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Dihydrolipoyl dehydrogenase (LPD) (EC 1.8.1.4) (Component of peroxynitrite reductase/peroxidase complex) (Component of PNR/P) (Dihydrolipoamide dehydrogenase) (E3 component of alpha-ketoacid dehydrogenase complexes)

 DLDH_MYCTO              Reviewed;         464 AA.
P9WHH8; L0T3N4; O53747; P66004;
16-APR-2014, integrated into UniProtKB/Swiss-Prot.
16-APR-2014, sequence version 1.
22-NOV-2017, entry version 29.
RecName: Full=Dihydrolipoyl dehydrogenase;
Short=LPD;
EC=1.8.1.4;
AltName: Full=Component of peroxynitrite reductase/peroxidase complex;
Short=Component of PNR/P;
AltName: Full=Dihydrolipoamide dehydrogenase;
AltName: Full=E3 component of alpha-ketoacid dehydrogenase complexes;
Name=lpdC; Synonyms=lpd; OrderedLocusNames=MT0478;
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
Mycobacterium; Mycobacterium tuberculosis complex.
NCBI_TaxID=83331;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=CDC 1551 / Oshkosh;
PubMed=12218036; DOI=10.1128/JB.184.19.5479-5490.2002;
Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H.,
Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D.,
Salzberg S.L., Delcher A., Utterback T.R., Weidman J.F., Khouri H.M.,
Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C.,
Fraser C.M.;
"Whole-genome comparison of Mycobacterium tuberculosis clinical and
laboratory strains.";
J. Bacteriol. 184:5479-5490(2002).
-!- FUNCTION: Lipoamide dehydrogenase is an essential component of the
alpha-ketoacid dehydrogenase complexes, namely the pyruvate
dehydrogenase (PDH) complex, the branched-chain alpha-ketoacid
dehydrogenase (BCKADH) complex, and likely also the 2-oxoglutarate
dehydrogenase (ODH) complex. Catalyzes the reoxidation of
dihydrolipoyl groups which are covalently attached to the lipoate
acyltransferase components (E2) of the complexes (By similarity).
{ECO:0000250}.
-!- FUNCTION: Together with AhpC, AhpD and DlaT, Lpd constitutes an
NADH-dependent peroxidase active against hydrogen and alkyl
peroxides as well as serving as a peroxynitrite reductase, thus
protecting the bacterium against reactive nitrogen intermediates
and oxidative stress generated by the host immune system.
{ECO:0000250}.
-!- FUNCTION: Appears to be essential for Mtb pathogenesis.
{ECO:0000250}.
-!- CATALYTIC ACTIVITY: Protein N(6)-(dihydrolipoyl)lysine + NAD(+) =
protein N(6)-(lipoyl)lysine + NADH.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
Note=Binds 1 FAD per subunit. {ECO:0000250};
-!- SUBUNIT: Homodimer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
-!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
oxidoreductase family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AE000516; AAK44702.1; -; Genomic_DNA.
PIR; B70828; B70828.
RefSeq; WP_003402301.1; NZ_KK341227.1.
ProteinModelPortal; P9WHH8; -.
SMR; P9WHH8; -.
BindingDB; P9WHH8; -.
PRIDE; P9WHH8; -.
EnsemblBacteria; AAK44702; AAK44702; MT0478.
KEGG; mtc:MT0478; -.
PATRIC; fig|83331.31.peg.508; -.
KO; K00382; -.
OrthoDB; POG091H0239; -.
Proteomes; UP000001020; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0016209; F:antioxidant activity; IEA:UniProtKB-KW.
GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; IEA:UniProtKB-EC.
GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
Gene3D; 3.30.390.30; -; 1.
Gene3D; 3.50.50.60; -; 2.
InterPro; IPR036188; FAD/NAD-bd_sf.
InterPro; IPR023753; FAD/NAD-binding_dom.
InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
InterPro; IPR006258; Lipoamide_DH.
InterPro; IPR001100; Pyr_nuc-diS_OxRdtase.
InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
InterPro; IPR012999; Pyr_OxRdtase_I_AS.
Pfam; PF07992; Pyr_redox_2; 1.
Pfam; PF02852; Pyr_redox_dim; 1.
PIRSF; PIRSF000350; Mercury_reductase_MerA; 1.
SUPFAM; SSF51905; SSF51905; 1.
SUPFAM; SSF55424; SSF55424; 1.
TIGRFAMs; TIGR01350; lipoamide_DH; 1.
PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
3: Inferred from homology;
Antioxidant; Complete proteome; Cytoplasm; Disulfide bond; FAD;
Flavoprotein; Glycolysis; NAD; Oxidoreductase; Redox-active center;
Tricarboxylic acid cycle; Virulence.
CHAIN 1 464 Dihydrolipoyl dehydrogenase.
/FTId=PRO_0000428184.
NP_BIND 33 41 FAD. {ECO:0000250}.
NP_BIND 178 182 NAD. {ECO:0000250}.
NP_BIND 266 269 NAD. {ECO:0000250}.
ACT_SITE 443 443 Proton acceptor. {ECO:0000250}.
BINDING 50 50 FAD.
BINDING 113 113 FAD; via amide nitrogen and carbonyl
oxygen. {ECO:0000250}.
BINDING 201 201 NAD. {ECO:0000250}.
BINDING 309 309 FAD. {ECO:0000250}.
BINDING 317 317 FAD; via amide nitrogen. {ECO:0000250}.
DISULFID 41 46 Redox-active. {ECO:0000250}.
SEQUENCE 464 AA; 49239 MW; DD93D95DC6F76B22 CRC64;
MTHYDVVVLG AGPGGYVAAI RAAQLGLSTA IVEPKYWGGV CLNVGCIPSK ALLRNAELVH
IFTKDAKAFG ISGEVTFDYG IAYDRSRKVA EGRVAGVHFL MKKNKITEIH GYGTFADANT
LLVDLNDGGT ESVTFDNAII ATGSSTRLVP GTSLSANVVT YEEQILSREL PKSIIIAGAG
AIGMEFGYVL KNYGVDVTIV EFLPRALPNE DADVSKEIEK QFKKLGVTIL TATKVESIAD
GGSQVTVTVT KDGVAQELKA EKVLQAIGFA PNVEGYGLDK AGVALTDRKA IGVDDYMRTN
VGHIYAIGDV NGLLQLAHVA EAQGVVAAET IAGAETLTLG DHRMLPRATF CQPNVASFGL
TEQQARNEGY DVVVAKFPFT ANAKAHGVGD PSGFVKLVAD AKHGELLGGH LVGHDVAELL
PELTLAQRWD LTASELARNV HTHPTMSEAL QECFHGLVGH MINF


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