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Reviewed, UniProtKB/Swiss-Prot Q5SLR4 (ODBA_THET8)

Last modified November 4, 2008. Version 30. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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) [Complete proteome] [HAMAP]
Taxonomic identifier300852 [NCBI]
Taxonomic lineageBacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Thermus

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Protein attributes

Sequence length367 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (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 + CO(2).

Cofactor

Thiamine pyrophosphate.

Subunit structure

Heterotetramer of two alpha and two beta chains. Directly associated with ODBB in the E1 complex.

Sequence similarities

Belongs to the BCKDHA family.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3673672-oxoisovalerate dehydrogenase subunit alpha
PRO_0000294975

Regions

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

Sites

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

Secondary structure

1 .............................................. 367
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Q5SLR4-1 [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

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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].
[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 ODBB AND THIAMINE PYROPHOSPHATE, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT.

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Cross-references

Sequence databases

AP008226 Genomic DNA. Translation: BAD70052.1.
RefSeqYP_143495.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1UM9X-ray2.20A/C1-367[»]
1UMBX-ray2.10A/C1-367[»]
1UMCX-ray2.40A/C1-367[»]
1UMDX-ray1.90A/C1-367[»]
ModBaseSearch...

Genome annotation databases

GeneID3168003.
GenomeReviewsGene locus TTHA0229 in contig AP008226_GR.
KEGGttj:TTHA0229.
NMPDRfig|300852.3.peg.260.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ5SLR4.

Enzyme and pathway databases

BioCycTTHE300852:TTHA0229-MON.

Family and domain databases

InterProIPR001017. DHase_E1.
[Graphical view]
PfamPF00676. E1_dh. 1 hit.
[Graphical view]
ProtoNetSearch...

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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 4, 2008
This is version 30 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents