[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=CWL029; DOI=10.1038/7716; PubMed=10192388 [NCBI, ExPASy, EBI, Israel, Japan] Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W., Olinger L., Grimwood J., Davis R.W., Stephens R.S.; "Comparative genomes of Chlamydia pneumoniae and C. trachomatis."; Nat. Genet. 21:385-389(1999).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=AR39; DOI=10.1093/nar/28.6.1397; PubMed=10684935 [NCBI, ExPASy, EBI, Israel, Japan] Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O., Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S., Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J., Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G., Salzberg S.L., Eisen J.A., Fraser C.M.; "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae AR39."; Nucleic Acids Res. 28:1397-1406(2000).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=J138; DOI=10.1093/nar/28.12.2311; PubMed=10871362 [NCBI, ExPASy, EBI, Israel, Japan] Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K., Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.; "Comparison of whole genome sequences of Chlamydia pneumoniae J138 from Japan and CWL029 from USA."; Nucleic Acids Res. 28:2311-2314(2000).
[4]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=J138; Shirai M.; "Genomic sequence comparison of two unrelated isolates of Chlamydia pneumoniae from Japan and U.S."; Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
[5]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=TW-183; Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P., Schneider S., Pohl T., Essig A., Marre R., Melchers K.; "The genome sequence of Chlamydia pneumoniae TW183 and comparison with other Chlamydia strains based on whole genome sequence analysis."; Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.

Comments

FUNCTION: The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of 3 enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity).
CATALYTIC ACTIVITY: Protein N⁶-(dihydrolipoyl)lysine + NAD⁺ = protein N⁶-(lipoyl)lysine + NADH.
COFACTOR: Binds 1 FAD per subunit (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
MISCELLANEOUS: The active site is a redox-active disulfide bond.
SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AE001363; AAD18970.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE002161; AAF38812.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BA000008; BAA99041.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB035943; BAA88651.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE017160; AAP98791.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

C72031; C72031.
G86594; G86594.

RefSeq

NP_225028.1; -.
NP_300890.1; -.
NP_445574.1; -.
NP_877134.1; -.

3D structure databases

HSSP

P14218; 1LPF. [HSSP ENTRY / PDB]

ModBase

Q9Z773.

Enzyme and pathway databases

BioCyc

CPNE115711:CP_1037-MON; -.
CPNE115713:CPN0833-MON; -.
CPNE138677:CPJ0833-MON; -.
CPNE182082:CPB0862-MON; -.

2D gel databases

PHCI-2DPAGE

Q9Z773; -.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from InterPro).
GO:0004148;	Molecular function: dihydrolipoyl dehydrogenase activity (inferred from electronic annotation from InterPro).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0050660;	Molecular function: FAD binding (inferred from electronic annotation from InterPro).
GO:0045454;	Biological process: cell redox homeostasis (inferred from electronic annotation from InterPro).
GO:0006096;	Biological process: glycolysis (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR013027; FAD_pyr_nucl-diS_OxRdtase.
IPR000815; Hg_reductase.
IPR006258; Lipoamide_DHase.
IPR001100; Pyr_nuc-diS_OxRdtase.
IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
IPR012999; Pyr_OxRdtase_I_AS.
IPR001327; Pyr_OxRdtase_NAD_bd.
Graphical view of domain structure.

Gene3D

G3DSA:3.30.390.30; Pyr_redox_dim; 1.

PANTHER

PTHR22912:SF20; Lipoamide_DH; 1.

Pfam

PF00070; Pyr_redox; 1.
PF07992; Pyr_redox_2; 1.
PF02852; Pyr_redox_dim; 1.
Pfam graphical view of domain structure.

PRINTS

PR00368; FADPNR.
PR00945; HGRDTASE.
PR00411; PNDRDTASEI.

ProDom

PD000139; FAD_pyr_redox; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGRFAMs

TIGR01350; lipoamide_DH; 1.

PROSITE

PS00076; PYRIDINE_REDOX_1; 1.

ProtoNet

Q9Z773.

Genome annotation databases

GeneID

1467541; -.
895532; -.
919599; -.
963515; -.

GenomeReviews

AE002161_GR; CP_1037.
AE009440_GR; CpB0862.
AE001363_GR; CPn_0833.
BA000008_GR; lpdA.

KEGG

cpa:CP1037; -.
cpn:CPn0833; -.
cpt:CpB0862; -.

TIGR

CP_1037; -.

Phylogenomic databases

HOGENOM

Q9Z773; -.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Cytoplasm; FAD; Flavoprotein; Glycolysis; NAD; Oxidoreductase; Redox-active center.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 461`	`461`	`Dihydrolipoyl dehydrogenase.`	`PRO_0000068025`
`NP_BIND`	`34 42`	`9`	`FAD (By similarity).`
`NP_BIND`	`177 181`	`5`	`NAD (By similarity).`
`NP_BIND`	`261 264`	`4`	`NAD (By similarity).`
`ACT_SITE`	`436 436`		`Proton acceptor (By similarity).`
`BINDING`	`51 51`		`FAD (By similarity).`
`BINDING`	`114 114`		`FAD; via amide nitrogen and carbonyl oxygen (By similarity).`
`BINDING`	`200 200`		`NAD (By similarity).`
`BINDING`	`304 304`		`FAD (By similarity).`
`BINDING`	`312 312`		`FAD; via amide nitrogen (By similarity).`
`DISULFID`	`42 47`		`Redox-active (By similarity).`
`CONFLICT`	`64 64`		`K -> T (in Ref. 5; AAP98791).`

Sequence information

Length: 461 AA [This is the length of the unprocessed precursor]

Molecular weight: 49167 Da [This is the MW of the unprocessed precursor]

CRC64: CADD4483E758FFAD [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTQEFDCVVI GAGPSGYVAA ITAAQSKLRT ALIEEDQAGG TCLNRGCIPS KALIAGANVV 

        70         80         90        100        110        120 
SHIKHAEQFG IHVDGYTIDY PAMAKRKNTV VQGIRQGLEG LIRSNKITVL KGTGSLVSST 

       130        140        150        160        170        180 
EVKVIGQDTT IIKANHIILA TGSEPRPFPG VPFSSRILSS TGILELEVLP KKLAIIGGGV 

       190        200        210        220        230        240 
IGCEFASLFH TLGVEITVIE ALDHILAVNN KEVSQTVTNK FTKQGIRILT KASISAIEES 

       250        260        270        280        290        300 
QNQVRITVND QVEEFDYVLV AIGRQFNTAS IGLDNAGVIR DDRGVIPVDE TMRTNVPNIY 

       310        320        330        340        350        360 
AIGDITGKWL LAHVASHQGV IAAKNISGHH EVMDYSAIPS VIFTHPEIAM VGLSLQEAEQ 

       370        380        390        400        410        420 
QNLPAKLTKF PFKAIGKAVA LGASDGFAAI VSHEITQQIL GAYVIGPHAS SLIGEMTLAI 

       430        440        450        460 
RNELTLPCIY ETVHAHPTLS EVWAEGALLA TNHPLHFPPK S

Q9Z773 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools