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Reviewed, UniProtKB/Swiss-Prot Q5SLR3 (ODBB_THET8)

Last modified January 19, 2010. Version 35. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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 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
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 length324 AA.
Sequence statusComplete.
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 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

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Ontologies

Keywords
   LigandThiamine pyrophosphate
   Molecular functionOxidoreductase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular function3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3243242-oxoisovalerate dehydrogenase subunit beta
PRO_0000294977

Regions

Region58 – 603Thiamine pyrophosphate
Region83 – 864Substrate
Region86 – 894Thiamine pyrophosphate

Sites

Active site1291Proton acceptor Probable
Binding site291Thiamine pyrophosphate
Binding site821Thiamine pyrophosphate
Binding site1291Substrate

Experimental info

Sequence conflict2091G → C Ref.2

Secondary structure

1 ............................................................... 324
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Q5SLR3-1 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: 679926805496D29A

FASTA32435,093
        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

« Hide

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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 ODBA AND THIAMINE PYROPHOSPHATE, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AP008226 Genomic DNA. Translation: BAD70053.1.
RefSeqYP_143496.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1UM9X-ray2.20B/D1-324[»]
1UMBX-ray2.10B/D1-324[»]
1UMCX-ray2.40B/D1-324[»]
1UMDX-ray1.90B/D1-324[»]
ModBaseSearch...

Protein-protein interaction databases

STRINGQ5SLR3.

Genome annotation databases

GeneID3168889.
GenomeReviewsGene locus TTHA0230 in contig AP008226_GR.
KEGGttj:TTHA0230.
NMPDRfig|300852.3.peg.261.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0022.
HOGENOMHBG753264.
OMASDAPRHA.

Enzyme and pathway databases

BioCycTTHE300852:TTHA0230-MONOMER.

Family and domain databases

InterProIPR009014. Transketo_C/Pyr-ferredox_oxred.
IPR015941. Transketolase-like_C.
IPR005475. Transketolase-like_Pyr-bd.
IPR005476. Transketolase_C.
[Graphical view]
Gene3DG3DSA:3.40.50.920. Transketo_C_like. 1 hit.
PfamPF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
[Graphical view]
SMARTSM00861. Transket_pyr. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameODBB_THET8
AccessionPrimary (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: January 19, 2010
This is version 35 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

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