ID   DLDH_TRYBB              Reviewed;         479 AA.
AC   Q04933;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   16-JUN-2009, entry version 66.
DE   RecName: Full=Dihydrolipoyl dehydrogenase;
DE            EC=1.8.1.4;
DE   AltName: Full=Dihydrolipoamide dehydrogenase;
OS   Trypanosoma brucei brucei.
OC   Eukaryota; Euglenozoa; Kinetoplastida; Trypanosomatidae; Trypanosoma.
OX   NCBI_TaxID=5702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=93185661; PubMed=8444180;
RX   DOI=10.1111/j.1432-1033.1993.tb17678.x;
RA   Else A.J., Hough D.W., Danson M.J.;
RT   "Cloning, sequencing, and expression of Trypanosoma brucei
RT   dihydrolipoamide dehydrogenase.";
RL   Eur. J. Biochem. 212:423-429(1993).
CC   -!- CATALYTIC ACTIVITY: Protein N(6)-(dihydrolipoyl)lysine + NAD(+) =
CC       protein N(6)-(lipoyl)lysine + NADH.
CC   -!- COFACTOR: Binds 1 FAD per subunit (By similarity).
CC   -!- SUBUNIT: Homodimer.
CC   -!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
CC   -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC       oxidoreductase family.
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DR   EMBL; X70646; CAA49991.1; -; Genomic_DNA.
DR   PIR; S30057; S30057.
DR   HSSP; P31023; 1DXL.
DR   BRENDA; 1.8.1.4; 74165.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; IEA:EC.
DR   GO; GO:0050660; F:FAD binding; IEA:InterPro.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   GO; GO:0006096; P:glycolysis; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR013027; FAD_pyr_nucl-diS_OxRdtase.
DR   InterPro; IPR000815; Hg_reductase.
DR   InterPro; IPR006258; Lipoamide_DH.
DR   InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR   InterPro; IPR001327; Pyr_OxRdtase_NAD_bd.
DR   Gene3D; G3DSA:3.30.390.30; Pyr_redox_dim; 1.
DR   PANTHER; PTHR22912:SF20; Lipoamide_DH; 1.
DR   Pfam; PF00070; Pyr_redox; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF02852; Pyr_redox_dim; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00945; HGRDTASE.
DR   ProDom; PD000139; FAD_pyr_redox; 1.
DR   TIGRFAMs; TIGR01350; lipoamide_DH; 1.
DR   PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; FAD; Flavoprotein; Glycolysis; NAD; Oxidoreductase;
KW   Redox-active center.
FT   CHAIN         1    479       Dihydrolipoyl dehydrogenase.
FT                                /FTId=PRO_0000068008.
FT   NP_BIND      41     50       FAD (By similarity).
FT   NP_BIND     153    155       FAD (By similarity).
FT   NP_BIND     190    197       NAD (By similarity).
FT   NP_BIND     332    335       FAD (By similarity).
FT   ACT_SITE    458    458       Proton acceptor (By similarity).
FT   BINDING      59     59       FAD (By similarity).
FT   BINDING     124    124       FAD; via amide nitrogen and carbonyl
FT                                oxygen (By similarity).
FT   BINDING     213    213       NAD (By similarity).
FT   BINDING     247    247       NAD; via amide nitrogen and carbonyl
FT                                oxygen (By similarity).
FT   BINDING     284    284       NAD; via amide nitrogen (By similarity).
FT   BINDING     325    325       FAD (By similarity).
FT   DISULFID     50     55       Redox-active (By similarity).
SQ   SEQUENCE   479 AA;  50220 MW;  ABE40113CDFAF830 CRC64;
     MFRRCFPIFN PYDVVVVGGG PGGYVAAIKA AQLGLKTACV EKRGALGGTC LNVGCIPSKA
     LLHATHMYHD AHANFERYGL MGGAGVTMDV AKMQQQKEKS VNGLTSGVEY LLKKNKVTYY
     KGEAGFVTPN TLNVKGIDGK DEAIEAKNTI IATGSEPTAL PFLPFDEKVV LSSTGALALQ
     QVPKKMVVIG GGVIGLELGS VWARLGSDVT VVEFAPRCAP TLDSDVTDAL VGALKRNGED
     EVPMTGIEGV NGTNNGSIAL TLEVEQAGGQ AETLHCDALL VSVGRRPYTA GLGLEKNNVS
     LNERGFVKIG SHFETNVAGV YAIGDVVDKG PMLAHKAEDE GVACAEILAG RPGHVNYDVI
     PGVIYTMPEV ASVGKTEEEL KKAGVAYKVG KFPFNANSRA KAVATEDGFV KVLTDKATDR
     ILGVHIVCSA AGELIAGALL AMEYGASSED VGRTCHAHPT MSEAVKEACM ACFAKTINF
//