[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=G2; PubMed=1902462 [NCBI, ExPASy, EBI, Israel, Japan] Palmer J.A., Hatter K., Sokatch J.R.; "Cloning and sequence analysis of the LPD-glc structural gene of Pseudomonas putida."; J. Bacteriol. 173:3109-3116(1991).
[2]	SEQUENCE REVISION. Sokatch J.R.; Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases.
[3]	PROTEIN SEQUENCE OF 2-26. PubMed=2914869 [NCBI, ExPASy, EBI, Israel, Japan] Burns G., Sykes P.J., Hatter K., Sokatch J.R.; "Isolation of a third lipoamide dehydrogenase from Pseudomonas putida."; J. Bacteriol. 171:665-668(1989).

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).
FUNCTION: Also acts in the glycine cleavage system.
CATALYTIC ACTIVITY: Protein N⁶-(dihydrolipoyl)lysine + NAD⁺ = protein N⁶-(lipoyl)lysine + NADH.
COFACTOR: Binds 1 FAD per subunit (By similarity).
SUBUNIT: Homodimer.
SUBCELLULAR LOCATION: Cytoplasm.
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

M80189; AAA96437.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A39406; A39406.

3D structure databases

HSSP

P14218; 1LPF. [HSSP ENTRY / PDB]

SMR

P31052; 2-473.

ModBase

P31052.

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

P31052.

Other

UniRef

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

Keywords

Cytoplasm; Direct protein sequencing; FAD; Flavoprotein; Glycolysis; NAD; Oxidoreductase; Redox-active center.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 478`	`477`	`Dihydrolipoamide dehydrogenase.`	`PRO_0000068039`
`NP_BIND`	`34 49`	`16`	`FAD (By similarity).`
`NP_BIND`	`188 192`	`5`	`NAD (By similarity).`
`NP_BIND`	`276 279`	`4`	`NAD (By similarity).`
`ACT_SITE`	`451 451`		`Proton acceptor (By similarity).`
`BINDING`	`58 58`		`FAD (By similarity).`
`BINDING`	`122 122`		`FAD; via amide nitrogen and carbonyl oxygen (By similarity).`
`BINDING`	`211 211`		`NAD (By similarity).`
`BINDING`	`245 245`		`NAD; via amide nitrogen (By similarity).`
`BINDING`	`319 319`		`FAD (By similarity).`
`BINDING`	`327 327`		`FAD; via amide nitrogen (By similarity).`
`DISULFID`	`49 54`		`Redox-active (By similarity).`

Sequence information

Length: 478 AA [This is the length of the unprocessed precursor]

Molecular weight: 49896 Da [This is the MW of the unprocessed precursor]

CRC64: 2B7979445DC60812 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTQKFDVVVI GAGPGGYVAA IKAAQLGLKT ACIEKYTDAE GKLALGGTCL NVGCIPSKAL 

        70         80         90        100        110        120 
LDSSWKYKEA KESFNVHGIS TGEVKMDVAA MVGRKAGIVK NLTGGVATLF KANGVTSIQG 

       130        140        150        160        170        180 
HGKLLAGKKV EVTKADGTTE VIEAENVILA SGSRPIDIPP APVDQNVIVD STGALEFQAV 

       190        200        210        220        230        240 
PKRLGVIGAG VIGLELGSVW ARLGAEVTVL EALDTFLMAA DTAVSKEAQK TLTKQGLDIK 

       250        260        270        280        290        300 
LGARVTGSKV NGNEVEVTYT NAEGEQKITF DKLIVAVGRR PVTTDLLAAD SGVTIDERGY 

       310        320        330        340        350        360 
IFVDDYCATS VPGVYAIGDV VRGMMLAHKA SEEGIMVVER IKGHKAQMNY DLIPSVIYTH 

       370        380        390        400        410        420 
PEIAWVGKTE QALKAEGVEV NVGTFPFAAS GRAMAANDTG GFVKVIADAK TDRVLGVHVI 

       430        440        450        460        470 
GPSAAELVQQ GAIAMEFGTS AEDLGMMVFS HPTLSEALHE AALAVNGGAI HVANRKKR

P31052 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