[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]	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:
P09060:bkdA1; NbExp=1; IntAct=EBI-1027848, EBI-1027855;

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; AAA65616.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M57613; AAA65615.1; ALT_INIT; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S01318; DEPSEB.

3D structure databases

PDB

1QS0; X-ray; 2.40 A; B=2-339.	[ExPASy / RCSB / EBI]
2BP7; X-ray; 2.90 A; B/D/F/H=1-339.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1QS0; -.
2BP7; -.

ModBase

P09061.

Protein-protein interaction databases

DIP

DIP:6209N; -.

IntAct

P09061; 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

IPR005476; Transketo_C.
IPR005475; Transketo_Cen_R.
IPR015941; Transketolase_C-like.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.920; Transketo_C_like; 1.

Pfam

PF02779; Transket_pyr; 1.
PF02780; Transketolase_C; 1.
Pfam graphical view of domain structure.

Other

ProtoNet

P09061.

UniRef

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

Keywords

3D-structure; Oxidoreductase; Thiamine pyrophosphate.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 339`	`339`	`2-oxoisovalerate dehydrogenase subunit beta.`	`PRO_0000162251`
`STRAND`	`3 5`	`3`
`HELIX`	`8 22`	`15`
`STRAND`	`26 30`	`5`
`STRAND`	`34 36`	`3`
`TURN`	`42 45`	`4`
`HELIX`	`46 50`	`5`
`TURN`	`52 54`	`3`
`STRAND`	`55 57`	`3`
`HELIX`	`62 75`	`14`
`STRAND`	`78 82`	`5`
`HELIX`	`86 88`	`3`
`HELIX`	`90 92`	`3`
`HELIX`	`93 97`	`5`
`TURN`	`98 102`	`5`
`HELIX`	`103 106`	`4`
`TURN`	`107 109`	`3`
`STRAND`	`116 121`	`6`
`STRAND`	`124 126`	`3`
`STRAND`	`129 132`	`4`
`HELIX`	`136 139`	`4`
`STRAND`	`146 148`	`3`
`HELIX`	`153 165`	`13`
`STRAND`	`166 168`	`3`
`STRAND`	`170 175`	`6`
`HELIX`	`176 178`	`3`
`STRAND`	`179 181`	`3`
`STRAND`	`187 189`	`3`
`STRAND`	`201 205`	`5`
`STRAND`	`216 218`	`3`
`STRAND`	`224 227`	`4`
`HELIX`	`231 242`	`12`
`STRAND`	`247 250`	`4`
`STRAND`	`252 256`	`5`
`HELIX`	`259 269`	`11`
`STRAND`	`272 278`	`7`
`HELIX`	`285 295`	`11`
`STRAND`	`296 299`	`4`
`STRAND`	`305 308`	`4`
`HELIX`	`319 322`	`4`
`HELIX`	`326 335`	`10`

Sequence information

Length: 339 AA [This is the length of the unprocessed precursor]

Molecular weight: 37134 Da [This is the MW of the unprocessed precursor]

CRC64: 318FE1E403B2AEA5 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MATTTMTMIQ ALRSAMDVML ERDDNVVVYG QDVGYFGGVF RCTEGLQTKY GKSRVFDAPI 

        70         80         90        100        110        120 
SESGIVGTAV GMGAYGLRPV VEIQFADYFY PASDQIVSEM ARLRYRSAGE FIAPLTLRMP 

       130        140        150        160        170        180 
CGGGIYGGQT HSQSPEAMFT QVCGLRTVMP SNPYDAKGLL IASIECDDPV IFLEPKRLYN 

       190        200        210        220        230        240 
GPFDGHHDRP VTPWSKHPHS AVPDGYYTVP LDKAAITRPG NDVSVLTYGT TVYVAQVAAE 

       250        260        270        280        290        300 
ESGVDAEVID LRSLWPLDLD TIVESVKKTG RCVVVHEATR TCGFGAELVS LVQEHCFHHL 

       310        320        330 
EAPIERVTGW DTPYPHAQEW AYFPGPSRVG AALKKVMEV

P09061 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