[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=G2; PubMed=3416875 [NCBI, ExPASy, EBI, Israel, Japan] Burns G., Brown T., Hatter K., Idriss J., Sokatch J.R.; "Similarity of the E1 subunits of branched-chain-oxoacid dehydrogenase from Pseudomonas putida to the corresponding subunits of mammalian branched-chain-oxoacid and pyruvate dehydrogenases."; Eur. J. Biochem. 176:311-317(1988).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-17. STRAIN=G2; PubMed=2211503 [NCBI, ExPASy, EBI, Israel, Japan] Madhusudhan K.T., Huang G., Burns G., Sokatch J.R.; "Transcriptional analysis of the promoter region of the Pseudomonas putida branched-chain keto acid dehydrogenase operon."; J. Bacteriol. 172:5655-5663(1990).
[3]	PROTEIN SEQUENCE OF 1-13. PubMed=8521848 [NCBI, ExPASy, EBI, Israel, Japan] Hester K., Luo J., Burns G., Braswell E.H., Sokatch J.R.; "Purification of active E1 alpha 2 beta 2 of Pseudomonas putida branched-chain-oxoacid dehydrogenase."; Eur. J. Biochem. 233:828-836(1995).
[4]	X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS). DOI=10.1038/11563; PubMed=10426958 [NCBI, ExPASy, EBI, Israel, Japan] Aevarsson A., Seger K., Turley S., Sokatch J.R., Hol W.G.J.; "Crystal structure of 2-oxoisovalerate and dehydrogenase and the architecture of 2-oxo acid dehydrogenase multienzyme complexes."; Nat. Struct. Biol. 6:785-792(1999).

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 three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3).
CATALYTIC ACTIVITY: 3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine = [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + CO₂.
COFACTOR: Thiamine pyrophosphate.
SUBUNIT: Heterodimer of an alpha and a beta chain.
INTERACTION:
P09061:bkdA2; NbExp=1; IntAct=EBI-1027855, EBI-1027848;
SIMILARITY: Belongs to the BCKDHA 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

M57613; AAA65614.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S01317; DEPSXA.

3D structure databases

PDB

1QS0; X-ray; 2.40 A; A=2-408.	[ExPASy / RCSB / EBI]
2BP7; X-ray; 2.90 A; A/C/E/G=1-410.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1QS0; -.
2BP7; -.

ModBase

P09060.

Protein-protein interaction databases

DIP

DIP:6208N; -.

IntAct

P09060; 1.

Ontologies

GO:0003863;	Molecular function: 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity (inferred from electronic annotation from EC).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001017; DHase_E1.
Graphical view of domain structure.

Pfam

PF00676; E1_dh; 1.
Pfam graphical view of domain structure.

Other

ProtoNet

P09060.

UniRef

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

Keywords

3D-structure; Direct protein sequencing; Oxidoreductase; Thiamine pyrophosphate.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 410`	`410`	`2-oxoisovalerate dehydrogenase subunit alpha.`	`PRO_0000162249`
`HELIX`	`24 26`	`3`
`HELIX`	`44 47`	`4`
`HELIX`	`48 51`	`4`
`HELIX`	`67 69`	`3`
`HELIX`	`74 99`	`26`
`STRAND`	`102 104`	`3`
`TURN`	`110 112`	`3`
`HELIX`	`113 122`	`10`
`STRAND`	`127 130`	`4`
`HELIX`	`136 141`	`6`
`HELIX`	`146 154`	`9`
`TURN`	`160 163`	`4`
`HELIX`	`173 175`	`3`
`STRAND`	`182 185`	`4`
`HELIX`	`186 200`	`15`
`STRAND`	`207 212`	`6`
`HELIX`	`214 217`	`4`
`HELIX`	`219 231`	`13`
`STRAND`	`235 241`	`7`
`STRAND`	`243 245`	`3`
`HELIX`	`250 253`	`4`
`TURN`	`254 257`	`4`
`HELIX`	`262 266`	`5`
`STRAND`	`270 275`	`6`
`HELIX`	`279 294`	`16`
`STRAND`	`300 305`	`6`
`HELIX`	`318 320`	`3`
`HELIX`	`326 329`	`4`
`HELIX`	`335 345`	`11`
`HELIX`	`351 373`	`23`
`STRAND`	`378 380`	`3`
`HELIX`	`388 390`	`3`
`STRAND`	`391 396`	`6`
`HELIX`	`399 406`	`8`

Sequence information

Length: 410 AA [This is the length of the unprocessed precursor]

Molecular weight: 45268 Da [This is the MW of the unprocessed precursor]

CRC64: 0C998460CCFB9CF4 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNEYAPLRLH VPEPTGRPGC QTDFSYLRLN DAGQARKPPV DVDAADTADL SYSLVRVLDE 

        70         80         90        100        110        120 
QGDAQGPWAE DIDPQILRQG MRAMLKTRIF DSRMVVAQRQ KKMSFYMQSL GEEAIGSGQA 

       130        140        150        160        170        180 
LALNRTDMCF PTYRQQSILM ARDVSLVEMI CQLLSNERDP LKGRQLPIMY SVREAGFFTI 

       190        200        210        220        230        240 
SGNLATQFVQ AVGWAMASAI KGDTKIASAW IGDGATAESD FHTALTFAHV YRAPVILNVV 

       250        260        270        280        290        300 
NNQWAISTFQ AIAGGESTTF AGRGVGCGIA SLRVDGNDFV AVYAASRWAA ERARRGLGPS 

       310        320        330        340        350        360 
LIEWVTYRAG PHSTSDDPSK YRPADDWSHF PLGDPIARLK QHLIKIGHWS EEEHQATTAE 

       370        380        390        400        410 
FEAAVIAAQK EAEQYGTLAN GHIPSAASMF EDVYKEMPDH LRRQRQELGV

P09060 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