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Database: UniProt
Entry: C9R8S7_AMMDK
LinkDB: C9R8S7_AMMDK
Original site: C9R8S7_AMMDK 
ID   C9R8S7_AMMDK            Unreviewed;       300 AA.
AC   C9R8S7;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   24-JAN-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=Adeg_1612 {ECO:0000313|EMBL:ACX52706.1};
OS   Ammonifex degensii (strain DSM 10501 / KC4).
OC   Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Ammonifex.
OX   NCBI_TaxID=429009 {ECO:0000313|EMBL:ACX52706.1, ECO:0000313|Proteomes:UP000002620};
RN   [1] {ECO:0000313|EMBL:ACX52706.1, ECO:0000313|Proteomes:UP000002620}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10501 / KC4 {ECO:0000313|Proteomes:UP000002620};
RG   US DOE Joint Genome Institute;
RA   Kerfeld C., Goodner B., Huber H., Stetter K., Lucas S., Copeland A.,
RA   Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L.,
RA   Pitluck S., Saunders E., Brettin T., Detter J.C., Han C., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Ovchinnikova G., Richardson P.;
RT   "Complete sequence of chromosome of Ammonifex degensii KC4.";
RL   Submitted (OCT-2009) 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};
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DR   EMBL; CP001785; ACX52706.1; -; Genomic_DNA.
DR   RefSeq; WP_015739583.1; NC_013385.1.
DR   AlphaFoldDB; C9R8S7; -.
DR   STRING; 429009.Adeg_1612; -.
DR   KEGG; adg:Adeg_1612; -.
DR   eggNOG; COG1227; Bacteria.
DR   HOGENOM; CLU_025243_0_1_9; -.
DR   OrthoDB; 9766150at2; -.
DR   Proteomes; UP000002620; 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:UP000002620}.
FT   DOMAIN          173..298
FT                   /note="DHHA2"
FT                   /evidence="ECO:0000259|SMART:SM01131"
SQ   SEQUENCE   300 AA;  33071 MW;  AEECD629E2EAB42A CRC64;
     MSEVYVIGHK SPDTDSICSA IVYAGLKGYK PARAGEINEE TAYVLDYFKV PVPELLENAA
     GKKLVLVDHN EAGQCVDGHD QAEILEVIDH HKMNFNYPNP IFIHVEPVGS TATVIAKMFK
     DKVKENPTYA GLLLAAILSD TVVFKSPTTT EEDKAIAAEL AQIAGIADIN QFGVDIKKAK
     ASIKGKPVAD VVHVDFKDYD FAGKKVGIGQ TELVDINEVY ERQEEFINYL KELKESKNYD
     MVIFMATDII KEGTELYFIG DPAIIEKAFG VKPQGNSVWL PGVMSRKKQV APPVEKAYCQ
//
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