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Q72GU1 (ODBA_THET2) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·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:TT_C1757
OrganismThermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039) [Complete proteome] [HAMAP]
Taxonomic identifier262724 [NCBI]
Taxonomic lineageBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

Protein attributes

Sequence length367 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 Q5SLR4

Catalytic activity

3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine = [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + CO2. UniProtKB Q5SLR4

Cofactor

Thiamine pyrophosphate By similarity. UniProtKB Q5SLR4

Subunit structure

Heterotetramer of two alpha and two beta chains. Directly associated with ODBB in the E1 complex By similarity. UniProtKB Q5SLR4

Sequence similarities

Belongs to the BCKDHA family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3673672-oxoisovalerate dehydrogenase subunit alpha
PRO_0000294974

Regions

Region94 – 963Thiamine pyrophosphate binding By similarity UniProtKB Q5SLR4
Region128 – 1314Substrate binding By similarity UniProtKB Q5SLR4
Region144 – 1463Thiamine pyrophosphate binding By similarity UniProtKB Q5SLR4
Region174 – 1807Thiamine pyrophosphate binding By similarity UniProtKB Q5SLR4
Region204 – 2085Thiamine pyrophosphate binding By similarity UniProtKB Q5SLR4

Sites

Metal binding1751Magnesium By similarity UniProtKB Q5SLR4
Metal binding2041Magnesium By similarity UniProtKB Q5SLR4
Metal binding2061Magnesium; via carbonyl oxygen By similarity UniProtKB Q5SLR4
Binding site661Substrate By similarity UniProtKB Q5SLR4
Binding site951Substrate By similarity UniProtKB Q5SLR4
Binding site1441Substrate By similarity UniProtKB Q5SLR4
Binding site2731Thiamine pyrophosphate By similarity UniProtKB Q5SLR4

Sequences

Sequence LengthMass (Da)Tools
Q72GU1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 726F33C315656E49

FASTA36741,442
        10         20         30         40         50         60 
MVKETHRFEP FTEEPIRLIG EEGEWLGDFP LDLEGEKLRR LYRDMLAARM LDERYTILIR 

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

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

       190        200        210        220        230        240 
GDWYAGINFA AVQGAPAVFV CENNFYAISV 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 PEWMFADVFA EKPWHLLRQE 


ALLKEEL 

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017221 Genomic DNA. Translation: AAS82099.1.
RefSeqYP_005726.1. NC_005835.1.

3D structure databases

ProteinModelPortalQ72GU1.
SMRQ72GU1. Positions 6-367.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING262724.TTC1757.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAS82099; AAS82099; TT_C1757.
GeneID2776443.
KEGGtth:TTC1757.
PATRIC23953983. VBITheThe54392_1757.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1071.
KOK00166.
OMANEEWEED.
OrthoDBEOG6VMTKR.
ProtClustDBCLSK2762003.

Enzyme and pathway databases

BioCycTTHE262724:GCAT-1795-MONOMER.

Family and domain databases

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

Entry information

Entry nameODBA_THET2
AccessionPrimary (citable) accession number: Q72GU1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 10, 2007
Last sequence update: July 5, 2004
Last modified: November 13, 2013
This is version 58 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