DLDH_MYCLE
ID DLDH_MYCLE Reviewed; 467 AA.
AC Q50068;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Dihydrolipoyl dehydrogenase;
DE EC=1.8.1.4;
DE AltName: Full=Dihydrolipoamide dehydrogenase;
DE AltName: Full=E3 component of alpha-ketoacid dehydrogenase complexes;
GN Name=lpd; OrderedLocusNames=ML2387; ORFNames=u1740l;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Smith D.R., Robison K.;
RL Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
CC -!- FUNCTION: Lipoamide dehydrogenase is a component of the alpha-ketoacid
CC dehydrogenase complexes. Catalyzes the reoxidation of dihydrolipoyl
CC groups which are covalently attached to the lipoate acyltransferase
CC components (E2) of the complexes (By similarity). {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. Part of the PDH complex, consisting of multiple
CC copies of AceE (E1), DlaT (E2) and Lpd (E3), and of the BCKADH complex,
CC consisting of multiple copies of BkdA/BkdB (E1), BkdC (E2) and Lpd
CC (E3). {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; U15183; AAA63016.1; -; Genomic_DNA.
DR EMBL; AL583925; CAC31903.1; -; Genomic_DNA.
DR PIR; G87207; G87207.
DR RefSeq; NP_302544.1; NC_002677.1.
DR RefSeq; WP_010908864.1; NC_002677.1.
DR AlphaFoldDB; Q50068; -.
DR SMR; Q50068; -.
DR STRING; 272631.ML2387; -.
DR EnsemblBacteria; CAC31903; CAC31903; CAC31903.
DR KEGG; mle:ML2387; -.
DR PATRIC; fig|272631.5.peg.4593; -.
DR Leproma; ML2387; -.
DR eggNOG; COG1249; Bacteria.
DR HOGENOM; CLU_016755_0_2_11; -.
DR OMA; DAKYGEW; -.
DR Proteomes; UP000000806; 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 GO; GO:0006099; P:tricarboxylic acid cycle; 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;
KW Tricarboxylic acid cycle.
FT CHAIN 1..467
FT /note="Dihydrolipoyl dehydrogenase"
FT /id="PRO_0000068033"
FT ACT_SITE 446
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 33..41
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 50
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 113
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 181..185
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 204
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 269..272
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 312
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 320
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT DISULFID 41..46
FT /note="Redox-active"
FT /evidence="ECO:0000250"
SQ SEQUENCE 467 AA; 50077 MW; CA46B807119FC15A CRC64;
MTHYDVVVLG AGPGGYVAAI RAAQLGLSTA VVEPKYWGGI CLNVGCIPSK VLLHNAELAH
IFTKEAKTFG ISGDASFDYG IAYDRSRKVS EGRVAGVHFL MKKNKITEIH GYGRFTDANT
LSVELSEGVP ETPLKVTFNN VIIATGSKTR LVPGTLLSTN VITYEEQILT RELPDSIVIV
GAGAIGIEFG YVLKNYGVDV TIVEFLPRAM PNEDAEVSKE IEKQFKKMGI KILTGTKVES
ISDNGSHVLV AVSKDGQFQE LKADKVLQAI GFAPNVDGYG LDKVGVALTA DKAVDIDDYM
QTNVSHIYAI GDVTGKLQLA HVAEAQGVVA AEAIAGAETL ALSDYRMMPR ATFCQPNVAS
FGLTEQQARD GGYDVVVAKF PFTANAKAHG MGDPSGFVKL VADAKYGELL GGHMIGHNVS
ELLPELTLAQ KWDLTATELV RNVHTHPTLS EALQECFHGL IGHMINF
