DLDH_CAEEL
ID DLDH_CAEEL Reviewed; 495 AA.
AC O17953; D3YT81;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Dihydrolipoyl dehydrogenase, mitochondrial;
DE EC=1.8.1.4;
DE AltName: Full=Dihydrolipoamide dehydrogenase;
DE Flags: Precursor;
GN Name=dld-1; ORFNames=LLC1.3;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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 -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=O17953-1; Sequence=Displayed;
CC Name=b;
CC IsoId=O17953-2; Sequence=VSP_045381;
CC -!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; Z82277; CAB05249.2; -; Genomic_DNA.
DR EMBL; Z82277; CBK19462.1; -; Genomic_DNA.
DR PIR; T23632; T23632.
DR RefSeq; NP_001255810.1; NM_001268881.1. [O17953-1]
DR RefSeq; NP_001255811.1; NM_001268882.1. [O17953-2]
DR AlphaFoldDB; O17953; -.
DR SMR; O17953; -.
DR BioGRID; 43470; 19.
DR IntAct; O17953; 2.
DR STRING; 6239.LLC1.3a; -.
DR EPD; O17953; -.
DR PaxDb; O17953; -.
DR PeptideAtlas; O17953; -.
DR EnsemblMetazoa; LLC1.3a.1; LLC1.3a.1; WBGene00010794. [O17953-1]
DR EnsemblMetazoa; LLC1.3b.1; LLC1.3b.1; WBGene00010794. [O17953-2]
DR GeneID; 178387; -.
DR KEGG; cel:CELE_LLC1.3; -.
DR UCSC; LLC1.3.1; c. elegans. [O17953-1]
DR CTD; 178387; -.
DR WormBase; LLC1.3a; CE31971; WBGene00010794; dld-1. [O17953-1]
DR WormBase; LLC1.3b; CE44593; WBGene00010794; dld-1. [O17953-2]
DR eggNOG; KOG1335; Eukaryota.
DR GeneTree; ENSGT00550000074844; -.
DR HOGENOM; CLU_016755_0_3_1; -.
DR InParanoid; O17953; -.
DR OMA; DAKYGEW; -.
DR OrthoDB; 581771at2759; -.
DR PhylomeDB; O17953; -.
DR Reactome; R-CEL-204174; Regulation of pyruvate dehydrogenase (PDH) complex.
DR Reactome; R-CEL-389661; Glyoxylate metabolism and glycine degradation.
DR Reactome; R-CEL-5362517; Signaling by Retinoic Acid.
DR Reactome; R-CEL-6783984; Glycine degradation.
DR Reactome; R-CEL-70268; Pyruvate metabolism.
DR Reactome; R-CEL-70895; Branched-chain amino acid catabolism.
DR Reactome; R-CEL-71064; Lysine catabolism.
DR Reactome; R-CEL-71403; Citric acid cycle (TCA cycle).
DR PRO; PR:O17953; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00010794; Expressed in larva and 4 other tissues.
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 GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic 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 Alternative splicing; Disulfide bond; FAD; Fatty acid biosynthesis;
KW Fatty acid metabolism; Flavoprotein; Lipid biosynthesis; Lipid metabolism;
KW Mitochondrion; NAD; Oxidoreductase; Redox-active center;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..495
FT /note="Dihydrolipoyl dehydrogenase, mitochondrial"
FT /id="PRO_0000421278"
FT ACT_SITE 472
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 59..68
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 77
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 169..171
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 206..213
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 229
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 264
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 299
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 340
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 346..349
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT DISULFID 68..73
FT /note="Redox-active"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..345
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_045381"
SQ SEQUENCE 495 AA; 52633 MW; 77EB4A2FA935F0F6 CRC64;
MSLSRTTQLP FAKRQFFQVL ARNYSNTQDA DLVVIGGGPG GYVAAIKAAQ LGMKTVCVEK
NATLGGTCLN VGCIPSKALL NNSHYLHMAQ HDFAARGIDC TASLNLPKMM EAKSNSVKQL
TGGIKQLFKA NKVGHVEGFA TIVGPNTVQA KKNDGSVETI NARNILIASG SEVTPFPGIT
IDEKQIVSST GALSLGQVPK KMVVIGAGVI GLELGSVWQR LGAEVTAVEF LGHVGGMGID
GEVSKNFQRS LTKQGFKFLL NTKVMGASQN GSTITVEVEG AKDGKKQTLE CDTLLVSVGR
RPYTEGLGLS NVQIDLDNRG RVPVNERFQT KVPSIFAIGD VIEGPMLAHK AEDEGILCVE
GIAGGPVHID YNCVPSVVYT HPEVAWVGKA EEQLKQEGVA YKIGKFPFVA NSRAKTNNDQ
EGFVKVLADK QTDRMLGVHI IGPNAGEMIA EATLAMEYGA SAEDVARVCH PHPTLSEAFR
EANLAAYCGK AINNV
