ID   DLDH_POPEU              Reviewed;          11 AA.
AC   P84545;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2005, sequence version 1.
DT   11-DEC-2019, entry version 29.
DE   RecName: Full=Dihydrolipoyl dehydrogenase;
DE            EC=1.8.1.4;
DE   AltName: Full=Dihydrolipoamide dehydrogenase;
DE   Flags: Fragment;
OS   Populus euphratica (Euphrates poplar).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Salicaceae; Saliceae; Populus.
OX   NCBI_TaxID=75702;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Leaf;
RX   PubMed=16740589; DOI=10.1093/aob/mcl106;
RA   Ferreira S., Hjernoe K., Larsen M., Wingsle G., Larsen P., Fey S.,
RA   Roepstorff P., Pais M.S.;
RT   "Proteome profiling of Populus euphratica Oliv. upon heat stress.";
RL   Ann. Bot. 98:361-377(2006).
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         Evidence={ECO:0000250|UniProtKB:P09622};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:P14218};
CC       Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:P14218};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P09622}.
CC   -!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000255}.
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DR   GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; IEA:UniProtKB-EC.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; FAD; Flavoprotein; NAD; Oxidoreductase;
KW   Redox-active center.
FT   CHAIN           <1..>11
FT                   /note="Dihydrolipoyl dehydrogenase"
FT                   /id="PRO_0000068011"
FT   NON_TER         1
FT   NON_TER         11
SQ   SEQUENCE   11 AA;  1201 MW;  C2E56DC3D7273769 CRC64;
     VGKFPLLANS R