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
//