ID Q8G5E0_BIFLO Unreviewed; 496 AA.
AC Q8G5E0;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 133.
DE SubName: Full=Dihydrolipoamide dehydrogenase {ECO:0000313|EMBL:AAN24882.1};
GN Name=pdhD {ECO:0000313|EMBL:AAN24882.1};
GN OrderedLocusNames=BL1074 {ECO:0000313|EMBL:AAN24882.1};
OS Bifidobacterium longum (strain NCC 2705).
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=206672 {ECO:0000313|EMBL:AAN24882.1, ECO:0000313|Proteomes:UP000000439};
RN [1] {ECO:0000313|EMBL:AAN24882.1, ECO:0000313|Proteomes:UP000000439}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCC 2705 {ECO:0000313|Proteomes:UP000000439};
RX PubMed=12381787; DOI=10.1073/pnas.212527599;
RA Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G.,
RA Zwahlen M.C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.;
RT "The genome sequence of Bifidobacterium longum reflects its adaptation to
RT the human gastrointestinal tract.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002).
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 ECO:0000256|RuleBase:RU003691}.
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DR EMBL; AE014295; AAN24882.1; -; Genomic_DNA.
DR RefSeq; NP_696246.1; NC_004307.2.
DR RefSeq; WP_007051179.1; NC_004307.2.
DR AlphaFoldDB; Q8G5E0; -.
DR STRING; 206672.BL1074; -.
DR EnsemblBacteria; AAN24882; AAN24882; BL1074.
DR GeneID; 69577785; -.
DR KEGG; blo:BL1074; -.
DR PATRIC; fig|206672.9.peg.781; -.
DR HOGENOM; CLU_016755_0_2_11; -.
DR OrthoDB; 4678789at2; -.
DR PhylomeDB; Q8G5E0; -.
DR Proteomes; UP000000439; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016668; F:oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor; 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 InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR PANTHER; PTHR22912:SF217; DIHYDROLIPOYL DEHYDROGENASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR22912; DISULFIDE OXIDOREDUCTASE; 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.
DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000350-3};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU003691};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR000350-3};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000350-3};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003691};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW ECO:0000256|RuleBase:RU003691};
KW Reference proteome {ECO:0000313|Proteomes:UP000000439}.
FT DOMAIN 5..350
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 370..484
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT ACT_SITE 474
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-2"
FT BINDING 52
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 205..212
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 298
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 335
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT DISULFID 43..48
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ SEQUENCE 496 AA; 52103 MW; 3A5BE89E8197C6AB CRC64;
MSEQFDLVII GAGPGGYSTA LRAAELGMKV ALVERDATVG GTCLNRGCIP SKALITATHT
IDTVHRAAEL GVNASVNGID FGTLRDYRLR VVKTMVGGLA GLLAHRGITV FRANAAFHAD
ETAPATSNHI VHLVPSPDQS DILTYHKADV PEPSGPTMDL TATNIVIATG AKPRPLPGNP
FAGALIDSTQ ALEVNEFPSS AVIIGAGAIA LEFASMWNAA GSKVTLLIRK DRVLSAWDRR
AGTTLTRELK RHGVNIITRA SVTHVDTGAN LGATVHYTCE GQDGEQSVWG EIALVAIGRD
PITDPAWGVT IDDHGHVATD AYGRTDKPGV WAVGDVTAGH ALAHRAFEQG IVIAETIAGL
NPKPVDEATV PQIVFSFPEA ASVGLTVEQA QAREDLIEIK ETNYPMLANA RMLMSGTAGS
LTIVSGCDAA NPDTPRVLGV HMVSQMASDI IAEAEQLVGN HVPLADAARL VHPHPTFSET
LGEALLKADG RPLHTR
//
