ID   DLDH_ACHLA              Reviewed;         336 AA.
AC   P35484;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   16-JUN-2009, entry version 72.
DE   RecName: Full=Dihydrolipoyl dehydrogenase;
DE            EC=1.8.1.4;
DE   AltName: Full=Dihydrolipoamide dehydrogenase;
DE   AltName: Full=E3 component of pyruvate complex;
DE   Flags: Fragment;
GN   Name=pdhD;
OS   Acholeplasma laidlawii.
OC   Bacteria; Tenericutes; Mollicutes; Acholeplasmatales;
OC   Acholeplasmataceae; Acholeplasma.
OX   NCBI_TaxID=2148;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=92138635; PubMed=1735725;
RA   Wallbrandt P., Tegman V., Jonsson B.-H., Wieslander A.;
RT   "Identification and analysis of the genes coding for the putative
RT   pyruvate dehydrogenase enzyme complex in Acholeplasma laidlawii.";
RL   J. Bacteriol. 174:1388-1396(1992).
CC   -!- FUNCTION: Lipoamide dehydrogenase is a component of the alpha-
CC       ketoacid dehydrogenase complexes.
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.
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; M81753; AAA21910.1; -; Genomic_DNA.
DR   PIR; D42653; D42653.
DR   HSSP; P11959; 1EBD.
DR   BRENDA; 1.8.1.4; 96506.
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: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; IPR012999; Pyr_OxRdtase_I_AS.
DR   InterPro; IPR001327; Pyr_OxRdtase_NAD_bd.
DR   PANTHER; PTHR22912:SF20; Lipoamide_DH; 1.
DR   Pfam; PF00070; Pyr_redox; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00945; HGRDTASE.
DR   ProDom; PD000139; FAD_pyr_redox; 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.
FT   CHAIN         1   >336       Dihydrolipoyl dehydrogenase.
FT                                /FTId=PRO_0000068012.
FT   NP_BIND      34     42       FAD (By similarity).
FT   NP_BIND     180    184       NAD (By similarity).
FT   NP_BIND     264    267       NAD (By similarity).
FT   BINDING      51     51       FAD (By similarity).
FT   BINDING     115    115       FAD; via amide nitrogen and carbonyl
FT                                oxygen (By similarity).
FT   BINDING     203    203       NAD (By similarity).
FT   BINDING     237    237       NAD; via amide nitrogen (By similarity).
FT   BINDING     304    304       FAD (By similarity).
FT   BINDING     312    312       FAD; via amide nitrogen (By similarity).
FT   DISULFID     42     47       Redox-active (By similarity).
FT   NON_TER     336    336
SQ   SEQUENCE   336 AA;  35996 MW;  4405B1097279B36C CRC64;
     MSKEYEIIIV GGGPGGYVAA IKAAQYGAKV ALVEKEVVGG ICLNHGCIPT KTFLKSAKVF
     NTVKKSMDFG VSTSGEVGFD WSKIVSRKDG VVKQLTNGVA FLLKKNGVDV YNGFGDIKSA
     NEVVVNGESL KTKNVIIATG SSAVVPPIPG VKEAYEKGIV VTSRELLNVK NYPKSIVIVG
     GGVIGVEFAT VFNSFGSKVT IIEMMDGILP TMDDDIRVAY AKTLKRDGIE ILTKAEVKKV
     DDHKVTYSLD GKETTIEGDL ILMSVGTRAN SKGLEHLGLE MDRANIKTNE YLQTNVPGVY
     AIGDVNGKFM LAHVAEHEGI TAVQHILKIG HAKMNY
//