ID   DLDH_RHIET              Reviewed;         277 AA.
AC   O05940;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   16-JUN-2009, entry version 64.
DE   RecName: Full=Probable 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;
DE   AltName: Full=ORF-E3;
DE   Flags: Fragment;
OS   Rhizobium etli.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=29449;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CE3;
RX   MEDLINE=97286510; PubMed=9141657; DOI=10.1016/S0378-1097(97)00069-4;
RA   Tate R., Riccio A., Iaccarino M., Patriarca E.J.;
RT   "Cloning and transcriptional analysis of the lipA (lipoic acid
RT   synthetase) gene from Rhizobium etli.";
RL   FEMS Microbiol. Lett. 149:165-172(1997).
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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; Y11708; CAA72399.1; -; Genomic_DNA.
DR   HSSP; P31023; 1DXL.
DR   BRENDA; 1.8.1.4; 1020.
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; 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   ProDom; PD000139; FAD_pyr_redox; 1.
DR   PROSITE; PS00076; PYRIDINE_REDOX_1; PARTIAL.
PE   3: Inferred from homology;
KW   Cytoplasm; FAD; Flavoprotein; Glycolysis; NAD; Oxidoreductase;
KW   Redox-active center.
FT   CHAIN        <1    277       Probable dihydrolipoyl dehydrogenase.
FT                                /FTId=PRO_0000068041.
FT   NP_BIND      83     86       NAD (By similarity).
FT   ACT_SITE    259    259       Proton acceptor (By similarity).
FT   BINDING      17     17       NAD (By similarity).
FT   BINDING      51     51       NAD; via amide nitrogen (By similarity).
FT   BINDING     125    125       FAD (By similarity).
FT   BINDING     133    133       FAD; via amide nitrogen (By similarity).
FT   NON_TER       1      1
SQ   SEQUENCE   277 AA;  29547 MW;  CD3E3B5DB1FE4C4F CRC64;
     EFASFYRSMG VDVTVVEVMP TIMPVEDAEI TAIARKQLEK RGLKIFTSAK VTKVEKGAGS
     ITAHVETSDG KVQQITADRM ISAVGVQGNI ENLGLEALGV LTDRRWLVAD GYGKTNVAGI
     YAIGDVAGPP IVAHKAEHEG VVCVEKIAGV PNVHPTDKGK VPGCTYCNPQ VASVGLTEAK
     AKELGSDIRV GRFSFAANRK AIALGEDQGM VKVIFDKKTG ELLGAHMVGA EVTELIQGFV
     VAMNLETTEE ELMHTIFPHP TVSETMKEAV LDAYGRV
//