ID   DLDH_BUCAP              Reviewed;         476 AA.
AC   Q8K9T7;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   16-DEC-2008, entry version 55.
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=lpdA; OrderedLocusNames=BUsg_201;
OS   Buchnera aphidicola subsp. Schizaphis graminum.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Buchnera.
OX   NCBI_TaxID=98794;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=22084549; PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(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 (By similarity).
CC   -!- MISCELLANEOUS: The active site is a redox-active disulfide bond
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC       oxidoreductase family.
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DR   EMBL; AE013218; AAM67765.1; -; Genomic_DNA.
DR   RefSeq; NP_660554.1; -.
DR   HSSP; Q51225; 1OJT.
DR   GeneID; 1005398; -.
DR   GenomeReviews; AE013218_GR; BUsg_201.
DR   KEGG; bas:BUsg201; -.
DR   HOGENOM; Q8K9T7; -.
DR   BioCyc; BAPH198804:BUSG201-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; IEA:InterPro.
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; IPR000759; Adrndx_reductase.
DR   InterPro; IPR013027; FAD_pyr_nucl-diS_OxRdtase.
DR   InterPro; IPR000815; Hg_reductase.
DR   InterPro; IPR006258; Lipoamide_DHase.
DR   InterPro; IPR001100; Pyr_nuc-diS_OxRdtase.
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; PR00419; ADXRDTASE.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00945; HGRDTASE.
DR   PRINTS; PR00411; PNDRDTASEI.
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; FAD; Flavoprotein; Glycolysis; NAD;
KW   Oxidoreductase; Redox-active center.
FT   CHAIN         1    476       Dihydrolipoyl dehydrogenase.
FT                                /FTId=PRO_0000068020.
FT   NP_BIND      36     45       FAD (By similarity).
FT   NP_BIND     182    186       NAD (By similarity).
FT   NP_BIND     271    274       NAD (By similarity).
FT   ACT_SITE    446    446       Proton acceptor (By similarity).
FT   BINDING      54     54       FAD (By similarity).
FT   BINDING     117    117       FAD; via amide nitrogen and carbonyl
FT                                oxygen (By similarity).
FT   BINDING     205    205       NAD (By similarity).
FT   BINDING     238    238       NAD; via amide nitrogen (By similarity).
FT   BINDING     314    314       FAD (By similarity).
FT   BINDING     322    322       FAD; via amide nitrogen (By similarity).
FT   DISULFID     45     50       Redox-active (By similarity).
SQ   SEQUENCE   476 AA;  52187 MW;  2BCD5F1ECB08BA58 CRC64;
     MHQEIQSEVV IIGSGPAGYS AAFRCADLGL ETVLIEHQER LGGVCLNVGC IPSKSLLHIA
     KIIKDASELS ESGVFFNKPI IDIKKINNWK EKIIKKLTTG LSNMGEKRKV RIVQGKALFN
     TDHSVLVKNK KNDFTIFFKH AIIATGSKPI KIPSLPNEDN RIWNSTDALS LKSIPNRFLI
     IGGGIIGLEM ATIYSALGSK VDIVDRFNAF LPSVDKDITD IYIKSIKKRF KLLLNTHVKS
     VEKSKDNDLI VKIAEENSDE NVCCYDNILV AIGRSPNVDF LGLEKIGLKL NESGFIEINQ
     QLKTNISHIY AIGDVTGFPM LAHKAVQQAH IAAEVISGKK HYFEPKVIPS VAYTDPEIAW
     VGLSEKEAEN NDIDYEVSLF PWSASGRAHA SNCTLGMTKL IFNKNTNKII GGSIIGTNAS
     ELISEIGLAI EMGSDAEDIS LTIHPHPTLS ESISLASEVF QGTITDLLNL KKSLLN
//