Reviewed, UniProtKB/Swiss-Prot Q5SLR3 (ODBB_THET8)

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

Ordered Locus Names:

TTHA0230

Organism

Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) [Complete proteome] [HAMAP]

Taxonomic identifier

300852 [NCBI]

Taxonomic lineage

Bacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Thermus

Protein attributes

Sequence length	324 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) By similarity. UniProtKB P37941
Catalytic activity	3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine = [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + CO2. Ref.2
Cofactor	Thiamine pyrophosphate. Ref.2
Subunit structure	Heterotetramer of two alpha and two beta chains. Directly associated with ODBA in the E1 complex. Ref.2

Ontologies

Keywords
Ligand	Thiamine pyrophosphate
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome
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
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 324

324

2-oxoisovalerate dehydrogenase subunit beta

PRO_0000294977

Regions

Region

58 – 60

3

Thiamine pyrophosphate

Region

83 – 86

4

Substrate

Region

86 – 89

4

Thiamine pyrophosphate

Sites

Active site

129

1

Proton acceptor Probable

Binding site

29

1

Thiamine pyrophosphate

Binding site

82

1

Thiamine pyrophosphate

Binding site

129

1

Substrate

Experimental info

Sequence conflict

209

1

G → C Ref.2

Secondary structure

1

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324

Helix Strand Turn

Details...

Helix

6 – 20

15

Beta strand

24 – 28

5

Turn

40 – 43

4

Helix

44 – 48

5

Turn

50 – 52

3

Beta strand

53 – 55

3

Helix

60 – 73

14

Beta strand

76 – 80

5

Helix

84 – 86

3

Helix

88 – 90

3

Helix

91 – 96

6

Turn

97 – 100

4

Helix

101 – 104

4

Turn

105 – 107

3

Beta strand

114 – 119

6

Beta strand

121 – 124

4

Helix

126 – 128

3

Helix

134 – 138

5

Beta strand

144 – 147

4

Helix

151 – 163

13

Beta strand

168 – 173

6

Helix

174 – 176

3

Beta strand

177 – 179

3

Beta strand

197 – 200

4

Beta strand

203 – 209

7

Helix

211 – 213

3

Helix

214 – 226

13

Beta strand

231 – 235

5

Beta strand

238 – 240

3

Helix

244 – 254

11

Beta strand

257 – 265

9

Helix

269 – 281

13

Helix

282 – 284

3

Beta strand

290 – 294

5

Helix

304 – 307

4

Helix

311 – 323

13

Sequences

	Sequence		Length	Mass (Da)
	Q5SLR3-1 [UniParc]. Last modified December 21, 2004. Version 1. Checksum: 679926805496D29A	FASTA	324	35,093
	10 20 30 40 50 60 MALMTMVQAL NRALDEEMAK DPRVVVLGED VGKRGGVFLV TEGLLQKYGP DRVMDTPLSE 70 80 90 100 110 120 AAIVGAALGM AAHGLRPVAE IQFADYIFPG FDQLVSQVAK LRYRSGGQFT APLVVRMPSG 130 140 150 160 170 180 GGVRGGHHHS QSPEAHFVHT AGLKVVAVST PYDAKGLLKA AIRDEDPVVF LEPKRLYRSV 190 200 210 220 230 240 KEEVPEEDYT LPIGKAALRR EGKDLTLIGY GTVMPEVLQA AAELAKAGVS AEVLDLRTLM 250 260 270 280 290 300 PWDYEAVMNS VAKTGRVVLV SDAPRHASFV SEVAATIAED LLDMLLAPPI RVTGFDTPYP 310 320 YAQDKLYLPT VTRILNAAKR ALDY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete genome sequence of Thermus thermophilus HB8." Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S. Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]	"Ligand-induced conformational changes and a reaction intermediate in branched-chain 2-oxo acid dehydrogenase (E1) from Thermus thermophilus HB8, as revealed by X-ray crystallography." Nakai T., Nakagawa N., Maoka N., Masui R., Kuramitsu S., Kamiya N. J. Mol. Biol. 337:1011-1033(2004) [PubMed: 15033367] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH ODBA AND THIAMINE PYROPHOSPHATE, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AP008226 Genomic DNA. Translation: BAD70053.1.

RefSeq

YP_143496.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1UM9	X-ray	2.20	B/D	1-324	[»]
1UMB	X-ray	2.10	B/D	1-324	[»]
1UMC	X-ray	2.40	B/D	1-324	[»]
1UMD	X-ray	1.90	B/D	1-324	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

Q5SLR3.

Genome annotation databases

GeneID

3168889.

GenomeReviews

Gene locus TTHA0230 in contig AP008226_GR.

KEGG

ttj:TTHA0230.

NMPDR

fig|300852.3.peg.261.

Organism-specific databases

CMR

Search...

Phylogenomic databases

HOGENOM

Q5SLR3.

OMA

TLENEIM.

Enzyme and pathway databases

BioCyc

TTHE300852:TTHA0230-MON.

Family and domain databases

InterPro

IPR015941. Transketolase-like_C.
IPR005475. Transketolase-like_Pyr-bd.
IPR005476. Transketolase_C.
[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_THET8

Accession

Primary (citable) accession number: Q5SLR3
Secondary accession number(s): P84130

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 10, 2007
Last sequence update:	December 21, 2004
Last modified:	November 3, 2009
This is version 32 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)