ID   DLDH_CHLTR              Reviewed;         465 AA.
AC   O84561;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   16-JUN-2009, entry version 71.
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=lpdA; OrderedLocusNames=CT_557;
OS   Chlamydia trachomatis.
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae; Chlamydia.
OX   NCBI_TaxID=813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D/UW-3/Cx;
RX   MEDLINE=99000809; PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA   Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA   Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V.,
RA   Davis R.W.;
RT   "Genome sequence of an obligate intracellular pathogen of humans:
RT   Chlamydia trachomatis.";
RL   Science 282:754-759(1998).
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; AE001273; AAC68159.1; -; Genomic_DNA.
DR   PIR; E71500; E71500.
DR   RefSeq; NP_220072.1; -.
DR   HSSP; P11959; 1EBD.
DR   PHCI-2DPAGE; O84561; -.
DR   GeneID; 884341; -.
DR   GenomeReviews; AE001273_GR; CT_557.
DR   KEGG; ctr:CT557; -.
DR   HOGENOM; O84561; -.
DR   OMA; O84561; IEVDACL.
DR   BioCyc; CTRA315277:CT557-MON; -.
DR   BRENDA; 1.8.1.4; 108.
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    465       Dihydrolipoyl dehydrogenase.
FT                                /FTId=PRO_0000068026.
FT   NP_BIND      34     42       FAD (By similarity).
FT   NP_BIND     180    184       NAD (By similarity).
FT   NP_BIND     264    267       NAD (By similarity).
FT   ACT_SITE    439    439       Proton acceptor (By similarity).
FT   BINDING      51     51       FAD (By similarity).
FT   BINDING     114    114       FAD; via amide nitrogen and carbonyl
FT                                oxygen (By similarity).
FT   BINDING     203    203       NAD (By similarity).
FT   BINDING     237    237       NAD; via amide nitrogen (By similarity).
FT   BINDING     307    307       FAD (By similarity).
FT   BINDING     315    315       FAD; via amide nitrogen (By similarity).
FT   DISULFID     42     47       Redox-active (By similarity).
SQ   SEQUENCE   465 AA;  49491 MW;  56449CCD2AB61477 CRC64;
     MNEAFDCVVI GAGPGGYVAA ITAAQAGLKT ALIEKREAGG TCLNRGCIPS KALLAGAEVV
     TQIRHADQFG IHVEGFSINY PAMVQRKDSV VRSIRDGLNG LIRSNKITVF SGRGSLISST
     EVKILGENPS VIKAHSIILA TGSEPRAFPG IPFSAESPRI LCSTGVLNLK EIPQKMAIIG
     GGVIGCEFAS LFHTLGSEVS VIEASSQILA LNNPDISKTM FDKFTRQGLR FVLEASVSNI
     EDIGDRVRLT INGNVEEYDY VLVSIGRRLN TENIGLDKAG VICDERGVIP TDATMRTNVP
     NIYAIGDITG KWQLAHVASH QGIIAARNIA GHKEEIDYSA VPSVIFTFPE VASVGLSPTA
     AQQQKIPVKV TKFPFRAIGK AVAMGEADGF AAIISHETTQ QILGAYVIGP HASSLISEIT
     LAVRNELTLP CIYETIHAHP TLAEVWAESA LLAVDTPLHM PPAKK
//