ID   DLDH_VIBPA              Reviewed;         475 AA.
AC   O50286;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2003, sequence version 2.
DT   16-JUN-2009, entry version 74.
DE   RecName: Full=Dihydrolipoyl dehydrogenase;
DE            EC=1.8.1.4;
DE   AltName: Full=Dihydrolipoamide dehydrogenase;
DE   AltName: Full=E3 component of 2-oxoglutarate dehydrogenase complex;
GN   Name=lpd; OrderedLocusNames=VP2517;
OS   Vibrio parahaemolyticus.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Vibrio.
OX   NCBI_TaxID=670;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=BB22;
RX   MEDLINE=98292750; PubMed=9620967;
RA   McCarter L.L.;
RT   "OpaR, a homolog of Vibrio harveyi LuxR, controls opacity of Vibrio
RT   parahaemolyticus.";
RL   J. Bacteriol. 180:3166-3173(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIMD 2210633 / Serotype O3:K6;
RX   MEDLINE=22508454; PubMed=12620739; DOI=10.1016/S0140-6736(03)12659-1;
RA   Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA   Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA   Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT   "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT   distinct from that of V. cholerae.";
RL   Lancet 361:743-749(2003).
CC   -!- FUNCTION: The branched-chain alpha-keto dehydrogenase complex
CC       catalyzes the overall conversion of alpha-keto acids to acyl-CoA
CC       and CO(2). It contains multiple copies of 3 enzymatic components:
CC       branched-chain alpha-keto acid decarboxylase (E1), lipoamide
CC       acyltransferase (E2) and lipoamide dehydrogenase (E3) (By
CC       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   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
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; AF035967; AAC46405.1; -; Genomic_DNA.
DR   EMBL; BA000031; BAC60780.1; -; Genomic_DNA.
DR   RefSeq; NP_798896.1; -.
DR   HSSP; Q51225; 1OJT.
DR   GeneID; 1190032; -.
DR   GenomeReviews; BA000031_GR; VP2517.
DR   KEGG; vpa:VP2517; -.
DR   NMPDR; fig|223926.1.peg.2517; -.
DR   HOGENOM; O50286; -.
DR   OMA; O50286; PFIPEDP.
DR   BioCyc; VPAR223926:VP2517-MON; -.
DR   BRENDA; 1.8.1.4; 3063.
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   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Disulfide bond; FAD; Flavoprotein;
KW   Glycolysis; NAD; Oxidoreductase; Redox-active center.
FT   CHAIN         1    475       Dihydrolipoyl dehydrogenase.
FT                                /FTId=PRO_0000068053.
FT   NP_BIND      36     45       FAD (By similarity).
FT   NP_BIND     182    186       NAD (By similarity).
FT   NP_BIND     270    273       NAD (By similarity).
FT   ACT_SITE    445    445       Proton acceptor (By similarity).
FT   BINDING      54     54       FAD (By similarity).
FT   BINDING     117    117       FAD; via amide nitrogen and carbonyl
FT                                oxygen (By similarity).
FT   BINDING     205    205       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     45     50       Redox-active (By similarity).
FT   CONFLICT    160    160       P -> S (in Ref. 1; AAC46405).
SQ   SEQUENCE   475 AA;  50988 MW;  67F6E3A8C28DFB44 CRC64;
     MSKEIKAQVV VLGSGPAGYS AAFRCADLGL ETVLVERYST LGGVCLNVGC IPSKALLHVS
     KVIEEAKAMA DHGVVFGEPQ TDINKIRIWK EKVVNQLTGG LSGMAKMRNV TVVNGYGKFT
     GPNSILVEGE GESTVVNFDN AIVAAGSRPI KLPFIPHEDP RIWDSTDALE LKEVPEKLLI
     MGGGIIGLEM GTVYHSLGSK VEVVEMFDQV IPAADKDIVK VYTKRIKDKF KLMLETKVTA
     VEAKEDGIYV SMEGKKAPAE AERYDAVLVA IGRVPNGKLI DGEKAGLEID ERGFINVDKQ
     MRTNVPHIFA IGDIVGQPML AHKGVHEGHV AAEVISGKKH YFDPKVIPSI AYTEPEVAWV
     GKTEKEAKAE GIKYEVATFP WAASGRAIAS DCSDGMTKLI FDKETHRVIG GAIVGTNGGE
     LLGEIGLAIE MGCDAEDIAL TIHAHPTLHE SVGLAAEVFE GSITDLPNKK AVKKK
//