ID A0A1Y4SG27_9FIRM Unreviewed; 554 AA.
AC A0A1Y4SG27;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=B5E77_00180 {ECO:0000313|EMBL:OUQ28824.1};
OS Lachnoclostridium sp. An131.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1965555 {ECO:0000313|EMBL:OUQ28824.1, ECO:0000313|Proteomes:UP000199743};
RN [1] {ECO:0000313|Proteomes:UP000199743}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An131 {ECO:0000313|Proteomes:UP000199743};
RA Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA Rychlik I.;
RT "Function of individual gut microbiota members based on whole genome
RT sequencing of pure cultures obtained from chicken caecum.";
RL Submitted (APR-2017) 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:OUQ28824.1}.
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DR EMBL; NFLI01000001; OUQ28824.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y4SG27; -.
DR OrthoDB; 9766150at2; -.
DR Proteomes; UP000199743; 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; 1.
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:UP000199743}.
FT DOMAIN 255..318
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
SQ SEQUENCE 554 AA; 61988 MW; 542B66189936B420 CRC64;
MEKDLTRPVY IIGHKNPDTD SICSALAYAY LKNHLEGGGY IAARAGQLNQ ETQYVLNFFQ
AEAPVYVADV MTQVKDIEIR KTEGVKGNLS LKQAWNLMRR LGVVTLPITR EQKLEGLITI
GDITTSYMDV YDSKILAQAN TQYSNIIDTL EGKILVGSPD DYYNKGKVLI AAANPDLMED
YIEEGDLVIL GNRYESQLCA IEMNAGCIIV CEGAKVSMTI TKLAQEHGCV VISTPLDTFT
AARLINQSMP IRYFMKSDNL TIFNVNEKTE DIREVMGQKR YRDFPIVDKD DNYVGMISRR
NLLNLKRKQV IMVDHNEESQ AVDGIEHAEI LEIIDHHRLG SLETMAPVFF RNQPLGCTAT
IMYQMYQEKG VEIPRKIAGL LCAAIISDTL MFRSPTCTAV DKAAAEYLAQ IAEVDIEDLA
VDMFSAGSNL SARTADEIFF QDFKRFSVGN VEFGVGQINS MNAIELGEIR EKIVPYISTA
LKESGLNMIF FMLTNIIRES TELLCCGANA DVLVKEAFQL PEDTDAYELK GLVSRKKQLI
PALVGMIQQM EEMR
//