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Database: UniProt
Entry: Q6AL66_DESPS
LinkDB: Q6AL66_DESPS
Original site: Q6AL66_DESPS 
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
//
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