ID   DLDH_MANSE              Reviewed;         497 AA.
AC   O18480;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   16-JUN-2009, entry version 67.
DE   RecName: Full=Dihydrolipoyl dehydrogenase;
DE            EC=1.8.1.4;
DE   AltName: Full=Dihydrolipoamide dehydrogenase;
DE   AltName: Full=E3;
OS   Manduca sexta (Tobacco hawkmoth) (Tobacco hornworm).
OC   Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC   Sphingidae; Sphinginae; Sphingini; Manduca.
OX   NCBI_TaxID=7130;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=98038988; PubMed=9373151; DOI=10.1016/S0378-1119(97)00413-7;
RA   Pullikuth A.K., Gill S.S.;
RT   "Primary structure of an invertebrate dihydrolipoamide dehydrogenase
RT   with phylogenetic relationship to vertebrate and bacterial disulfide
RT   oxidoreductases.";
RL   Gene 200:163-172(1997).
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 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Potential).
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; AF008586; AAB88282.1; -; mRNA.
DR   HSSP; P31023; 1DXL.
DR   BRENDA; 1.8.1.4; 15145.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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   2: Evidence at transcript level;
KW   Cytoplasm; Disulfide bond; FAD; Flavoprotein; Glycolysis; NAD;
KW   Oxidoreductase; Redox-active center.
FT   CHAIN         1    497       Dihydrolipoyl dehydrogenase.
FT                                /FTId=PRO_0000068007.
FT   NP_BIND      60     69       FAD (By similarity).
FT   NP_BIND     170    172       FAD (By similarity).
FT   NP_BIND     207    214       NAD (By similarity).
FT   NP_BIND     349    352       FAD (By similarity).
FT   ACT_SITE    475    475       Proton acceptor (By similarity).
FT   BINDING      78     78       FAD (By similarity).
FT   BINDING     142    142       FAD; via amide nitrogen and carbonyl
FT                                oxygen (By similarity).
FT   BINDING     230    230       NAD (By similarity).
FT   BINDING     264    264       NAD; via amide nitrogen and carbonyl
FT                                oxygen (By similarity).
FT   BINDING     302    302       NAD; via amide nitrogen (By similarity).
FT   BINDING     343    343       FAD (By similarity).
FT   DISULFID     69     74       Redox-active (By similarity).
SQ   SEQUENCE   497 AA;  53083 MW;  1689E564E165137A CRC64;
     MGYKFLKLAS ASFRNGGVRI VSRQYSTTHD ADLVVIGAGP GGYVAAIKAA QLGMKVVSVE
     KEPSLGGTCL NVGCIPSKAL LHNTHLYHMA KHDFKHRGIE TGEVKFNFKA MMDYKVNAVK
     ALTGGIAMLF QKNKVKLVRG AGTIVAPNKV EVKGEKGVET VNTKNILIAT GSEVTPFPGV
     TFDEKQIITS TGALSLESVP KKMLVIGAGV IGLELGSVYQ RLGADVTAIE FLGSIGGIGI
     DMEVSKDYRI LAKQGMKFKL ETKVLGVKKE GSTVKVEDVS IEGAKGGNKE TMDCDVVLIS
     IGRRPYTKDL GLDKVGIALD DRGRVPVNNK FQTTVPGIYA IGDVIHGPML AHKAEDEGIV
     CVEGIKGMPV HFNYDAIPSV IYTSPEVGWV RKTEEDLKKE GKAYKVRKFP FLANSRAKTN
     GEPDGFVKVL SDKATDVILG THIIGPGGGE LINEAVLAQE YGAAAEDVAR VCHAHPTCAE
     ALREANLAAY CGKPINF
//