ID D4MPC7_9FIRM Unreviewed; 550 AA.
AC D4MPC7;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 53.
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 ORFNames=CL3_03740 {ECO:0000313|EMBL:CBL35613.1};
OS butyrate-producing bacterium SM4/1.
OC Bacteria; Bacillota; Clostridia; Eubacteriales.
OX NCBI_TaxID=245012 {ECO:0000313|EMBL:CBL35613.1, ECO:0000313|Proteomes:UP000008959};
RN [1] {ECO:0000313|EMBL:CBL35613.1, ECO:0000313|Proteomes:UP000008959}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM4/1 {ECO:0000313|EMBL:CBL35613.1,
RC ECO:0000313|Proteomes:UP000008959};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT "The genome sequence of Clostridiales sp. SM4/1.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBL35613.1, ECO:0000313|Proteomes:UP000008959}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM4/1 {ECO:0000313|EMBL:CBL35613.1,
RC ECO:0000313|Proteomes:UP000008959};
RA Pajon A.;
RL Submitted (MAR-2010) 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; FP929060; CBL35613.1; -; Genomic_DNA.
DR AlphaFoldDB; D4MPC7; -.
DR KEGG; bprm:CL3_03740; -.
DR PATRIC; fig|245012.3.peg.2855; -.
DR HOGENOM; CLU_025243_1_0_9; -.
DR BioCyc; BBAC245012:G1313-167-MONOMER; -.
DR Proteomes; UP000008959; 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; 3.10.580.10; CBS-domain; 1.
DR Gene3D; 3.10.310.20; DHHA2 domain; 1.
DR Gene3D; 3.40.1390.20; HprK N-terminal domain-like; 1.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR001667; DDH_dom.
DR InterPro; IPR038763; DHH_sf.
DR InterPro; IPR004097; DHHA2.
DR InterPro; IPR038222; DHHA2_dom_sf.
DR InterPro; IPR010766; DRTGG.
DR InterPro; IPR028979; Ser_kin/Pase_Hpr-like_N_sf.
DR PANTHER; PTHR12112; BNIP - RELATED; 1.
DR PANTHER; PTHR12112:SF22; MANGANESE-DEPENDENT INORGANIC PYROPHOSPHATASE; 1.
DR Pfam; PF00571; CBS; 2.
DR Pfam; PF01368; DHH; 1.
DR Pfam; PF02833; DHHA2; 1.
DR Pfam; PF07085; DRTGG; 1.
DR SMART; SM00116; CBS; 2.
DR SMART; SM01131; DHHA2; 1.
DR SUPFAM; SSF54631; CBS-domain pair; 1.
DR SUPFAM; SSF64182; DHH phosphoesterases; 1.
DR SUPFAM; SSF75138; HprK N-terminal domain-like; 1.
DR PROSITE; PS51371; CBS; 1.
PE 4: Predicted;
KW CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CBL35613.1};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000008959}.
FT DOMAIN 256..313
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
SQ SEQUENCE 550 AA; 61391 MW; A431581046DE52F7 CRC64;
MSDSKKRRTI VIGHKNPDTD SICSAICYAN LKHILTGEEY TPARAGHVNS ETQYVLDYFG
VEAPELIENV RTQVKDIEIR ETKGVDKNIS LKKAWNLMQD NTVVTIPAVT EDNTLEGLIT
VGDITRSYMN VYDSSILSKA CTQYSNILET LEGALLVGDP EAYFDKGKVL VAAANPDMME
YYIEKHDLVI LGNRYESQLC AIEMEADCII VCEGAGVSMT IKKLAQERGC TVLTTPYDTY
TAARLINQSM PISYFMTKDN LITFGTEDFI DDIRDVMTNK RHRDFPILDR DGKYKGMISR
RNLLGARGKN LILVDHNERS QAVEGMESAN VMEIIDHHRL GTVETMSPVF FRNQPLGCTA
TIIYQMYNEN KVEIDRKIAG LLCSAILSDT LLFRSPTCTA VDKAAALELA EIAGVDAESL
AKEMFEAGSK LKGKTDSEIF YQDFKRFTAG KLTFGVGQIT SLNVEELGKI KERLIEYIGE
ARNEQKVDMM FFMMTNILEQ STELICDGQG AEQLAALAFH LKEGEKVVTL PGVVSRKKQL
IPALMIATEQ
//