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Database: UniProt
Entry: A0A139CTH3_9FIRM
LinkDB: A0A139CTH3_9FIRM
Original site: A0A139CTH3_9FIRM 
ID   A0A139CTH3_9FIRM        Unreviewed;       545 AA.
AC   A0A139CTH3;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
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=AWU54_749 {ECO:0000313|EMBL:KXS44479.1};
OS   Candidatus Frackibacter sp. T328-2.
OC   Bacteria; Bacillota; Clostridia; Halanaerobiales; Halobacteroidaceae;
OC   Frackibacter.
OX   NCBI_TaxID=1785949 {ECO:0000313|EMBL:KXS44479.1, ECO:0000313|Proteomes:UP000070439};
RN   [1] {ECO:0000313|EMBL:KXS44479.1, ECO:0000313|Proteomes:UP000070439}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T328-2 {ECO:0000313|EMBL:KXS44479.1};
RA   Wolfe R., Daly R., Wrighton K.;
RT   "Candidatus Frackibacter-2 T328 Annotated.";
RL   Submitted (JAN-2016) 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:KXS44479.1}.
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DR   EMBL; LSBO01000024; KXS44479.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A139CTH3; -.
DR   PATRIC; fig|1785949.3.peg.582; -.
DR   Proteomes; UP000070439; 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; 3.10.310.20; 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); 2.
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; 2.
PE   4: Predicted;
KW   CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          73..130
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
FT   DOMAIN          253..310
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
SQ   SEQUENCE   545 AA;  60854 MW;  F46B94337D1B517C CRC64;
     MFKEKLVIGH QNPDTDSICS AIGYAELKQK QGENVVAARC GKLNPETEFV LDYFDLPAPK
     LVTDVYTRVS DIMEKSNLKS VLPSTPIKEV GELLEQEAIK VIPVVDKDNK LLGIVTASDI
     AHRYLQELAV ESLREVPTSL ENIIQTLDGE LINNQQDLSS EVTGNIFTGA MDTETMCEYI
     NPGDIVLLGN RIKAQEAVLE REISCLIVTG NLEIKSEVKD LAIEKGITVI RVPYDTFAAA
     RLINMSIPIS KVMSTEVEKF YPDELVEDVK EEIINSAHRS YPVTDRQNRL LGLVSARNLI
     DVETKEVILV DHNEKSQAVD GIEEATLVEV IDHHRLGDLE TLEPILVRNE PVGSTATIIA
     KLYFEYGVEL SVEIAGVLLS AILSDTVIFR SPTCTGVDKM IAEKLAEIVE VEIEKFGRRL
     FKAGSVLNKL EPRELILNDY KEYKFDEIKI GVGQIEIMDL AEFKEMQHNI LNVMNEVKKE
     SGNDYLFLLV TDVLNEGSLL LYNQTATSLV KRNFVGEEEE VGFYLPGVMS RKKQVIPVLS
     KALID
//
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