ID E2ZET6_9FIRM Unreviewed; 551 AA.
AC E2ZET6;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 24-JAN-2024, entry version 61.
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=HMPREF9436_00165 {ECO:0000313|EMBL:EFQ08310.1};
OS Faecalibacterium cf. prausnitzii KLE1255.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Faecalibacterium.
OX NCBI_TaxID=748224 {ECO:0000313|EMBL:EFQ08310.1, ECO:0000313|Proteomes:UP000006028};
RN [1] {ECO:0000313|EMBL:EFQ08310.1, ECO:0000313|Proteomes:UP000006028}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KLE1255 {ECO:0000313|EMBL:EFQ08310.1,
RC ECO:0000313|Proteomes:UP000006028};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (AUG-2010) 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:EFQ08310.1}.
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DR EMBL; AECU01000016; EFQ08310.1; -; Genomic_DNA.
DR RefSeq; WP_005937394.1; NZ_GL538228.1.
DR AlphaFoldDB; E2ZET6; -.
DR STRING; 748224.HMPREF9436_00165; -.
DR eggNOG; COG0517; Bacteria.
DR eggNOG; COG1227; Bacteria.
DR eggNOG; COG4109; Bacteria.
DR HOGENOM; CLU_025243_1_0_9; -.
DR OrthoDB; 9766150at2; -.
DR BioCyc; FCF748224-HMP:GTSS-3098-MONOMER; -.
DR Proteomes; UP000006028; 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; cd02205; CBS_pair_SF; 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 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-RELATED; 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 77..133
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 255..312
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
SQ SEQUENCE 551 AA; 61163 MW; 97FD4565EFAB366B CRC64;
MPKAAHKVVV IGHRNPDTDS ICSAIAYAEL KNKTSDLVCE PRRAGKMNQE TEFVLKKFGV
KPPRMCTDVN PKIRDVDYRE MPGIPGSTSL RKAWEIMRDK QIDTLPVTSP DNELEGVITV
KDIATANMDV FDTGILAKSQ TTYRNILETL GGTMVVGRED DVCTTGHIRI GTATPEMLEN
TVEKGDIVIL TNRYESQLCA IEKEASLLII CNGSKVGRTI QRIAEEMGVA IMSAPVDTYA
AGKLISQCAP ISYYMTRSDI MKFTLVTPVA DVTRVMAKVR HRYFPILDED GKYCGMVSRR
NIINLQKRRI ILVDHNEATQ AVEGFDQAEI LEIIDHHRIG SLETSGPVYF RNQPVGCTAT
IITQMYDEND MEIPPQIAGL LLAAILSDTL VFRSPTCTPL DEALAKRLAK IAGVDIDEFA
SEMFEAGEKL DGKTAEEVFL QDFKVFMCGD IRFGVAQGSY MTRKNLLAAE ALLQPYLEEA
RNKQNVEDIY MLLTDVPKEE SVVISDGRYA SEVLSDGFET QPAEDGSFTL PGVVSRKKQF
IPALMTAYQE L
//