ID   DLDH_TRYBB              Reviewed;         479 AA.
AC   Q04933;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Dihydrolipoyl dehydrogenase;
DE            EC=1.8.1.4;
DE   AltName: Full=Dihydrolipoamide dehydrogenase;
OS   Trypanosoma brucei brucei.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX   NCBI_TaxID=5702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8444180; DOI=10.1111/j.1432-1033.1993.tb17678.x;
RA   Else A.J., Hough D.W., Danson M.J.;
RT   "Cloning, sequencing, and expression of Trypanosoma brucei dihydrolipoamide
RT   dehydrogenase.";
RL   Eur. J. Biochem. 212:423-429(1993).
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   -!- 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; X70646; CAA49991.1; -; Genomic_DNA.
DR   PIR; S30057; S30057.
DR   AlphaFoldDB; Q04933; -.
DR   SMR; Q04933; -.
DR   GO; GO:0005737; C:cytoplasm; IDA:GeneDB.
DR   GO; GO:0005739; C:mitochondrion; IDA:GeneDB.
DR   GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0015036; F:disulfide oxidoreductase activity; ISM:GeneDB.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.390.30; -; 1.
DR   Gene3D; 3.50.50.60; -; 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; IPR006258; Lipoamide_DH.
DR   InterPro; IPR001100; Pyr_nuc-diS_OxRdtase.
DR   InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF02852; Pyr_redox_dim; 1.
DR   PIRSF; PIRSF000350; Mercury_reductase_MerA; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   SUPFAM; SSF55424; SSF55424; 1.
DR   TIGRFAMs; TIGR01350; lipoamide_DH; 1.
DR   PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; FAD; Flavoprotein; Glycolysis; NAD; Oxidoreductase;
KW   Redox-active center.
FT   CHAIN           1..479
FT                   /note="Dihydrolipoyl dehydrogenase"
FT                   /id="PRO_0000068008"
FT   ACT_SITE        458
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         41..50
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         59
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         124
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         153..155
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         190..197
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         213
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         247
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         284
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         325
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         332..335
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   DISULFID        50..55
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   479 AA;  50220 MW;  ABE40113CDFAF830 CRC64;
     MFRRCFPIFN PYDVVVVGGG PGGYVAAIKA AQLGLKTACV EKRGALGGTC LNVGCIPSKA
     LLHATHMYHD AHANFERYGL MGGAGVTMDV AKMQQQKEKS VNGLTSGVEY LLKKNKVTYY
     KGEAGFVTPN TLNVKGIDGK DEAIEAKNTI IATGSEPTAL PFLPFDEKVV LSSTGALALQ
     QVPKKMVVIG GGVIGLELGS VWARLGSDVT VVEFAPRCAP TLDSDVTDAL VGALKRNGED
     EVPMTGIEGV NGTNNGSIAL TLEVEQAGGQ AETLHCDALL VSVGRRPYTA GLGLEKNNVS
     LNERGFVKIG SHFETNVAGV YAIGDVVDKG PMLAHKAEDE GVACAEILAG RPGHVNYDVI
     PGVIYTMPEV ASVGKTEEEL KKAGVAYKVG KFPFNANSRA KAVATEDGFV KVLTDKATDR
     ILGVHIVCSA AGELIAGALL AMEYGASSED VGRTCHAHPT MSEAVKEACM ACFAKTINF