ID A0A140DW52_9FIRM Unreviewed; 532 AA.
AC A0A140DW52;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=AALO17_17450 {ECO:0000313|EMBL:AMK54879.1};
OS Faecalibaculum rodentium.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae; Faecalibaculum.
OX NCBI_TaxID=1702221 {ECO:0000313|EMBL:AMK54879.1, ECO:0000313|Proteomes:UP000069771};
RN [1] {ECO:0000313|EMBL:AMK54879.1, ECO:0000313|Proteomes:UP000069771}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Alo17 {ECO:0000313|EMBL:AMK54879.1,
RC ECO:0000313|Proteomes:UP000069771};
RX PubMed=26877770; DOI=10.1186/s13099-016-0087-3;
RA Lim S., Chang D.H., Ahn S., Kim B.C.;
RT "Whole genome sequencing of "Faecalibaculum rodentium" ALO17, isolated from
RT C57BL/6J laboratory mouse feces.";
RL Gut Pathog. 8:3-3(2016).
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};
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DR EMBL; CP011391; AMK54879.1; -; Genomic_DNA.
DR RefSeq; WP_067557855.1; NZ_CP011391.1.
DR AlphaFoldDB; A0A140DW52; -.
DR STRING; 1702221.AALO17_17450; -.
DR GeneID; 78478400; -.
DR KEGG; fro:AALO17_17450; -.
DR PATRIC; fig|1702221.3.peg.1701; -.
DR OrthoDB; 9766150at2; -.
DR Proteomes; UP000069771; Chromosome.
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; 1.
DR Pfam; PF01368; DHH; 2.
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:UP000069771}.
FT DOMAIN 246..304
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
SQ SEQUENCE 532 AA; 59710 MW; 54527B27240E8F62 CRC64;
MEQPIYVIGH KNPDTDSICA ALSLAELKRQ LGQNAVAARI GHVNPETKFV LEKAGMEPPL
HINTAKSTLA EIEIDQAVTV DKGATLRRGW DLLIENDAKT LYATDSEGNY SGLVTLGDIS
KIQMQDLNIT RDLLKVTPVE NFRAALRGTI LLEGTRPLSG EVRIADKKMM DRNLEGAIMV
LNDHEDSMIK SMAKGAAMIL IAENFVPNDY IIDMARNMGV TLITTPYNLM KIVQMVYRSI
PIESIMLPAS DMVQFSRDEF LEDVEREMLK TRHSSYPVVS QGRITGSVAR YHLLKSTPKR
FILVDHNEKK QTINDIDKGE IIEIVDHHRI GDITTNKPIQ FRNMIVGSSC TIVGLMWQEY
GLKMPENIAK LVIYAMISDT MNFNSPTCTP VDRMLAERIA TEYGFDINAM AEELFANTAS
IKGKTVQQLT GTDSKEFNIG GHKVAISQTF VFNYDDIPAI RDELLDYMRQ EAKSRRLDLF
LMTFTNVEGR GSRFLAAGPE AARMRPVLDR FEDQGFVSRK KQIVPGLARE LE
//
