ID   DLDH_CHLP8              Reviewed;         469 AA.
AC   O50311; B3QMJ0;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 2.
DT   16-JUN-2009, entry version 68.
DE   RecName: Full=Dihydrolipoyl dehydrogenase;
DE            EC=1.8.1.4;
DE   AltName: Full=Dihydrolipoamide dehydrogenase;
DE   AltName: Full=E3 component of pyruvate and 2-oxoglutarate dehydrogenases complexes;
GN   Name=lpd; OrderedLocusNames=Cpar_0724;
OS   Chlorobaculum parvum (strain NCIB 8327) (Chlorobium vibrioforme subsp.
OS   thiosulfatophilum (strain DSM 263 / NCIB 8327)).
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC   Chlorobaculum.
OX   NCBI_TaxID=517417;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Petersen B.L., Moeller M.G., Stummann B.M., Henningsen K.W.;
RT   "Clustering of genes with function in the biosynthesis of
RT   bacteriochlorophyll and heme in the green sulfur bacterium Chlorobium
RT   vibrioforme.";
RL   Hereditas 125:93-96(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Mikhailova N., Zhao F., Li T.,
RA   Liu Z., Overmann J., Bryant D.A., Richardson P.;
RT   "Complete sequence of Chlorobaculum parvum NCIB 8327.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Lipoamide dehydrogenase is a component of the alpha-
CC       ketoacid dehydrogenase complexes (By similarity).
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; Z83933; CAB06298.1; -; Genomic_DNA.
DR   EMBL; CP001099; ACF11143.1; -; Genomic_DNA.
DR   PIR; T17191; T17191.
DR   RefSeq; YP_001998343.1; -.
DR   HSSP; P11959; 1EBD.
DR   GeneID; 6419649; -.
DR   GenomeReviews; CP001099_GR; Cpar_0724.
DR   KEGG; cpc:Cpar_0724; -.
DR   OMA; O50311; GMLLAHK.
DR   BRENDA; 1.8.1.4; 190276.
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   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   Complete proteome; Cytoplasm; Disulfide bond; FAD; Flavoprotein;
KW   Glycolysis; NAD; Oxidoreductase; Redox-active center.
FT   CHAIN         1    469       Dihydrolipoyl dehydrogenase.
FT                                /FTId=PRO_0000068023.
FT   NP_BIND      40     48       FAD (By similarity).
FT   NP_BIND     186    190       NAD (By similarity).
FT   NP_BIND     275    278       NAD (By similarity).
FT   ACT_SITE    450    450       Proton acceptor (By similarity).
FT   BINDING      57     57       FAD (By similarity).
FT   BINDING     120    120       FAD; via amide nitrogen and carbonyl
FT                                oxygen (By similarity).
FT   BINDING     209    209       NAD (By similarity).
FT   BINDING     317    317       FAD (By similarity).
FT   BINDING     325    325       FAD; via amide nitrogen (By similarity).
FT   DISULFID     48     53       Redox-active (By similarity).
FT   CONFLICT     42     42       A -> R (in Ref. 1; CAB06298).
FT   CONFLICT    463    463       A -> S (in Ref. 1; CAB06298).
FT   CONFLICT    466    467       QS -> PN (in Ref. 1; CAB06298).
SQ   SEQUENCE   469 AA;  48755 MW;  97FDD6D88E8249F8 CRC64;
     MQQSESSSAQ FDVAVIGSGP GGYEAALHAA RHGMKVCLVE KASLGGVCVN WGCIPTKALL
     RSAEVYDLAK NPSEFGVNVS ELSFDLAQAV KRSRKVSLKS SKGVEFMLKK AKVEVWRGEA
     VLTGSKGVKV TAEDGSERSL EAANIIVATG AQPRVIPGLE PDGKKIITSR EALILKDVPE
     SMIVVGGGAI GVEMAWFYAK AGAKVTIVEL MPRLLPAEEA EVSEALKRSF EKVDITVQCG
     AKLGNVAISE FGVNADLLAE GKEPQKIEAS CMLVAVGVTG VIDGLGLDAA GIETERGFIR
     TDELCRTSAS GIYAIGDVRG GMLLAHKASA EAAIAVEAIA GKLPEPLSEP LIPRCVYAQP
     SVASVGLTEE AAIAAGYKVL VGRSQFAASG KANAYGQLEG FVKLVFNAET GKMLGGHLIG
     HDAVELIGEL GLACRYGVTA EGLVGTVHAH PTLSETVREA AFAALQSKG
//