ID   DLDH_HYMDI              Reviewed;          53 AA.
AC   P80647;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   02-SEP-2026, entry version 60.
DE   RecName: Full=Dihydrolipoyl dehydrogenase;
DE            EC=1.8.1.4;
DE   AltName: Full=Dihydrolipoamide dehydrogenase;
DE   Flags: Fragment;
OS   Hymenolepis diminuta (Rat tapeworm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC   Rhabditophora; Neodermata; Cestoda; Eucestoda; Cyclophyllidea;
OC   Hymenolepididae; Hymenolepis.
OX   NCBI_TaxID=6216;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP   BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND SUBCELLULAR LOCATION.
RC   TISSUE=Larva {ECO:0000269|PubMed:9030666};
RX   PubMed=9030666; DOI=10.1006/expr.1996.4135;
RA   Walker D.J., Burkhart W., Fioravanti C.F.;
RT   "Hymenolepis diminuta: mitochondrial NADH --> NAD transhydrogenation and
RT   the lipoamide dehydrogenase system.";
RL   Exp. Parasitol. 85:158-167(1997).
CC   -!- FUNCTION: Lipoamide dehydrogenase is a component of the glycine
CC       cleavage system as well as of the alpha-ketoacid dehydrogenase
CC       complexes (By similarity). This enzyme has lipoamide dehydrogenase
CC       activity and NADH -> NAD transhydrogenation activity. Also displays
CC       some NADH-ferricyanide reductase and NADPH -> NAD transydrogenation
CC       activities. {ECO:0000250|UniProtKB:P09622, ECO:0000269|PubMed:9030666}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] + NAD(+) = N(6)-
CC         [(R)-lipoyl]-L-lysyl-[protein] + NADH + H(+); 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; Evidence={ECO:0000269|PubMed:9030666};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:P00390};
CC       Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:P00390};
CC   -!- ACTIVITY REGULATION: Lipoamide reduction and the NADH -> NAD reaction
CC       are both completely inhibited by copper and cadmium ions.
CC       {ECO:0000269|PubMed:9030666}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.09 mM for NADH for the NADH -> NAD reaction
CC         {ECO:0000269|PubMed:9030666};
CC         KM=0.18 mM for NADH for the lipoamide dehydrogenase reaction
CC         {ECO:0000269|PubMed:9030666};
CC         KM=0.23 mM for AcPyAD for the NADH -> NAD reaction
CC         {ECO:0000269|PubMed:9030666};
CC         KM=0.51 mM for lipoamide {ECO:0000269|PubMed:9030666};
CC       pH dependence:
CC         Optimum pH is 7.5 for NADH -> NAD transhydrogenation, 6.5 for
CC         lipoamide reduction, 4.5 for NADPH -> NAD transhydrogenation, and 6.5
CC         for NADH-ferricyanide reduction. {ECO:0000269|PubMed:9030666};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:9030666}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:9030666}.
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   AlphaFoldDB; P80647; -.
DR   SMR; P80647; -.
DR   STRING; 6216.P80647; -.
DR   GO; GO:0005739; C:mitochondrion; EXP:UniProtKB.
DR   GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IEA:TreeGrafter.
DR   GO; GO:0004148; F:dihydrolipoyl dehydrogenase (NADH) activity; EXP:UniProtKB.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:TreeGrafter.
DR   GO; GO:0006103; P:2-oxoglutarate metabolic process; IEA:TreeGrafter.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR050151; Class-I_Pyr_Nuc-Dis_Oxidored.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR   PANTHER; PTHR22912:SF151; DIHYDROLIPOYL DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR22912; DISULFIDE OXIDOREDUCTASE; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; FAD; Flavoprotein;
KW   Mitochondrion; NAD; Oxidoreductase; Redox-active center.
FT   CHAIN           1..>53
FT                   /note="Dihydrolipoyl dehydrogenase"
FT                   /id="PRO_0000311713"
FT   BINDING         35..44
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P00390"
FT   BINDING         53
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   DISULFID        44..49
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250|UniProtKB:P00390"
FT   NON_TER         53
FT                   /evidence="ECO:0000303|PubMed:9030666"
SQ   SEQUENCE   53 AA;  5315 MW;  D7C11AE8F2F03D94 CRC64;
     LSSGEKDLVV IGSGPGGYVA AIKAAQLGML TVCIEKYPTF GGTCLNVGCI PSK
//