ID Q6AL66_DESPS Unreviewed; 319 AA.
AC Q6AL66;
DT 13-SEP-2004, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2004, sequence version 1.
DT 24-JAN-2024, entry version 90.
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=DP2180 {ECO:0000313|EMBL:CAG36909.1};
OS Desulfotalea psychrophila (strain LSv54 / DSM 12343).
OC Bacteria; Thermodesulfobacteriota; Desulfobulbia; Desulfobulbales;
OC Desulfocapsaceae; Desulfotalea.
OX NCBI_TaxID=177439 {ECO:0000313|EMBL:CAG36909.1, ECO:0000313|Proteomes:UP000000602};
RN [1] {ECO:0000313|Proteomes:UP000000602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12343 / LSv54 {ECO:0000313|Proteomes:UP000000602};
RX PubMed=15305914; DOI=10.1111/j.1462-2920.2004.00665.x;
RA Rabus R., Ruepp A., Frickey T., Rattei T., Fartmann B., Stark M., Bauer M.,
RA Zibat A., Lombardot T., Becker I., Amann J., Gellner K., Teeling H.,
RA Leuschner W.D., Gloeckner F.-O., Lupas A.N., Amann R., Klenk H.-P.;
RT "The genome of Desulfotalea psychrophila, a sulfate-reducing bacterium from
RT permanently cold Arctic sediments.";
RL Environ. Microbiol. 6:887-902(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; CR522870; CAG36909.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6AL66; -.
DR STRING; 177439.DP2180; -.
DR KEGG; dps:DP2180; -.
DR eggNOG; COG1227; Bacteria.
DR HOGENOM; CLU_025243_0_1_7; -.
DR OMA; IMLCAIL; -.
DR Proteomes; UP000000602; 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-RELATED; 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 Reference proteome {ECO:0000313|Proteomes:UP000000602}.
FT DOMAIN 192..317
FT /note="DHHA2"
FT /evidence="ECO:0000259|SMART:SM01131"
SQ SEQUENCE 319 AA; 33693 MW; 138C3717E4C00F67 CRC64;
MFSFFTGGTP MTISVVGHSN PDTDSVFSAI AFATLLNAQG QEAQACMQSA AADLNPESAM
LLARFGLAAP EEIGDVAGQD VALVDFSDLN QGPANLATAN VVAVVDHHKV GDLTTNSPIL
FRAEPVGCTG TILNKMYKEA GVAIPQAVAA GMLSAILSDT VNFKSPTCTE DDKIAVADLK
AVAKVEDTEE LFMAMLEAKS SVDGVPAKDL LFRDYKDFEM NGKKVGIGQL ELANLEQVAS
IRADLLAAME EVKADGRHSV LLMLTDVVKE GTDLVVLSDD PALIEGAFAG TLEMSAMWIE
GMMSRKKQTV PNLQKAFGC
//