ID   DLDH_RHIEC              Reviewed;         481 AA.
AC   O05940; Q2K8W2;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   21-SEP-2011, sequence version 2.
DT   03-AUG-2022, entry version 151.
DE   RecName: Full=Dihydrolipoyl dehydrogenase;
DE            EC=1.8.1.4;
DE   AltName: Full=Dihydrolipoamide dehydrogenase;
DE   AltName: Full=E3 component of pyruvate and 2-oxoglutarate dehydrogenases complexes;
DE   AltName: Full=ORF-E3;
GN   Name=lpdA; OrderedLocusNames=RHE_CH01938;
OS   Rhizobium etli (strain CFN 42 / ATCC 51251).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=347834;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFN 42 / ATCC 51251;
RX   PubMed=16505379; DOI=10.1073/pnas.0508502103;
RA   Gonzalez V., Santamaria R.I., Bustos P., Hernandez-Gonzalez I.,
RA   Medrano-Soto A., Moreno-Hagelsieb G., Janga S.C., Ramirez M.A.,
RA   Jimenez-Jacinto V., Collado-Vides J., Davila G.;
RT   "The partitioned Rhizobium etli genome: genetic and metabolic redundancy in
RT   seven interacting replicons.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:3834-3839(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 202-481.
RC   STRAIN=CE3;
RX   PubMed=9141657; DOI=10.1111/j.1574-6968.1997.tb10324.x;
RA   Tate R., Riccio A., Iaccarino M., Patriarca E.J.;
RT   "Cloning and transcriptional analysis of the lipA (lipoic acid synthetase)
RT   gene from Rhizobium etli.";
RL   FEMS Microbiol. Lett. 149:165-172(1997).
CC   -!- FUNCTION: Lipoamide dehydrogenase is a component of the alpha-ketoacid
CC       dehydrogenase complexes. {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   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC       Note=Binds 1 FAD per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
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; CP000133; ABC90724.1; -; Genomic_DNA.
DR   EMBL; Y11708; CAA72399.1; -; Genomic_DNA.
DR   RefSeq; WP_011425214.1; NC_007761.1.
DR   AlphaFoldDB; O05940; -.
DR   SMR; O05940; -.
DR   STRING; 347834.RHE_CH01938; -.
DR   EnsemblBacteria; ABC90724; ABC90724; RHE_CH01938.
DR   GeneID; 61480402; -.
DR   KEGG; ret:RHE_CH01938; -.
DR   eggNOG; COG1249; Bacteria.
DR   HOGENOM; CLU_016755_0_2_5; -.
DR   OMA; WASMLND; -.
DR   Proteomes; UP000001936; Chromosome.
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..481
FT                   /note="Dihydrolipoyl dehydrogenase"
FT                   /id="PRO_0000068041"
FT   ACT_SITE        460
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         34..42
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         51
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         195..199
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         218
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         284..287
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         326
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         334
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   DISULFID        42..47
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        302
FT                   /note="K -> L (in Ref. 2; CAA72399)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        306..308
FT                   /note="GCV -> RWL (in Ref. 2; CAA72399)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        332..333
FT                   /note="ML -> IV (in Ref. 2; CAA72399)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        351
FT                   /note="L -> V (in Ref. 2; CAA72399)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        387
FT                   /note="R -> S (in Ref. 2; CAA72399)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        400
FT                   /note="G -> R (in Ref. 2; CAA72399)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        479..481
FT                   /note="Missing (in Ref. 2; CAA72399)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   481 AA;  50956 MW;  873F3ABC67179655 CRC64;
     MAESYDVIII GSGPGGYVAA IRASQLGLKT AIVEREHMGG ICLNWGCIPT KALLRSAEVL
     DHANHFKDFG LVLEGSVKPD AKAVVGRSRA VSARLNAGVG FLMKKNKIDI IWGEAKLTKP
     GEIVVGKSSK PVVEPQHPLP KNVKGEGTYT AKHIIIATGA RPRALPGIEP DGKLIWTYFE
     ALKPDALPKS LIVMGSGAIG IEFASFYRSM GVDVTVVEVM PTIMPVEDAE ITAIARKQLE
     KRGLKIFTSA KVTKVEKGAG SITAHVETSD GKVQQITADR MISAVGVQGN IENLGLEALG
     VKTDRGCVVA DGYGKTNVAG IYAIGDVAGP PMLAHKAEHE GVVCVEKIAG LPNVHPTDKG
     KVPGCTYCNP QVASVGLTEA KAKELGRDIR VGRFSFAANG KAIALGEDQG MVKVIFDKKT
     GELLGAHMVG AEVTELIQGF VVAMNLETTE EELMHTIFPH PTVSETMKEA VLDAYGRVLN
     A