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Reviewed, UniProtKB/Swiss-Prot Q72GU2 (ODBB_THET2)

Last modified June 16, 2009. Version 30. Feed History...

Clusters with 100%, 90%, 50% identity | 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

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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: TT_C1756
OrganismThermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039) [Complete proteome] [HAMAP]
Taxonomic identifier262724 [NCBI]
Taxonomic lineageBacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Thermus

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Protein attributes

Sequence length324 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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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. UniProtKB Q5SLR3

Cofactor

Thiamine pyrophosphate By similarity. UniProtKB Q5SLR3

Subunit structure

Heterotetramer of two alpha and two beta chains. Directly associated with ODBA in the E1 complex By similarity. UniProtKB Q5SLR3

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Ontologies

Keywords
   LigandThiamine pyrophosphate
   Molecular functionOxidoreductase
   Technical termComplete 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_0000294976

Regions

Region58 – 603Thiamine pyrophosphate By similarity UniProtKB Q5SLR3
Region83 – 864Substrate By similarity UniProtKB Q5SLR3
Region86 – 894Thiamine pyrophosphate By similarity UniProtKB Q5SLR3

Sites

Active site1291Proton acceptor Probable UniProtKB Q5SLR3
Binding site291Thiamine pyrophosphate By similarity UniProtKB Q5SLR3
Binding site821Thiamine pyrophosphate By similarity UniProtKB Q5SLR3
Binding site1291Substrate By similarity UniProtKB Q5SLR3

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Sequences

Sequence LengthMass (Da)Tools
Q72GU2-1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 6799254F5589D04A

FASTA32435,083
        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 LSIGKAALRR EGKDLTLIGY GTVMPEVLQA AAELAKAGVS AEVLDLRTLM 

       250        260        270        280        290        300 
PWDYEAVMNS VAKTGRVVLV SDAPRHASFV SEVAATIAED LLDMLLAPPI RVTGFDTPYP 

       310        320 
YAQDKLYLPT VTRILNAAKR ALDY

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References

[1]"The genome sequence of the extreme thermophile Thermus thermophilus."
Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H., Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C., Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P., Kramer W., Merkl R., Gottschalk G., Fritz H.-J.
Nat. Biotechnol. 22:547-553(2004) [PubMed: 15064768] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

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Cross-references

Sequence databases

AE017221 Genomic DNA. Translation: AAS82098.1.
RefSeqYP_005725.1.

3D structure databases

SMRQ72GU2. Positions 2-324.
ModBaseSearch...

Genome annotation databases

GeneID2775494.
GenomeReviewsGene locus TT_C1756 in contig AE017221_GR.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ72GU2.
OMAQ72GU2. TLENEIM.

Enzyme and pathway databases

BioCycTTHE262724:TT_C1756-MON.

Family and domain databases

InterProIPR005476. Transketo_C.
IPR015941. Transketolase_C-like.
IPR005475. Transketolase_central-reg.
[Graphical view]
Gene3DG3DSA:3.40.50.920. Transketo_C_like. 1 hit.
PfamPF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameODBB_THET2
AccessionPrimary (citable) accession number: Q72GU2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 10, 2007
Last sequence update: July 5, 2004
Last modified: June 16, 2009
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)
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information