ID   Q0HN57_SHESM            Unreviewed;       475 AA.
AC   Q0HN57;
DT   03-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2006, sequence version 1.
DT   01-MAY-2013, entry version 54.
DE   RecName: Full=Dihydrolipoyl dehydrogenase;
DE            EC=1.8.1.4;
GN   OrderedLocusNames=Shewmr4_0430;
OS   Shewanella sp. (strain MR-4).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=60480;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR-4;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Nealson K., Konstantinidis K., Klappenbach J.,
RA   Tiedje J., Richardson P.;
RT   "Complete sequence of Shewanella sp. MR-4.";
RL   Submitted (AUG-2006) 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; CP000446; ABI37510.1; -; Genomic_DNA.
DR   RefSeq; YP_732567.1; NC_008321.1.
DR   ProteinModelPortal; Q0HN57; -.
DR   SMR; Q0HN57; 19-471.
DR   STRING; 60480.Shewmr4_0430; -.
DR   EnsemblBacteria; ABI37510; ABI37510; Shewmr4_0430.
DR   GeneID; 4251904; -.
DR   KEGG; she:Shewmr4_0430; -.
DR   PATRIC; 23577290; VBISheSp133532_0446.
DR   eggNOG; COG1249; -.
DR   HOGENOM; HOG000276708; -.
DR   KO; K00382; -.
DR   OMA; GMAAEIY; -.
DR   ProtClustDB; PRK06467; -.
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   475 AA;  50549 MW;  5C3FC8F00DE5BC0E CRC64;
     MSNEIKTQVV VLGAGPAGYS AAFRAADLGL ETVIVERFST LGGVCLNVGC IPSKALLHVA
     KVIEEAKAVA AHGVVFGEPT IDLDKLRSFK QKVISQLTGG LGGMSKMRKV NVVNGFGKFT
     GPNSLEVTAQ DGTVTVVKFD QAIIAAGSRP IKLPFIPHED PRIWDSTDAL ELKEVPGKLL
     VMGGGIIGLE MGTVYSSLGS EIDVVEMFDQ VIPAADKDVV RVFTKQIKKK FNLILETKVT
     AVEAREDGIY VSMEGKSAPA EPVRYDAVLV AIGRTPNGKL IDAEKAGVKI DERGFINVDK
     QLRTNVPHIY AIGDIVGQPM LAHKGVHEGH VAAEVIAGMK HYFDPKVIPS IAYTDPEVAW
     VGLTEKEAKE QGIAYETATF PWAASGRAIA SDCSEGMTKL IFDKDTHRVI GGAIVGVNGG
     ELLGEIGLAI EMGCDAEDLA LTIHAHPTLH ESVGLAAEIY EGSITDLPNP KAKKK
//