ID   DLDH_STAAW              Reviewed;         468 AA.
AC   P0A0E7; Q59822;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   16-JUN-2009, entry version 35.
DE   RecName: Full=Dihydrolipoyl dehydrogenase;
DE            EC=1.8.1.4;
DE   AltName: Full=Dihydrolipoamide dehydrogenase;
DE   AltName: Full=E3 component of pyruvate complex;
DE   AltName: Full=Membrane-bound ribosome protein complex 50 kDa subunit;
GN   Name=pdhD; OrderedLocusNames=MW0979;
OS   Staphylococcus aureus (strain MW2).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=196620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=22040717; PubMed=12044378; DOI=10.1016/S0140-6736(02)08713-5;
RA   Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A.,
RA   Nagai Y., Iwama N., Asano K., Naimi T., Kuroda H., Cui L.,
RA   Yamamoto K., Hiramatsu K.;
RT   "Genome and virulence determinants of high virulence community-
RT   acquired MRSA.";
RL   Lancet 359:1819-1827(2002).
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). Membrane; Peripheral
CC       membrane protein.
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; BA000033; BAB94844.1; -; Genomic_DNA.
DR   RefSeq; NP_645796.1; -.
DR   HSSP; P11959; 1EBD.
DR   SMR; P0A0E7; 8-461.
DR   GeneID; 1003091; -.
DR   GenomeReviews; BA000033_GR; MW0979.
DR   KEGG; sam:MW0979; -.
DR   HOGENOM; P0A0E7; -.
DR   OMA; P0A0E7; PFIPEDP.
DR   BioCyc; SAUR196620:MW0979-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; 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   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Disulfide bond; FAD; Flavoprotein;
KW   Glycolysis; Membrane; NAD; Oxidoreductase; Redox-active center.
FT   CHAIN         1    468       Dihydrolipoyl dehydrogenase.
FT                                /FTId=PRO_0000068049.
FT   NP_BIND      39     47       FAD (By similarity).
FT   NP_BIND     183    187       NAD (By similarity).
FT   NP_BIND     271    274       NAD (By similarity).
FT   ACT_SITE    446    446       Proton acceptor (By similarity).
FT   BINDING      56     56       FAD (By similarity).
FT   BINDING     119    119       FAD; via amide nitrogen and carbonyl
FT                                oxygen (By similarity).
FT   BINDING     206    206       NAD (By similarity).
FT   BINDING     314    314       FAD (By similarity).
FT   BINDING     322    322       FAD; via amide nitrogen (By similarity).
FT   DISULFID     47     52       Redox-active (By similarity).
SQ   SEQUENCE   468 AA;  49451 MW;  7B061FE2C39ED2D9 CRC64;
     MVVGDFPIET DTIVIGAGPG GYVAAIRAAQ LGQKVTIVEK GNLGGVCLNV GCIPSKALLH
     ASHRFVEAQH SENLGVIAES VSLNFQKVQE FKSSVVNKLT GGVEGLLKGN KVNIVKGEAY
     FVDNNSLRVM DEKSAQTYNF KNAIIATGSR PIEIPNFKFG KRVIDSTGAL NLQEVPGKLV
     VVGGGYIGSE LGTAFANFGS EVTILEGAKD ILGGFEKQMT QPVKKGMKEK GVEIVTEAMA
     KSAEETDNGV KVTYEAKGEE KTIEADYVLV TVGRRPNTDE LGLEELGVKF ADRGLLEVDK
     QSRTSISNIY AIGDIVPGLP LAHKASYEAK VAAEAIDGQA AEVDYIGMPA VCFTEPELAT
     VGYSEAQAKE EGLAIKASKF PYAANGRALS LDDTNGFVKL ITLKEDDTLI GAQVVGTGAS
     DIISELGLAI EAGMNAEDIA LTIHAHPTLG EMTMEAAEKA IGYPIHTM
//