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
//