ID M2P7Y0_9FIRM Unreviewed; 546 AA.
AC M2P7Y0;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, 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=HMPREF9943_01358 {ECO:0000313|EMBL:EMD16432.1};
OS Eggerthia catenaformis OT 569 = DSM 20559.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Coprobacillaceae; Eggerthia.
OX NCBI_TaxID=999415 {ECO:0000313|EMBL:EMD16432.1, ECO:0000313|Proteomes:UP000011758};
RN [1] {ECO:0000313|EMBL:EMD16432.1, ECO:0000313|Proteomes:UP000011758}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OT 569 {ECO:0000313|EMBL:EMD16432.1,
RC ECO:0000313|Proteomes:UP000011758};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Blanton J.M.,
RA Mathney J., Dewhirst F.E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M.,
RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.,
RA Chapman S.B., Gearin G., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Heiman D., Howarth C., Larimer J., Lui A., MacDonald P.J.P., McCowen C.,
RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Lactobacillus catenaformis F0143.";
RL Submitted (FEB-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:EMD16432.1}.
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DR EMBL; AGEJ01000021; EMD16432.1; -; Genomic_DNA.
DR RefSeq; WP_004803365.1; NZ_KB446648.1.
DR AlphaFoldDB; M2P7Y0; -.
DR STRING; 999415.HMPREF9943_01358; -.
DR PATRIC; fig|999415.3.peg.1379; -.
DR eggNOG; COG1227; Bacteria.
DR OrthoDB; 9766150at2; -.
DR BioCyc; ECAT999415-HMP:GTTI-1393-MONOMER; -.
DR Proteomes; UP000011758; 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; 3.10.310.20; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000011758}.
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 546 AA; 61244 MW; 73FD3D83478ACF10 CRC64;
MNDIVYVSGH KNPDSDSVCS AIAYSYLLNK TNKYHAVPVR LGEINRETEY ILKRFNQESP
VLLKTVKQKV EDLDYDKVTV FSKELTLKTA WSLMKQQNLK SAPILDDHGK LLGLLSSTNI
LEGYLDHWDA DVLKKAHTPI ENVIDTLRAN VIYLDKNLLT INGTVHIIAM DSEAKGYIRK
DDVVLIGSDR LEMIKYLAEI QAGLIVLTGM HYPSEEIIAL CKEKGVSLII TPYTTFMTSQ
QIVQSIPVEY VMQKGNLTVF STDDTVEYLK EVMSHTRYRS YPVVDLNNNV VGTISRYQLL
NGERKKIIQV DHNERGQAVD GIEEAEILEV IDHHRIADFQ TIGPLSFRAE PLGCTCTIIN
KIYEEQDVEI PPEIAGIMLG AILSDSLIFK SPTCTNVDKK TAYKLAKIAG VDLEEFGMEM
FKAGTSLSGK TVEEIFNQDY KKFNIGDTKI GIAQVNTMDI DGFAPYKKEM LQYMDQVVKE
NQYSVAVLLL TDVINANSEV FTAGPRQEFV EEAFHVKLDD SQATLPGIIS RKKQVVPAIT
NAINNA
//
