Reviewed, UniProtKB/Swiss-Prot P09060 (ODBA_PSEPU)

Names and origin

Protein names

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

Gene names

Name:

bkdA1

Organism

Pseudomonas putida

Taxonomic identifier

303 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

Protein attributes

Sequence length	410 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.
Sequence similarities	Belongs to the BCKDHA family.

Ontologies

Keywords
Ligand	Thiamine pyrophosphate
Molecular function	Oxidoreductase
Technical term	3D-structure Direct protein sequencing
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.4 Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
bkdA2	P09061	1	EBI-1027855,EBI-1027848

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 410

410

2-oxoisovalerate dehydrogenase subunit alpha

PRO_0000162249

Secondary structure

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410

Helix Strand Turn

Details...

Helix

24 – 26

3

Helix

44 – 47

4

Helix

48 – 51

4

Helix

67 – 69

3

Helix

74 – 99

26

Beta strand

102 – 104

3

Turn

110 – 112

3

Helix

113 – 122

10

Beta strand

127 – 130

4

Helix

136 – 141

6

Helix

146 – 154

9

Turn

160 – 163

4

Helix

173 – 175

3

Beta strand

182 – 185

4

Helix

186 – 200

15

Beta strand

207 – 212

6

Helix

214 – 217

4

Helix

219 – 231

13

Beta strand

235 – 241

7

Beta strand

243 – 245

3

Helix

250 – 253

4

Turn

254 – 257

4

Helix

262 – 266

5

Beta strand

270 – 275

6

Helix

279 – 294

16

Beta strand

300 – 305

6

Helix

318 – 320

3

Helix

326 – 329

4

Helix

335 – 345

11

Helix

351 – 373

23

Beta strand

378 – 380

3

Helix

388 – 390

3

Beta strand

391 – 396

6

Helix

399 – 406

8

Sequences

	Sequence		Length	Mass (Da)
	P09060-1 [UniParc]. Last modified February 1, 1996. Version 2. Checksum: 0C998460CCFB9CF4	FASTA	410	45,268
	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

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]	"Transcriptional analysis of the promoter region of the Pseudomonas putida branched-chain keto acid dehydrogenase operon." Madhusudhan K.T., Huang G., Burns G., Sokatch J.R. J. Bacteriol. 172:5655-5663(1990) [PubMed: 2211503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-17. Strain: G2.
[3]	"Purification of active E1 alpha 2 beta 2 of Pseudomonas putida branched-chain-oxoacid dehydrogenase." Hester K., Luo J., Burns G., Braswell E.H., Sokatch J.R. Eur. J. Biochem. 233:828-836(1995) [PubMed: 8521848] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-13.
[4]	"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: AAA65614.1.

PIR

DEPSXA. S01317.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1QS0	X-ray	2.40	A	2-408	[»]
2BP7	X-ray	2.90	A/C/E/G	1-410	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:6208N.

IntAct

P09060. 1 interaction.

Enzyme and pathway databases

BRENDA

1.2.4.4. 403.

Family and domain databases

InterPro

IPR001017. DH_E1.
[Graphical view]

Pfam

PF00676. E1_dh. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

ODBA_PSEPU

Accession

Primary (citable) accession number: P09060

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1988
Last sequence update:	February 1, 1996
Last modified:	June 16, 2009
This is version 68 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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