ID V1DAF4_9FIRM Unreviewed; 544 AA.
AC V1DAF4;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
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=HMPREF9089_00893 {ECO:0000313|EMBL:ESE30609.1};
OS Eubacterium brachy ATCC 33089.
OC Bacteria; Bacillota; Clostridia; Eubacteriales;
OC Eubacteriales Family XIII. Incertae Sedis.
OX NCBI_TaxID=1321814 {ECO:0000313|EMBL:ESE30609.1, ECO:0000313|Proteomes:UP000017536};
RN [1] {ECO:0000313|EMBL:ESE30609.1, ECO:0000313|Proteomes:UP000017536}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33089 {ECO:0000313|EMBL:ESE30609.1,
RC ECO:0000313|Proteomes:UP000017536};
RA Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R., Fronick C.,
RA O'Laughlin M., Godfrey J., Miner T., Herter B., Appelbaum E., Cordes M.,
RA Lek S., Wollam A., Pepin K.H., Palsikar V.B., Mitreva M., Wilson R.K.;
RL Submitted (AUG-2013) 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:ESE30609.1}.
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DR EMBL; AXUD01000006; ESE30609.1; -; Genomic_DNA.
DR AlphaFoldDB; V1DAF4; -.
DR STRING; 1321814.HMPREF9089_00893; -.
DR PATRIC; fig|1321814.3.peg.849; -.
DR eggNOG; COG1227; Bacteria.
DR HOGENOM; CLU_025243_1_0_9; -.
DR OrthoDB; 9766150at2; -.
DR Proteomes; UP000017536; 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 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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000017536}.
FT DOMAIN 74..130
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 252..310
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
SQ SEQUENCE 544 AA; 61031 MW; 562E4CB678684C59 CRC64;
MKDKVYVVGH RNPDTDSICS ALSYAYLKNR IGEFEYLPMR AGEISPETKF VLEHFNVEEP
KLLTDLRSQI KDADYRKTKG VHKDEPISRA WRILGEADIS SLPVVDGKNR VIGIISLGDI
TKSFIKSCDS MALVREKTPY ENVVEVLDGT VICGEVENRT IEGRVVVAGS STNTVDKLID
ENSVVILADN REIQKLAMER GARCLILCLN SDVDESLIAL AKKKKCVLIK TEKDTFTVSR
IISQSVPIES YMVAKNLIKF QEDEFIVDIK PVVAEGKHRY FPVIDEKGGL LGMLSRNDIV
NTQKKKVIMV DHNERRQGVT GMMEAQVIEI LDHHKIGNIN TVYPIFYRNR QYGCTCTIVY
QLFKENNVKI PKDIAGLMCS AILSDTLMFK SPTCTPVDKA AVLELAQTAE IEYEKYAMDM
FSAASDFASK SIDEIFNLDY KKFQSGEIAY GVGQVSSVSR AELDNLKVKL QEYMEKNIER
GELNMIFLML TDILDESTEL LCAGSGAIEM ARRAFNTEGK DSLMLADTVS RKKQIIPALS
EAMQ
//
