ID   DLDH_ACHLA              Reviewed;         336 AA.
AC   P35484;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Dihydrolipoyl dehydrogenase;
DE            EC=1.8.1.4;
DE   AltName: Full=Dihydrolipoamide dehydrogenase;
DE   AltName: Full=E3 component of pyruvate complex;
DE   Flags: Fragment;
GN   Name=pdhD;
OS   Acholeplasma laidlawii.
OC   Bacteria; Tenericutes; Mollicutes; Acholeplasmatales; Acholeplasmataceae;
OC   Acholeplasma.
OX   NCBI_TaxID=2148;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1735725; DOI=10.1128/jb.174.4.1388-1396.1992;
RA   Wallbrandt P., Tegman V., Jonsson B.-H., Wieslander A.;
RT   "Identification and analysis of the genes coding for the putative pyruvate
RT   dehydrogenase enzyme complex in Acholeplasma laidlawii.";
RL   J. Bacteriol. 174:1388-1396(1992).
CC   -!- FUNCTION: Lipoamide dehydrogenase is a component of the alpha-ketoacid
CC       dehydrogenase complexes.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + NAD(+) = (R)-N(6)-
CC         lipoyl-L-lysyl-[protein] + H(+) + NADH; Xref=Rhea:RHEA:15045,
CC         Rhea:RHEA-COMP:10474, Rhea:RHEA-COMP:10475, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:83099,
CC         ChEBI:CHEBI:83100; EC=1.8.1.4;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC       Note=Binds 1 FAD per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
CC   -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000305}.
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DR   EMBL; M81753; AAA21910.1; -; Genomic_DNA.
DR   PIR; D42653; D42653.
DR   AlphaFoldDB; P35484; -.
DR   SMR; P35484; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.50.50.60; -; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Disulfide bond; FAD; Flavoprotein; Glycolysis; NAD;
KW   Oxidoreductase; Redox-active center.
FT   CHAIN           1..>336
FT                   /note="Dihydrolipoyl dehydrogenase"
FT                   /id="PRO_0000068012"
FT   BINDING         34..42
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         51
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         115
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         180..184
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         203
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         237
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         264..267
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         304
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         312
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   DISULFID        42..47
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
FT   NON_TER         336
SQ   SEQUENCE   336 AA;  35996 MW;  4405B1097279B36C CRC64;
     MSKEYEIIIV GGGPGGYVAA IKAAQYGAKV ALVEKEVVGG ICLNHGCIPT KTFLKSAKVF
     NTVKKSMDFG VSTSGEVGFD WSKIVSRKDG VVKQLTNGVA FLLKKNGVDV YNGFGDIKSA
     NEVVVNGESL KTKNVIIATG SSAVVPPIPG VKEAYEKGIV VTSRELLNVK NYPKSIVIVG
     GGVIGVEFAT VFNSFGSKVT IIEMMDGILP TMDDDIRVAY AKTLKRDGIE ILTKAEVKKV
     DDHKVTYSLD GKETTIEGDL ILMSVGTRAN SKGLEHLGLE MDRANIKTNE YLQTNVPGVY
     AIGDVNGKFM LAHVAEHEGI TAVQHILKIG HAKMNY