DLDH_CORGL
ID DLDH_CORGL Reviewed; 469 AA.
AC Q8NTE1; Q6M7Z6; Q9Z466;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Dihydrolipoyl dehydrogenase;
DE Short=LPD;
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=Cgl0366, cg0441;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-15, FUNCTION,
RP CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=11495999; DOI=10.1099/00221287-147-8-2223;
RA Schwinde J.W., Hertz P.F., Sahm H., Eikmanns B.J., Guyonvarch A.;
RT "Lipoamide dehydrogenase from Corynebacterium glutamicum: molecular and
RT physiological analysis of the lpd gene and characterization of the
RT enzyme.";
RL Microbiology 147:2223-2231(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
RN [4]
RP IDENTIFICATION IN THE ODH/PDH COMPLEX.
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=16522631; DOI=10.1074/jbc.m512515200;
RA Niebisch A., Kabus A., Schultz C., Weil B., Bott M.;
RT "Corynebacterial protein kinase G controls 2-oxoglutarate dehydrogenase
RT activity via the phosphorylation status of the OdhI protein.";
RL J. Biol. Chem. 281:12300-12307(2006).
CC -!- FUNCTION: Lipoamide dehydrogenase is an essential component of the
CC pyruvate dehydrogenase (PDH) and 2-oxoglutarate dehydrogenase (ODH)
CC complexes. Catalyzes the reoxidation of dihydrolipoyl groups which are
CC covalently attached to the lipoate acyltransferase components (E2) of
CC the complexes. Also catalyzes a reversible NADH:NAD(+)
CC transhydrogenation, and is able to transfer electrons from NADH to
CC various redox-active compounds and quinones. May be involved in quinone
CC redox cycling in C.glutamicum. {ECO:0000269|PubMed:11495999}.
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 Evidence={ECO:0000269|PubMed:11495999};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:11495999};
CC Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:11495999};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.636 uM for lipoate {ECO:0000269|PubMed:11495999};
CC pH dependence:
CC Optimum pH is 7.0-7.5 for the reduction of lipoate by NADH.
CC {ECO:0000269|PubMed:11495999};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius for the reduction of
CC lipoate by NADH. {ECO:0000269|PubMed:11495999};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinyl-
CC CoA from 2-oxoglutarate (dehydrogenase route): step 1/1.
CC -!- SUBUNIT: Homodimer (By similarity). Part of an unusual ODH/PDH
CC supercomplex, consisting of AceE (E1), AceF (E2), and Lpd (E3) together
CC with OdhA (E1+E2). {ECO:0000250, ECO:0000269|PubMed:16522631}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11495999}.
CC -!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: Overexpression of LPD enhances sensitivity to menadione,
CC but has no effect on sensitivity to paraquat or hydrogen peroxide.
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; Y16642; CAA76340.1; -; Genomic_DNA.
DR EMBL; BA000036; BAB97759.1; -; Genomic_DNA.
DR EMBL; BX927149; CAF19080.1; -; Genomic_DNA.
DR RefSeq; NP_599614.1; NC_003450.3.
DR RefSeq; WP_011013602.1; NC_006958.1.
DR AlphaFoldDB; Q8NTE1; -.
DR SMR; Q8NTE1; -.
DR STRING; 196627.cg0441; -.
DR KEGG; cgb:cg0441; -.
DR KEGG; cgl:Cgl0366; -.
DR PATRIC; fig|196627.13.peg.366; -.
DR eggNOG; COG1249; Bacteria.
DR HOGENOM; CLU_016755_0_2_11; -.
DR OMA; DAKYGEW; -.
DR BRENDA; 1.2.1.104; 960.
DR BRENDA; 1.2.1.105; 960.
DR BRENDA; 1.8.1.4; 960.
DR SABIO-RK; Q8NTE1; -.
DR UniPathway; UPA00223; UER00997.
DR Proteomes; UP000000582; 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-UniPathway.
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 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Disulfide bond; FAD; Flavoprotein;
KW Glycolysis; NAD; Oxidoreductase; Redox-active center; Reference proteome;
KW Tricarboxylic acid cycle.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:11495999"
FT CHAIN 2..469
FT /note="Dihydrolipoyl dehydrogenase"
FT /id="PRO_0000420523"
FT ACT_SITE 448
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 114
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 179..183
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 202
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 42..47
FT /note="Redox-active"
FT /evidence="ECO:0000250"
FT CONFLICT 382
FT /note="F -> L (in Ref. 1; CAA76340)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 469 AA; 50652 MW; 7F8FFE6B510B8725 CRC64;
MTEHYDVVVL GAGPGGYVSA IRAAQLGKKV AVIEKQYWGG VCLNVGCIPS KSLIKNAEVA
HTFTHEKKTF GINGEVTFNY EDAHKRSRGV SDKIVGGVHY LMKKNKIIEI HGLGNFKDAK
TLEVTDGKDA GKTITFDDCI IATGSVVNTL RGVDFSENVV SFEEQILNPV APKKMVIVGA
GAIGMEFAYV LGNYGVDVTV IEFMDRVLPN EDAEVSKVIA KAYKKMGVKL LPGHATTAVR
DNGDFVEVDY QKKGSDKTET LTVDRVMVSV GFRPRVEGFG LENTGVKLTE RGAIEIDDYM
RTNVDGIYAI GDVTAKLQLA HVAEAQGIVA AETIAGAETQ TLGDYMMMPR ATFCNPQVSS
FGYTEEQAKE KWPDREIKVA SFPFSANGKA VGLAETDGFA KIVADAEFGE LLGAHLVGAN
ASELINELVL AQNWDLTTEE ISRSVHIHPT LSEAVKEAAH GISGHMINF
