DLDH_CUPNH
ID DLDH_CUPNH Reviewed; 474 AA.
AC P52992; Q0K9A2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Dihydrolipoyl dehydrogenase;
DE EC=1.8.1.4;
DE AltName: Full=Dihydrolipoamide dehydrogenase;
DE AltName: Full=E3 component of 2-oxoglutarate dehydrogenase complex;
GN Name=odhL; OrderedLocusNames=H16_A2323;
OS Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442
OS / H16 / Stanier 337) (Ralstonia eutropha).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=381666;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8867378; DOI=10.1111/j.1574-6968.1996.tb08054.x;
RA Hein S., Steinbuechel A.;
RT "Cloning and characterization of the Alcaligenes eutrophus 2-oxoglutarate
RT dehydrogenase complex.";
RL FEMS Microbiol. Lett. 136:231-238(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337;
RX PubMed=16964242; DOI=10.1038/nbt1244;
RA Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R.,
RA Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I.,
RA Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.;
RT "Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia
RT eutropha H16.";
RL Nat. Biotechnol. 24:1257-1262(2006).
CC -!- FUNCTION: The branched-chain alpha-keto dehydrogenase complex catalyzes
CC the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It
CC contains multiple copies of 3 enzymatic components: branched-chain
CC alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and
CC lipoamide dehydrogenase (E3).
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: Cytoplasm.
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; X91877; CAA62982.1; -; Genomic_DNA.
DR EMBL; AM260479; CAJ93419.1; -; Genomic_DNA.
DR PIR; T44424; T44424.
DR RefSeq; WP_010809466.1; NZ_CP039287.1.
DR AlphaFoldDB; P52992; -.
DR SMR; P52992; -.
DR STRING; 381666.H16_A2323; -.
DR EnsemblBacteria; CAJ93419; CAJ93419; H16_A2323.
DR GeneID; 57644453; -.
DR KEGG; reh:H16_A2323; -.
DR eggNOG; COG1249; Bacteria.
DR HOGENOM; CLU_016755_0_1_4; -.
DR OMA; DAKYGEW; -.
DR OrthoDB; 267896at2; -.
DR Proteomes; UP000008210; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; IEA:UniProtKB-EC.
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 Cytoplasm; Disulfide bond; FAD; Flavoprotein; Glycolysis; NAD;
KW Oxidoreductase; Redox-active center; Reference proteome.
FT CHAIN 1..474
FT /note="Dihydrolipoyl dehydrogenase"
FT /id="PRO_0000068013"
FT ACT_SITE 453
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 34..51
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 60
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 189..193
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 212
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 246
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 278..281
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 321
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 329
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT DISULFID 51..56
FT /note="Redox-active"
FT /evidence="ECO:0000250"
FT CONFLICT 471..472
FT /note="QL -> HV (in Ref. 1; CAA62982)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 474 AA; 50267 MW; CEA48054D8D4DAA3 CRC64;
MSKQFDVLVI GAGPGGYIAA IRAGQLGLNV ACCEGNPYDD PKGEARLGGT CLNVGCIPSK
ALLASSEEFE NVQHHLGDHG ITVGDVKVDV AKMLKRKDDI VGKMTKGIEF LFRKNKVTLL
KGYGKFVGKS AEGFQVDVAG EVVTAKQVII ATGSKARHLP GIKVDNDLVS DNEGALKFPA
VPKKLGVIGA GVIGLELGSV WRRLGSDVTV LEALPAFLGA ADEGVAKEAQ KQLTKQGLKF
SLGVNVNEVT TGKNGVTVKY TDKDGKAQTL EVDRLIVSVG RVPNTDNLGL DAVGLAADQR
GFIEVDDHCA TKVPGLWAIG DVVRGPMLAH KAEDEGVAVA ERIAGQKPHI DYNCVPWVIY
TFPEIAWVGK TEAQLKAEGR EYKAGQFPFM ANGRALGMGH ADGFVKMLAD AKTDEILGVH
IVAANASDLI AEAVVAMEFK AASEDIGRVC HPHPSMSEVM REAALAVDKR QLNM
