ID I7LIZ2_9CLOT Unreviewed; 540 AA.
AC I7LIZ2;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, 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=CAAU_1243 {ECO:0000313|EMBL:CCJ33327.1};
OS Caloramator australicus RC3.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Caloramator.
OX NCBI_TaxID=857293 {ECO:0000313|EMBL:CCJ33327.1, ECO:0000313|Proteomes:UP000007652};
RN [1] {ECO:0000313|EMBL:CCJ33327.1, ECO:0000313|Proteomes:UP000007652}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RC3 {ECO:0000313|EMBL:CCJ33327.1,
RC ECO:0000313|Proteomes:UP000007652};
RX PubMed=21421756; DOI=10.1128/JB.00193-11;
RA Ogg C.D., Patel B.K.C.;
RT "Draft genome sequence of Caloramator australicus strain RC3T, a
RT thermoanaerobe from the Great Artesian Basin of Australia.";
RL J. Bacteriol. 193:2664-2665(2011).
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:CCJ33327.1}.
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DR EMBL; CAKP01000067; CCJ33327.1; -; Genomic_DNA.
DR RefSeq; WP_008908597.1; NZ_CAKP01000067.1.
DR AlphaFoldDB; I7LIZ2; -.
DR STRING; 857293.CAAU_1243; -.
DR eggNOG; COG1227; Bacteria.
DR OrthoDB; 9766150at2; -.
DR Proteomes; UP000007652; 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 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 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, ECO:0000313|EMBL:CCJ33327.1};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000007652}.
FT DOMAIN 72..129
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 248..306
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
SQ SEQUENCE 540 AA; 60822 MW; A7FA1A3744A1A47E CRC64;
MTDIIYIFGH KNPDTDSISA AIAYAELKKR LGFNAIAKRL GDINQETDFV LNYFNIPKPD
ILPTVKTQVS DLNLDKVIPI SPDSSIKTAW MLMKKNNVKT LAVIDENEKF LGLVTLSNIT
SKYMDTLENN IIKTPLRNIL ETLNAKIILG DEAKFNSNGK IVVAALSPES MKPFIEKGDI
VIIGNRKDSQ KKAIELGANC LIITGGFSAE DEILELAKQN NCIIINTPND TYTTARLINQ
SIPVKYVMTT ENIISFHIDD FVDEIRDKML QTRYRSYPVL DENNKIYGFI SRYHLISQKK
KQVILVDHNE RSQTVHGIDD AEILEIIDHH RVADIQTGKP IFFRNEPVGS TSTIIAGMYF
ENGIRPPKNI AGLLCAAIIS DTVKFKSPTC TYIDKITAER LAEIAGIDIE SFALEMFRAG
TSLQNRTPEE IFFQDFKEFK LGKYKIGISQ VNTMNVESLG ETKNDLLNFM NKLCNEKGYD
LLIIMLTDII REGSEIIFTG KEKDLIAKAF NVDVHNNFVF LPGVISRKKQ IIPPLSQIIE
//
