ID   DLDH_SOLTU              Reviewed;          40 AA.
AC   P80503;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Dihydrolipoyl dehydrogenase;
DE            EC=1.8.1.4;
DE   AltName: Full=Dihydrolipoamide dehydrogenase;
DE   Flags: Fragment;
OS   Solanum tuberosum (Potato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX   NCBI_TaxID=4113;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Tuber;
RX   PubMed=8919912; DOI=10.1046/j.1365-313x.1996.09030357.x;
RA   Jansch L., Kruft V., Schmitz U.K., Braun H.P.;
RT   "New insights into the composition, molecular mass and stoichiometry of the
RT   protein complexes of plant mitochondria.";
RL   Plant J. 9:357-368(1996).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-20.
RC   STRAIN=cv. Romano; TISSUE=Tuber;
RX   PubMed=9729464; DOI=10.1042/bj3340571;
RA   Millar A.H., Knorpp C., Leaver C.J., Hill S.A.;
RT   "Plant mitochondrial pyruvate dehydrogenase complex: purification and
RT   identification of catalytic components in potato.";
RL   Biochem. J. 334:571-576(1998).
RN   [3]
RP   PROTEIN SEQUENCE OF 1-20.
RC   STRAIN=cv. Romano; TISSUE=Tuber;
RX   PubMed=10510296; DOI=10.1042/0264-6021:3430327;
RA   Millar A.H., Hill S.A., Leaver C.J.;
RT   "Plant mitochondrial 2-oxoglutarate dehydrogenase complex: purification and
RT   characterization in potato.";
RL   Biochem. J. 343:327-334(1999).
CC   -!- FUNCTION: Lipoamide dehydrogenase is a component of the glycine
CC       cleavage system as well as of the alpha-ketoacid dehydrogenase
CC       complexes. The pyruvate dehydrogenase complex contains multiple copies
CC       of three enzymatic components: pyruvate dehydrogenase (E1),
CC       dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase
CC       (E3) (By similarity). {ECO:0000250}.
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.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
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   STRING; 4113.PGSC0003DMT400011741; -.
DR   eggNOG; KOG1335; Eukaryota.
DR   BRENDA; 1.2.1.104; 5757.
DR   BRENDA; 1.2.1.105; 5757.
DR   SABIO-RK; P80503; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IBA:GO_Central.
DR   GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; FAD; Flavoprotein; Mitochondrion; NAD;
KW   Oxidoreductase; Redox-active center; Reference proteome.
FT   CHAIN           1..>40
FT                   /note="Dihydrolipoyl dehydrogenase"
FT                   /id="PRO_0000068010"
FT   BINDING         36..40
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   NON_TER         40
SQ   SEQUENCE   40 AA;  3913 MW;  17397BE30C2E9523 CRC64;
     ASGSDENDVV VIGGGPGGYV AAIKAAQLGL KTTXIEKRGT