ID G7M8X5_9CLOT Unreviewed; 548 AA.
AC G7M8X5;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
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=CDLVIII_4969 {ECO:0000313|EMBL:EHJ01460.1};
OS Clostridium sp. DL-VIII.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=641107 {ECO:0000313|EMBL:EHJ01460.1, ECO:0000313|Proteomes:UP000005106};
RN [1] {ECO:0000313|EMBL:EHJ01460.1, ECO:0000313|Proteomes:UP000005106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DL-VIII {ECO:0000313|EMBL:EHJ01460.1,
RC ECO:0000313|Proteomes:UP000005106};
RX PubMed=23929491;
RA Taghavi S., Izquierdo J.A., van der Lelie D.;
RT "Complete Genome Sequence of Clostridium sp. Strain DL-VIII, a Novel
RT Solventogenic Clostridium Species Isolated from Anaerobic Sludge.";
RL Genome Announc. 1:e00605-e00613(2013).
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; CM001240; EHJ01460.1; -; Genomic_DNA.
DR RefSeq; WP_009172100.1; NZ_CM001240.1.
DR AlphaFoldDB; G7M8X5; -.
DR STRING; 641107.CDLVIII_4969; -.
DR eggNOG; COG1227; Bacteria.
DR HOGENOM; CLU_025243_1_0_9; -.
DR Proteomes; UP000005106; 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 CDD; cd04597; CBS_pair_inorgPPase; 1.
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 Gene3D; 3.90.1640.10; inorganic pyrophosphatase (n-terminal core); 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; 2.
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; 2.
PE 4: Predicted;
KW CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EHJ01460.1};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000005106}.
FT DOMAIN 73..132
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 252..310
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
SQ SEQUENCE 548 AA; 60444 MW; B4C8F5EF92B67EC3 CRC64;
MENVVYVTGH KNPDSDSICA AYGYAEFKNK TSDLPAVPVR LGNVNPETQF ILDYFGVKAP
RLLETVKLKV EDLNFDTIKP INGNYSLRMA WNIMRDNHIK SLPVVDDKGG LIGILSISNL
TSAYMDIGDN DILAKSKTSI ENILDTLSAT SIYINEACKV FNGKIVVSAM QPESLKEIVD
EGDIAIVGDR PDVHEALIDI KTSLIIITGS HKLAENLLSK AKENGVTVIS TPHDSFTASR
LLIQSIPVSY VMATKDLISF SKDELADDIK DTMAETRYNS YPVVDEEGKV IGTVSRYHLI
SNHKKKVIQV DHNERGQSVD GLEEAEVLEI IDHHRVADIQ TSNPIFFRNE PLGSSSTIVG
KSYFEHNITP SKEVAGLLCG AIISDTLLFK SPTCTEQDKV ICRKLAEIAG ISSLEDFAKE
MFKAGTSLKG KSVSQIFNQD FKPFTMGESK VGVAQVNTMD IEGFMPLKDE MLSFMKSEAD
KKGYDVVMLL LTDILTEGSQ VLVAGERQDY VEKTFNVELK DSMAFLPGVL SRKKQVIPPL
TNVINSMK
//