ID   A9W391_METEP            Unreviewed;       467 AA.
AC   A9W391;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   01-MAY-2013, entry version 48.
DE   RecName: Full=Dihydrolipoyl dehydrogenase;
DE            EC=1.8.1.4;
GN   OrderedLocusNames=Mext_1648;
OS   Methylobacterium extorquens (strain PA1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Methylobacteriaceae; Methylobacterium.
OX   NCBI_TaxID=419610;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PA1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Saunders E., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Marx C., Richardson P.;
RT   "Complete sequence of Methylobacterium extorquens PA1.";
RL   Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
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   -!- 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; CP000908; ABY30047.1; -; Genomic_DNA.
DR   RefSeq; YP_001639118.1; NC_010172.1.
DR   ProteinModelPortal; A9W391; -.
DR   SMR; A9W391; 2-467.
DR   STRING; 419610.Mext_1648; -.
DR   EnsemblBacteria; ABY30047; ABY30047; Mext_1648.
DR   GeneID; 5832618; -.
DR   KEGG; mex:Mext_1648; -.
DR   PATRIC; 22533787; VBIMetExt98426_1654.
DR   eggNOG; COG1249; -.
DR   HOGENOM; HOG000276708; -.
DR   KO; K00382; -.
DR   OMA; HIVGFGA; -.
DR   ProtClustDB; PRK06292; -.
DR   BioCyc; MEXT419610:GI32-1687-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; IEA:EC.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   Gene3D; 3.30.390.30; -; 1.
DR   InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer.
DR   InterPro; IPR013027; FAD_pyr_nucl-diS_OxRdtase.
DR   InterPro; IPR006258; Lipoamide_DH.
DR   InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   InterPro; IPR023753; Pyr_nucl-diS_OxRdtase_FAD/NAD.
DR   InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR   InterPro; IPR001327; Pyr_OxRdtase_NAD-bd_dom.
DR   PANTHER; PTHR22912:SF20; PTHR22912:SF20; 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   SUPFAM; SSF55424; FAD/NAD-linked_reductase_dimer; 1.
DR   TIGRFAMs; TIGR01350; lipoamide_DH; 1.
DR   PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE   3: Inferred from homology;
KW   Complete proteome; FAD; Flavoprotein; NAD; Oxidoreductase;
KW   Redox-active center.
SQ   SEQUENCE   467 AA;  48967 MW;  6B18C32097726FCF CRC64;
     MSYDLIVIGT GPGGYVCAIR AAQLGLKTAV VEKRATHGGT CLNVGCIPSK ALLHASEAFE
     EANKHFSELG IDVGTPKLDL KKMQSFKQSG VDGNTKGVEF LLKKNKVDTY HGRGRIAGAG
     RVEVISDDGG NQLLETKNIV IATGSDVTRL PGVEIDEKTV VSSTGALELA EVPKRLVVIG
     AGVIGLELGS VWRRLGAEVT VIEYLDRVLP GMDGEVGKQF QRILAKQGMV FKLSTKVTGV
     ETGKKGRATV TVEPAQGGEP EKLEADVVLV AIGRVPYTEG LGLETVGVAT DDKGRIEVDS
     HYATNVTGIY AIGDVIAGPM LAHKAEDEGV AVAEILAGQS GHVNYGVIPN VVYTFPEVAS
     VGKTEEELKK DGIAYNVGKF PFTANGRAKA NGTTDGFVKI LADAQSDRVL GVHIVGADAG
     NLIAEVAVAM EFAASAEDIA RTCHAHPTLT EAIKEAALAV DKRAIHV
//