ID H1BBR6_9FIRM Unreviewed; 547 AA.
AC H1BBR6;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
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=HMPREF0981_02649 {ECO:0000313|EMBL:EHO26212.1};
OS Erysipelotrichaceae bacterium 6_1_45.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae.
OX NCBI_TaxID=469614 {ECO:0000313|EMBL:EHO26212.1, ECO:0000313|Proteomes:UP000003818};
RN [1] {ECO:0000313|EMBL:EHO26212.1, ECO:0000313|Proteomes:UP000003818}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=6_1_45 {ECO:0000313|EMBL:EHO26212.1,
RC ECO:0000313|Proteomes:UP000003818};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J.,
RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Goldberg J.,
RA Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A.,
RA MacDonald P.J.P., Montmayeur A., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Erysipelotrichaceae bacterium 6_1_45.";
RL Submitted (OCT-2011) 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:EHO26212.1}.
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DR EMBL; ACTK01000044; EHO26212.1; -; Genomic_DNA.
DR AlphaFoldDB; H1BBR6; -.
DR PATRIC; fig|469614.3.peg.2725; -.
DR HOGENOM; CLU_025243_1_0_9; -.
DR BioCyc; EBAC469614-HMP:GMFG-2670-MONOMER; -.
DR Proteomes; UP000003818; 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 75..131
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 252..309
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
SQ SEQUENCE 547 AA; 61182 MW; B4D1D0EED7467951 CRC64;
MLNKEKIYIT GHRHPDTDSI ASAIAYAKLK QRQGFHAIAC RLGPVNAETE YLLERFHMDL
PMLFEDARAT LDEIEIDGPL AISPQTTIME TLELMSEQNK QSYGVINAQG KLMGMVTKSD
LATVGLGDTA VAIQLLQETP PEYIAKTVSG KMIYMDKAYH FNGKTSVIAI AETKLNNYEL
QDRLVIVGND SEAQEAAIRK GAGILVAVWT EHIEESVIAL AKEYHCPIIL SGHGTMNTSR
YLFFSPPVKL LMKTDLVSFN KNEFVDEVGK KMLKSRYRSY PVIDDENHLI GYVSRYHILN
QHNKKVILVD HNEYAQSVKS IEKADLLEVV DHHRVCDIST NRPISFRNEI IGSTASIITS
IYLENQMSIP KDIAGLLLGA ILSDTLKFKS PTTTAKDKGL ARMLAEIAEL DIDVFAKEMF
KVSSNISNKT PRELLNQDIK KFEIDGRTVM ISQVIAYQVS EAKEIEDTLQ SEMVKFAQEK
GLDLLVVAFT SILENGSVFY AAGDIADVVA EAFPNHFEEE HSFQEDILSR KNQIVPLLSR
AIINSVH
//
