ID   DLDH3_PSEPU             Reviewed;         466 AA.
AC   P31046;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   16-JUN-2009, entry version 75.
DE   RecName: Full=Dihydrolipoyl dehydrogenase 3;
DE            EC=1.8.1.4;
DE   AltName: Full=Dihydrolipoamide dehydrogenase 3;
DE            Short=LPD-3;
GN   Name=lpd3;
OS   Pseudomonas putida.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=303;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=G2;
RX   MEDLINE=92104139; PubMed=1722146;
RX   DOI=10.1111/j.1432-1033.1991.tb16367.x;
RA   Palmer J.A., Madhusudhan K.T., Hatter K., Sokatch J.R.;
RT   "Cloning, sequence and transcriptional analysis of the structural gene
RT   for LPD-3, the third lipoamide dehydrogenase of Pseudomonas putida.";
RL   Eur. J. Biochem. 202:231-240(1991).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-10.
RX   MEDLINE=89123137; PubMed=2914869;
RA   Burns G., Sykes P.J., Hatter K., Sokatch J.R.;
RT   "Isolation of a third lipoamide dehydrogenase from Pseudomonas
RT   putida.";
RL   J. Bacteriol. 171:665-668(1989).
CC   -!- FUNCTION: LPD-3 may substitute for lipoamide dehydrogenase of the
CC       2-oxoglutarate dehydrogenase and pyruvate multienzyme complexes
CC       when the latter is inactive or missing.
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.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
CC   -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC       oxidoreductase family.
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DR   EMBL; X55704; CAA39235.1; -; Genomic_DNA.
DR   PIR; S19685; S19685.
DR   HSSP; P31023; 1DXL.
DR   BRENDA; 1.8.1.4; 403.
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; IPR000815; Hg_reductase.
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   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00945; HGRDTASE.
DR   ProDom; PD000139; FAD_pyr_redox; 1.
DR   TIGRFAMs; TIGR01350; lipoamide_DH; 1.
DR   PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Disulfide bond; FAD;
KW   Flavoprotein; Glycolysis; NAD; Oxidoreductase; Redox-active center.
FT   CHAIN         1    466       Dihydrolipoyl dehydrogenase 3.
FT                                /FTId=PRO_0000068040.
FT   NP_BIND      33     42       FAD (By similarity).
FT   NP_BIND     181    185       NAD (By similarity).
FT   NP_BIND     271    274       NAD (By similarity).
FT   ACT_SITE    445    445       Proton acceptor (By similarity).
FT   BINDING      51     51       FAD (By similarity).
FT   BINDING     115    115       FAD; via amide nitrogen and carbonyl
FT                                oxygen (By similarity).
FT   BINDING     204    204       NAD (By similarity).
FT   BINDING     238    238       NAD; via amide nitrogen (By similarity).
FT   BINDING     313    313       FAD (By similarity).
FT   BINDING     321    321       FAD; via amide nitrogen (By similarity).
FT   DISULFID     42     47       Redox-active (By similarity).
SQ   SEQUENCE   466 AA;  49257 MW;  E805AC5E879881F3 CRC64;
     MKSYDVVIIG GGPGGYNAAI RAGQLGLTVA CVEGRSTLGG TCLNVGCMPS KALLHASELY
     EAASGDEFAH LGIEVKPTLN LAQMMKQKDE SVTGLTKGIE YLFRKNKVDW IKGWGRLDGV
     GKVVVKAEDG SETALQAKDI VIATGSEPTP LPGVTIDNQR IIDSTGALSL PQVPKHLVVI
     GAGVIGLELG SVWRRLGSQV TVIEYLDRIC PGTDTETAKT LQKALAKQGM VFKLGSKVTQ
     ATASADGVSL VLEPAAGGTA ESLQADYVLV AIGRRPYTKG LNLESVGLET DKRGMLAQRT
     PPTSVPGVWV IGDVTSGPML AHKAEDEAVA CIERIAGKPH EVNYNLIPGV IYTRPELATV
     GKTEEQLKAE GRAYKVGKFP FTANSRAKIN HETEGFAKVI ADAETDEVLG VHLVGPSVSE
     MIGEFCVAME FSASAEDIAL TCHPHPTRSE ALRQAAMNVD GMAMQI
//