NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
"Complete genome sequence of Thermus thermophilus HB8.";
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.

[2]

X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH ODBB AND THIAMINE PYROPHOSPHATE, CATALYTIC ACTIVITY, COFACTOR, AND SUBUNIT.
DOI=10.1016/j.jmb.2004.02.011; PubMed=15033367 [NCBI, ExPASy, EBI, Israel, Japan]
Nakai T., Nakagawa N., Maoka N., Masui R., Kuramitsu S., Kamiya N.;
"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.";
J. Mol. Biol. 337:1011-1033(2004).

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) (By similarity).
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: Heterotetramer of two alpha and two beta chains. Directly associated with ODBB in the E1 complex.
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

AP008226; BAD70052.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_143495.1; -.

3D structure databases

PDB

1UM9; X-ray; 2.20 A; A/C=1-367.	[ExPASy / RCSB / EBI]
1UMB; X-ray; 2.10 A; A/C=1-367.	[ExPASy / RCSB / EBI]
1UMC; X-ray; 2.40 A; A/C=1-367.	[ExPASy / RCSB / EBI]
1UMD; X-ray; 1.90 A; A/C=1-367.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1UM9; -.
1UMB; -.
1UMC; -.
1UMD; -.

ModBase

Q5SLR4.

Enzyme and pathway databases

BioCyc

TTHE300852:TTHA0229-MON; -.

Ontologies

GO:0003863;	Molecular function: 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity (inferred from electronic annotation from EC).
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.

BLOCKS

Q5SLR4.

Genome annotation databases

GeneID

3168003; -.

GenomeReviews

AP008226_GR; TTHA0229.

KEGG

ttj:TTHA0229; -.

NMPDR

fig|300852.3.peg.260; -.

Phylogenomic databases

HOGENOM

Q5SLR4; -.

Genome annotation databases

CMR

Q5SLR4; TTHA0229.

Other

ProtoNet

Q5SLR4.

UniRef

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

Keywords

3D-structure; Complete proteome; Magnesium; Metal-binding; Oxidoreductase; Thiamine pyrophosphate.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 367`	`367`	`2-oxoisovalerate dehydrogenase subunit alpha.`	`PRO_0000294975`
`REGION`	`94 96`	`3`	`Thiamine pyrophosphate binding.`
`REGION`	`128 131`	`4`	`Substrate binding.`
`REGION`	`144 146`	`3`	`Thiamine pyrophosphate binding.`
`REGION`	`174 180`	`7`	`Thiamine pyrophosphate binding.`
`REGION`	`204 208`	`5`	`Thiamine pyrophosphate binding.`
`METAL`	`175 175`		`Magnesium.`
`METAL`	`204 204`		`Magnesium.`
`METAL`	`206 206`		`Magnesium (via carbonyl oxygen).`
`BINDING`	`66 66`		`Substrate.`
`BINDING`	`95 95`		`Substrate.`
`BINDING`	`144 144`		`Substrate.`
`BINDING`	`273 273`		`Thiamine pyrophosphate.`
`HELIX`	`35 60`	`26`
`HELIX`	`74 83`	`10`
`STRAND`	`89 92`	`4`
`HELIX`	`98 104`	`7`
`HELIX`	`108 116`	`9`
`TURN`	`122 125`	`4`
`TURN`	`135 138`	`4`
`STRAND`	`144 147`	`4`
`HELIX`	`150 162`	`13`
`STRAND`	`169 173`	`5`
`HELIX`	`176 179`	`4`
`HELIX`	`181 193`	`13`
`STRAND`	`196 204`	`9`
`HELIX`	`222 227`	`6`
`STRAND`	`232 236`	`5`
`HELIX`	`240 255`	`16`
`STRAND`	`261 267`	`7`
`HELIX`	`296 305`	`10`
`TURN`	`306 308`	`3`
`HELIX`	`312 334`	`23`
`HELIX`	`341 345`	`5`
`STRAND`	`348 351`	`4`
`HELIX`	`354 366`	`13`

Sequence information

Length: 367 AA [This is the length of the unprocessed precursor]

Molecular weight: 41452 Da [This is the MW of the unprocessed precursor]

CRC64: 178B4EFE0CA5F1D1 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MVKETHRFET FTEEPIRLIG EEGEWLGDFP LDLEGEKLRR LYRDMLAARM LDERYTILIR 

        70         80         90        100        110        120 
TGKTSFIAPA AGHEAAQVAI AHAIRPGFDW VFPYYRDHGL ALALGIPLKE LLGQMLATKA 

       130        140        150        160        170        180 
DPNKGRQMPE HPGSKALNFF TVASPIASHV PPAAGAAISM KLLRTGQVAV CTFGDGATSE 

       190        200        210        220        230        240 
GDWYAGINFA AVQGAPAVFI AENNFYAISV DYRHQTHSPT IADKAHAFGI PGYLVDGMDV 

       250        260        270        280        290        300 
LASYYVVKEA VERARRGEGP SLVELRVYRY GPHSSADDDS RYRPKEEVAF WRKKDPIPRF 

       310        320        330        340        350        360 
RRFLEARGLW NEEWEEDVRE EIRAELERGL KEAEEAGPVP PEWMFEDVFA EKPWHLLRQE 


ALLKEEL

Q5SLR4 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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