ID A9W391_METEP Unreviewed; 467 AA.
AC A9W391;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 04-FEB-2015, entry version 57.
DE RecName: Full=Dihydrolipoyl dehydrogenase {ECO:0000256|RuleBase:RU003692};
DE EC=1.8.1.4 {ECO:0000256|RuleBase:RU003692};
GN OrderedLocusNames=Mext_1648 {ECO:0000313|EMBL:ABY30047.1};
OS Methylobacterium extorquens (strain PA1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC Methylobacteriaceae; Methylobacterium.
OX NCBI_TaxID=419610 {ECO:0000313|EMBL:ABY30047.1, ECO:0000313|Proteomes:UP000008546};
RN [1] {ECO:0000313|EMBL:ABY30047.1, ECO:0000313|Proteomes:UP000008546}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PA1 {ECO:0000313|EMBL:ABY30047.1,
RC ECO:0000313|Proteomes:UP000008546};
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 {ECO:0000256|RuleBase:RU003692}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|RuleBase:RU003692};
CC Note=Binds 1 FAD per subunit. {ECO:0000256|RuleBase:RU003692};
CC -!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
CC {ECO:0000256|RuleBase:RU003692}.
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|RuleBase:RU003691}.
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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; HDDPRVW; -.
DR OrthoDB; EOG6QCD6D; -.
DR BioCyc; MEXT419610:GI32-1687-MONOMER; -.
DR Proteomes; UP000008546; Chromosome.
DR GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; IEA:UniProtKB-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 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; SSF55424; 1.
DR TIGRFAMs; TIGR01350; lipoamide_DH; 1.
DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE 3: Inferred from homology;
KW Complete proteome {ECO:0000313|Proteomes:UP000008546};
KW FAD {ECO:0000256|RuleBase:RU003691};
KW Flavoprotein {ECO:0000256|RuleBase:RU003691};
KW NAD {ECO:0000256|RuleBase:RU003692};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003691};
KW Redox-active center {ECO:0000256|RuleBase:RU003691}.
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
//
