Reviewed, UniProtKB/Swiss-Prot P09061 (ODBB_PSEPU)

Names and origin

Protein names

Recommended name:
    2-oxoisovalerate dehydrogenase subunit beta
    EC=1.2.4.4
Alternative name(s):
    Branched-chain alpha-keto acid dehydrogenase E1 component beta chain
      Short name=BCKDH E1-beta

Gene names

Name:

bkdA2

Organism

Pseudomonas putida

Taxonomic identifier

303 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

Protein attributes

Sequence length	339 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO2. 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 structure	Heterodimer of an alpha and a beta chain.

Ontologies

Keywords
Ligand	Thiamine pyrophosphate
Molecular function	Oxidoreductase
Technical term	3D-structure
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity Inferred from electronic annotation. Source: EC protein binding Ref.2 Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
bkdA1	P09060	1	EBI-1027848,EBI-1027855

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 339

339

2-oxoisovalerate dehydrogenase subunit beta

PRO_0000162251

Secondary structure

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339

Helix Strand Turn

Details...

Beta strand

3 – 5

3

Helix

8 – 22

15

Beta strand

26 – 30

5

Beta strand

34 – 36

3

Turn

42 – 45

4

Helix

46 – 50

5

Turn

52 – 54

3

Beta strand

55 – 57

3

Helix

62 – 75

14

Beta 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

Beta strand

116 – 121

6

Beta strand

124 – 126

3

Beta strand

129 – 132

4

Helix

136 – 139

4

Beta strand

146 – 148

3

Helix

153 – 165

13

Beta strand

166 – 168

3

Beta strand

170 – 175

6

Helix

176 – 178

3

Beta strand

179 – 181

3

Beta strand

187 – 189

3

Beta strand

201 – 205

5

Beta strand

216 – 218

3

Beta strand

224 – 227

4

Helix

231 – 242

12

Beta strand

247 – 250

4

Beta strand

252 – 256

5

Helix

259 – 269

11

Beta strand

272 – 278

7

Helix

285 – 295

11

Beta strand

296 – 299

4

Beta strand

305 – 308

4

Helix

319 – 322

4

Helix

326 – 335

10

Sequences

	Sequence		Length	Mass (Da)
	P09061-1 [UniParc]. Last modified November 1, 1988. Version 1. Checksum: 318FE1E403B2AEA5	FASTA	339	37,134
	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

References

[1]	"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." Burns G., Brown T., Hatter K., Idriss J., Sokatch J.R. Eur. J. Biochem. 176:311-317(1988) [PubMed: 3416875] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: G2.
[2]	"Crystal structure of 2-oxoisovalerate and dehydrogenase and the architecture of 2-oxo acid dehydrogenase multienzyme complexes." Aevarsson A., Seger K., Turley S., Sokatch J.R., Hol W.G.J. Nat. Struct. Biol. 6:785-792(1999) [PubMed: 10426958] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M57613 Genomic DNA. Translation: AAA65616.1.
M57613 Genomic DNA. Translation: AAA65615.1. Different initiation.

PIR

DEPSEB. S01318.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1QS0	X-ray	2.40	B	2-339	[»]
2BP7	X-ray	2.90	B/D/F/H	1-339	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:6209N.

IntAct

P09061. 1 interaction.

Enzyme and pathway databases

BRENDA

1.2.4.4. 403.

Family and domain databases

InterPro

IPR005476. Transketo_C.
IPR015941. Transketolase_C-like.
IPR005475. Transketolase_central-reg.
[Graphical view]

Gene3D

G3DSA:3.40.50.920. Transketo_C_like. 1 hit.

Pfam

PF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

ODBB_PSEPU

Accession

Primary (citable) accession number: P09061

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1988
Last sequence update:	November 1, 1988
Last modified:	May 5, 2009
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)