DLDH_CHLP8
ID DLDH_CHLP8 Reviewed; 469 AA.
AC O50311; B3QMJ0;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 2.
DT 03-AUG-2022, entry version 135.
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;
GN Name=lpd; OrderedLocusNames=Cpar_0724;
OS Chlorobaculum parvum (strain DSM 263 / NCIMB 8327) (Chlorobium vibrioforme
OS subsp. thiosulfatophilum).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; Chlorobaculum.
OX NCBI_TaxID=517417;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Petersen B.L., Moeller M.G., Stummann B.M., Henningsen K.W.;
RT "Clustering of genes with function in the biosynthesis of
RT bacteriochlorophyll and heme in the green sulfur bacterium Chlorobium
RT vibrioforme.";
RL Hereditas 125:93-96(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 263 / NCIMB 8327;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Zhao F., Li T., Liu Z., Overmann J.,
RA Bryant D.A., Richardson P.;
RT "Complete sequence of Chlorobaculum parvum NCIB 8327.";
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
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; Z83933; CAB06298.1; -; Genomic_DNA.
DR EMBL; CP001099; ACF11143.1; -; Genomic_DNA.
DR PIR; T17191; T17191.
DR RefSeq; WP_012501976.1; NC_011027.1.
DR AlphaFoldDB; O50311; -.
DR SMR; O50311; -.
DR STRING; 517417.Cpar_0724; -.
DR EnsemblBacteria; ACF11143; ACF11143; Cpar_0724.
DR KEGG; cpc:Cpar_0724; -.
DR eggNOG; COG1249; Bacteria.
DR HOGENOM; CLU_016755_0_3_10; -.
DR OMA; DAKYGEW; -.
DR OrthoDB; 267896at2; -.
DR Proteomes; UP000008811; 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.
FT CHAIN 1..469
FT /note="Dihydrolipoyl dehydrogenase"
FT /id="PRO_0000068023"
FT ACT_SITE 450
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 40..48
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 57
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 120
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 186..190
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 209
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 275..278
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 317
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 325
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT DISULFID 48..53
FT /note="Redox-active"
FT /evidence="ECO:0000250"
FT CONFLICT 42
FT /note="A -> R (in Ref. 1; CAB06298)"
FT /evidence="ECO:0000305"
FT CONFLICT 463
FT /note="A -> S (in Ref. 1; CAB06298)"
FT /evidence="ECO:0000305"
FT CONFLICT 466..467
FT /note="QS -> PN (in Ref. 1; CAB06298)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 469 AA; 48755 MW; 97FDD6D88E8249F8 CRC64;
MQQSESSSAQ FDVAVIGSGP GGYEAALHAA RHGMKVCLVE KASLGGVCVN WGCIPTKALL
RSAEVYDLAK NPSEFGVNVS ELSFDLAQAV KRSRKVSLKS SKGVEFMLKK AKVEVWRGEA
VLTGSKGVKV TAEDGSERSL EAANIIVATG AQPRVIPGLE PDGKKIITSR EALILKDVPE
SMIVVGGGAI GVEMAWFYAK AGAKVTIVEL MPRLLPAEEA EVSEALKRSF EKVDITVQCG
AKLGNVAISE FGVNADLLAE GKEPQKIEAS CMLVAVGVTG VIDGLGLDAA GIETERGFIR
TDELCRTSAS GIYAIGDVRG GMLLAHKASA EAAIAVEAIA GKLPEPLSEP LIPRCVYAQP
SVASVGLTEE AAIAAGYKVL VGRSQFAASG KANAYGQLEG FVKLVFNAET GKMLGGHLIG
HDAVELIGEL GLACRYGVTA EGLVGTVHAH PTLSETVREA AFAALQSKG
