; -.
DR Proteomes; UP000002194; Chromosome.
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:AAS96114.1};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000002194}.
FT DOMAIN 179..304
FT /note="DHHA2"
FT /evidence="ECO:0000259|SMART:SM01131"
SQ SEQUENCE 306 AA; 32673 MW; 48EB89D19303AF1D CRC64;
MAVLVLGHMN PDTDSIIAAI GVADLMTKRG VAAKAVAQGA PTPESTFVLE KFGLTAPEVV
SSVAGQKVIL VDTTERAQLP ADLGDAEILG VVDHHKLGDV TTPNPLEMWV WPVGCTGTVI
KAMYDFYGIE VPKGIAGGLL CAILSDTVMF KSVTCTPQDK KAVEELAKIA GVADVMALGM
DMFKVKSAVE GASMKDLVFR DYKDFDMNGN KVGIGQLEVV DLSILEPVKA GLYEEITRVK
GEGRHSVFLL LTDIMKEGSE MLIVSDDPSK VEAAFGVKPE GTSVWLDGVM SRKKQVVPNF
EKAFKG
//
