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Q5SLR4 (ODBA_THET8) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
Ordered Locus Names:TTHA0229
OrganismThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) [Reference proteome] [HAMAP]
Taxonomic identifier300852 [NCBI]
Taxonomic lineageBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

Protein attributes

Sequence length367 AA.
Sequence statusComplete.
Protein existenceEvidence 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 P37940

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 ODBB in the E1 complex. Ref.2

Sequence similarities

Belongs to the BCKDHA family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

TTHA0230Q5SLR34EBI-1038222,EBI-1038230

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3673672-oxoisovalerate dehydrogenase subunit alpha
PRO_0000294975

Regions

Region94 – 963Thiamine pyrophosphate binding Ref.2
Region128 – 1314Substrate binding Ref.2
Region144 – 1463Thiamine pyrophosphate binding Ref.2
Region174 – 1807Thiamine pyrophosphate binding Ref.2
Region204 – 2085Thiamine pyrophosphate binding Ref.2

Sites

Metal binding1751Magnesium Ref.2
Metal binding2041Magnesium Ref.2
Metal binding2061Magnesium; via carbonyl oxygen Ref.2
Binding site661Substrate Ref.2
Binding site951Substrate Ref.2
Binding site1441Substrate Ref.2
Binding site2731Thiamine pyrophosphate Ref.2

Secondary structure

......................................................... 367
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q5SLR4 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: 178B4EFE0CA5F1D1

FASTA36741,452
        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 

« Hide

References

« Hide '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].
Strain: HB8 / ATCC 27634 / DSM 579.
[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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH ODBB AND THIAMINE PYROPHOSPHATE, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP008226 Genomic DNA. Translation: BAD70052.1.
RefSeqYP_143495.1. NC_006461.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1UM9X-ray2.20A/C1-367[»]
1UMBX-ray2.10A/C1-367[»]
1UMCX-ray2.40A/C1-367[»]
1UMDX-ray1.90A/C1-367[»]
ProteinModelPortalQ5SLR4.
SMRQ5SLR4. Positions 6-367.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ5SLR4. 1 interaction.
STRING300852.TTHA0229.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD70052; BAD70052; BAD70052.
GeneID3168003.
KEGGttj:TTHA0229.
PATRIC23955399. VBITheThe93045_0227.

Phylogenomic databases

eggNOGCOG1071.
HOGENOMHOG000281335.
KOK00166.
OMANEEWEED.
OrthoDBEOG6VMTKR.
ProtClustDBCLSK2762003.

Enzyme and pathway databases

BioCycTTHE300852:GH8R-238-MONOMER.

Family and domain databases

InterProIPR001017. DH_E1.
[Graphical view]
PfamPF00676. E1_dh. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ5SLR4.

Entry information

Entry nameODBA_THET8
AccessionPrimary (citable) accession number: Q5SLR4
Secondary accession number(s): P84129
Entry history
Integrated into UniProtKB/Swiss-Prot: July 10, 2007
Last sequence update: December 21, 2004
Last modified: November 13, 2013
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references