ID W3ANG4_9FIRM Unreviewed; 449 AA.
AC W3ANG4;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE SubName: Full=Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide dehydrogenase component {ECO:0000313|EMBL:ETP72566.1};
GN ORFNames=UYO_1495 {ECO:0000313|EMBL:ETP72566.1};
OS Lachnospiraceae bacterium JC7.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1165092 {ECO:0000313|EMBL:ETP72566.1, ECO:0000313|Proteomes:UP000018967};
RN [1] {ECO:0000313|EMBL:ETP72566.1, ECO:0000313|Proteomes:UP000018967}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JC7 {ECO:0000313|EMBL:ETP72566.1,
RC ECO:0000313|Proteomes:UP000018967};
RA Rosewarne C.P., Cheung J.L., Evans P.N., Tomkins N.W., Denman S.E.,
RA O Cuiv P., Morrison M.;
RT "Isolation and genomic characterisation of Lachnospiraceae sp. JC7, a newly
RT identified member of the bovine rumen core microbiota.";
RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRSR:PIRSR000350-3};
CC Note=Binds 1 FAD per subunit. {ECO:0000256|PIRSR:PIRSR000350-3};
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00007532}.
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:ETP72566.1}.
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DR EMBL; ALYD01000013; ETP72566.1; -; Genomic_DNA.
DR AlphaFoldDB; W3ANG4; -.
DR PATRIC; fig|1165092.3.peg.1490; -.
DR OrthoDB; 9807946at2; -.
DR Proteomes; UP000018967; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR InterPro; IPR001100; Pyr_nuc-diS_OxRdtase.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR PANTHER; PTHR43014; MERCURIC REDUCTASE; 1.
DR PANTHER; PTHR43014:SF4; PYRIDINE NUCLEOTIDE-DISULFIDE OXIDOREDUCTASE RCLA-RELATED; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR PIRSF; PIRSF000350; Mercury_reductase_MerA; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|PIRSR:PIRSR000350-3};
KW Flavoprotein {ECO:0000256|PIRSR:PIRSR000350-3};
KW NAD {ECO:0000256|PIRSR:PIRSR000350-3};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000350-3};
KW Pyruvate {ECO:0000313|EMBL:ETP72566.1}.
FT DOMAIN 4..313
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 336..437
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT BINDING 49
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 113
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 172..179
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 259
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 299
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT DISULFID 41..46
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ SEQUENCE 449 AA; 49464 MW; 06EC1EB3B53FD104 CRC64;
MYDYDVLFIG SGHAAWHGAL KLVKAGKKVA FVDGDLIGGT CTNYGCDAKI LLDAPFAFIN
GLKRYKGIGV DSTPSVNWSD LMRYKKQVID PLPTLMEQGI FGRAGMPVIH AMGKFVDAHT
VLAGDQTVTA DRIVIATGEH PVKRDIPGKE YIRDSRDFLD METFPERIAF IGAGIIAMEF
ASMAIELGSE VTVIHHNDRA LKMYPRDYVD IVVNKMRDEG VKFAFNESVS SIEKQGDEFV
ITCESGKKLT VDYVLEATGR EANVEGLDLE KAGVEYSRKG IKVNAYLQTN VPNIYASGDV
IDKKIPKLTP TATFESNYIA DHILDAGTAP ISYPVVPNLV FTLPRIAQVG VSVDTAKQDT
EHYDVVTVPY GKTLLFEAKN ETYAEFTFVF NKEHDLVGAA FISDDAGMFV DIITMMINRK
ISSQEINKMI FAFPTESYGL ISMVAGLLK
//
