ID   DLDH_CHLTE              Reviewed;         469 AA.
AC   Q8KCW2;
DT   25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   16-JUN-2009, entry version 54.
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; Synonyms=lpd-1; OrderedLocusNames=CT1298;
OS   Chlorobium tepidum.
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC   Chlorobaculum.
OX   NCBI_TaxID=1097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49652 / DSM 12025 / TLS;
RX   MEDLINE=22103685; PubMed=12093901; DOI=10.1073/pnas.132181499;
RA   Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M.,
RA   Dodson R.J., DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H.,
RA   Hickey E.K., Peterson J.D., Durkin A.S., Kolonay J.F., Yang F.,
RA   Holt I.E., Umayam L.A., Mason T.M., Brenner M., Shea T.P.,
RA   Parksey D.S., Nierman W.C., Feldblyum T.V., Hansen C.L., Craven M.B.,
RA   Radune D., Vamathevan J.J., Khouri H.M., White O., Gruber T.M.,
RA   Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A., Fraser C.M.;
RT   "The complete genome sequence of Chlorobium tepidum TLS, a
RT   photosynthetic, anaerobic, green-sulfur bacterium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002).
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; AE006470; AAM72528.1; -; Genomic_DNA.
DR   RefSeq; NP_662186.1; -.
DR   HSSP; P11959; 1EBD.
DR   GeneID; 1006658; -.
DR   GenomeReviews; AE006470_GR; CT1298.
DR   KEGG; cte:CT1298; -.
DR   TIGR; CT1298; -.
DR   HOGENOM; Q8KCW2; -.
DR   OMA; Q8KCW2; GMLLAHK.
DR   BioCyc; CTEP194439:CT_1298-MON; -.
DR   BRENDA; 1.8.1.4; 189605.
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   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_0000068022.
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).
SQ   SEQUENCE   469 AA;  48007 MW;  CEEB79308FD4DC4E CRC64;
     MQQADTLAAQ FDVAVIGSGP GGYEAAIHAA RYGLKTCIVE KAVLGGVCVN WGCIPTKALL
     RSAEVFDLAK NPETFGVNVG NVSFDLAQAV KRSRNVALKS SKGVAYLLKK AAVEVLAGEA
     VLTGGAGVMV TMPDGSVRML GAKNIIVATG STPRVIPGLE PDGKKIITSR EALILKEVPK
     SMIVVGGGAI GVEMAWFYAK AGSKVTIVEL MPRMLPAEEA EVSEALKRSF EKAGITVHCG
     AKLDNVAVSE SGVSAELVVE GSAPQTLNAS CLLVAVGVTG AIDGLGLDAV GVETERGFIR
     TDGQCRTSAP GIYAIGDVRG GMLLAHKASA EAAIAVEAIA GKSPEPLSEP LIPRCVYAQP
     SVASVGLTEE AAVNAGYQVA VGRSQFAASG KANAYGQLEG FVKLVFDAAT GKMLGGHLIG
     HDAVELIGEL GLACRYGVTA GGLVNTVHAH PTLSETVREA AFDALQSMG
//