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Database: UniProt
Entry: A0A0F0C521_9CLOT
LinkDB: A0A0F0C521_9CLOT
Original site: A0A0F0C521_9CLOT 
ID   A0A0F0C521_9CLOT        Unreviewed;       556 AA.
AC   A0A0F0C521;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
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=CLFS41_43770 {ECO:0000313|EMBL:KJJ68312.1};
OS   Clostridium sp. FS41.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1609975 {ECO:0000313|EMBL:KJJ68312.1, ECO:0000313|Proteomes:UP000033604};
RN   [1] {ECO:0000313|EMBL:KJJ68312.1, ECO:0000313|Proteomes:UP000033604}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FS41 {ECO:0000313|EMBL:KJJ68312.1,
RC   ECO:0000313|Proteomes:UP000033604};
RA   Poehlein A., Daniel R.;
RT   "Genome sequencing of Clostridium sp. FS41.";
RL   Submitted (FEB-2015) 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};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KJJ68312.1}.
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DR   EMBL; JYHN01000069; KJJ68312.1; -; Genomic_DNA.
DR   RefSeq; WP_007866329.1; NZ_JYHN01000069.1.
DR   AlphaFoldDB; A0A0F0C521; -.
DR   GeneID; 77446013; -.
DR   PATRIC; fig|1609975.3.peg.4688; -.
DR   Proteomes; UP000033604; Unassembled WGS sequence.
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; 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:KJJ68312.1};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033604}.
FT   DOMAIN          256..314
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
SQ   SEQUENCE   556 AA;  61754 MW;  06EF794EA14BDF36 CRC64;
     MEHDLKRKTT VIGHRNPDTD SICSAICYAN LKNKLTGEEY VPARAGHVNG ETQFVLDYFG
     VEEPKLVEDV RTQVKDIEIR KTRGVADNIS LKKAWKIMQE NNVVTIPSVR PDGTLEGLIT
     VGDITKTYMN IYDSSILSKA NTQYSNIIET LEADLLVGDA DVYFDKGKVL IAAANPDLME
     FYIEPHDLVI LGNRYESQLC AIEMGAAAII VCEGAGVSMT IKKIAQDRGC TVIATTYDTY
     TAARLINQSM PISYFMTREH LITFNSDDYT DEIREVMASK RHRDFPILDK EGRYLGMISR
     RNLLGAKGKQ VILVDHNEKS QAVAGIESAE IQEIIDHHRL GTVQTMAPVF FRNQPLGCTA
     TIIYQMYQEA GVDIEKKIAG LLCSAIVSDT LLFRSPTCTP VDEMAARSLA AIAGLDIEKY
     AMEMFGAGSN LKDKSDEEIF YQDFKRFTAG KVMIGVGQIT SLNGGELEGL KHRMPEFMEK
     AREGSGLDMV FFMLTNILTE STDLICQGQG AVQLAAKAFH LDLEEATQKE EPILNLPGVV
     SRKKQLIPEL MLAEQD
//
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