DLDH_CHLPN
ID DLDH_CHLPN Reviewed; 461 AA.
AC Q9Z773; Q9JQE6;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 157.
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=CPn_0833, CP_1037, CpB0862;
OS Chlamydia pneumoniae (Chlamydophila pneumoniae).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=83558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CWL029;
RX PubMed=10192388; DOI=10.1038/7716;
RA Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W.,
RA Olinger L., Grimwood J., Davis R.W., Stephens R.S.;
RT "Comparative genomes of Chlamydia pneumoniae and C. trachomatis.";
RL Nat. Genet. 21:385-389(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AR39;
RX PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA Salzberg S.L., Eisen J.A., Fraser C.M.;
RT "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT AR39.";
RL Nucleic Acids Res. 28:1397-1406(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J138;
RX PubMed=10871362; DOI=10.1093/nar/28.12.2311;
RA Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K.,
RA Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.;
RT "Comparison of whole genome sequences of Chlamydia pneumoniae J138 from
RT Japan and CWL029 from USA.";
RL Nucleic Acids Res. 28:2311-2314(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=J138;
RA Shirai M.;
RT "Genomic sequence comparison of two unrelated isolates of Chlamydia
RT pneumoniae from Japan and U.S.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TW-183;
RA Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P.,
RA Schneider S., Pohl T., Essig A., Marre R., Melchers K.;
RT "The genome sequence of Chlamydia pneumoniae TW183 and comparison with
RT other Chlamydia strains based on whole genome sequence analysis.";
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: The branched-chain alpha-keto dehydrogenase complex catalyzes
CC the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It
CC contains multiple copies of 3 enzymatic components: branched-chain
CC alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and
CC lipoamide dehydrogenase (E3) (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + NAD(+) = (R)-N(6)-
CC lipoyl-L-lysyl-[protein] + H(+) + NADH; Xref=Rhea:RHEA:15045,
CC Rhea:RHEA-COMP:10474, Rhea:RHEA-COMP:10475, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:83099,
CC ChEBI:CHEBI:83100; EC=1.8.1.4;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC Note=Binds 1 FAD per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; AE001363; AAD18970.1; -; Genomic_DNA.
DR EMBL; AE002161; AAF38812.1; -; Genomic_DNA.
DR EMBL; BA000008; BAA99041.1; -; Genomic_DNA.
DR EMBL; AB035943; BAA88651.1; -; Genomic_DNA.
DR EMBL; AE009440; AAP98791.1; -; Genomic_DNA.
DR PIR; C72031; C72031.
DR PIR; G86594; G86594.
DR RefSeq; NP_225028.1; NC_000922.1.
DR RefSeq; WP_010883470.1; NZ_LN847257.1.
DR AlphaFoldDB; Q9Z773; -.
DR SMR; Q9Z773; -.
DR STRING; 115711.CP_1037; -.
DR EnsemblBacteria; AAD18970; AAD18970; CPn_0833.
DR EnsemblBacteria; AAF38812; AAF38812; CP_1037.
DR KEGG; cpa:CP_1037; -.
DR KEGG; cpj:lpdA; -.
DR KEGG; cpn:CPn_0833; -.
DR KEGG; cpt:CpB0862; -.
DR PATRIC; fig|115713.3.peg.912; -.
DR eggNOG; COG1249; Bacteria.
DR HOGENOM; CLU_016755_0_3_0; -.
DR OrthoDB; 267896at2; -.
DR Proteomes; UP000000583; Chromosome.
DR Proteomes; UP000000801; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR InterPro; IPR006258; Lipoamide_DH.
DR InterPro; IPR001100; Pyr_nuc-diS_OxRdtase.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR PIRSF; PIRSF000350; Mercury_reductase_MerA; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR SUPFAM; SSF55424; SSF55424; 1.
DR TIGRFAMs; TIGR01350; lipoamide_DH; 1.
DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Disulfide bond; FAD; Flavoprotein; Glycolysis; NAD;
KW Oxidoreductase; Redox-active center.
FT CHAIN 1..461
FT /note="Dihydrolipoyl dehydrogenase"
FT /id="PRO_0000068025"
FT ACT_SITE 436
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 34..42
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 51
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 114
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 177..181
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 200
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 261..264
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 304
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 312
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT DISULFID 42..47
FT /note="Redox-active"
FT /evidence="ECO:0000250"
FT CONFLICT 64
FT /note="K -> T (in Ref. 5; AAP98791)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 461 AA; 49167 MW; CADD4483E758FFAD CRC64;
MTQEFDCVVI GAGPSGYVAA ITAAQSKLRT ALIEEDQAGG TCLNRGCIPS KALIAGANVV
SHIKHAEQFG IHVDGYTIDY PAMAKRKNTV VQGIRQGLEG LIRSNKITVL KGTGSLVSST
EVKVIGQDTT IIKANHIILA TGSEPRPFPG VPFSSRILSS TGILELEVLP KKLAIIGGGV
IGCEFASLFH TLGVEITVIE ALDHILAVNN KEVSQTVTNK FTKQGIRILT KASISAIEES
QNQVRITVND QVEEFDYVLV AIGRQFNTAS IGLDNAGVIR DDRGVIPVDE TMRTNVPNIY
AIGDITGKWL LAHVASHQGV IAAKNISGHH EVMDYSAIPS VIFTHPEIAM VGLSLQEAEQ
QNLPAKLTKF PFKAIGKAVA LGASDGFAAI VSHEITQQIL GAYVIGPHAS SLIGEMTLAI
RNELTLPCIY ETVHAHPTLS EVWAEGALLA TNHPLHFPPK S
