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UniProtKB/Swiss-Prot entry Q72GU1

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ODBA_THET2
Primary accession number Q72GU1
Secondary accession numbers None
Integrated into Swiss-Prot on July 10, 2007
Sequence was last modified on July 5, 2004 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 27)
Name and origin of the protein
Protein name 2-oxoisovalerate dehydrogenase subunit alpha
Synonyms EC 1.2.4.4
Branched-chain alpha-keto acid dehydrogenase E1 component alpha chain
BCKDH E1-alpha
Gene name
OrderedLocusNames: TT_C1757
From
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039) [TaxID: 262724] [HAMAP proteome]
Taxonomy Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nbt956; PubMed=15064768 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The genome sequence of the extreme thermophile Thermus thermophilus.";
Nat. Biotechnol. 22:547-553(2004).
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 + CO2.
  • COFACTOR: Thiamine pyrophosphate (By similarity).
  • SUBUNIT: Heterotetramer of two alpha and two beta chains. Directly associated with ODBB in the E1 complex (By similarity).
  • SIMILARITY: Belongs to the BCKDHA family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AE017221; AAS82099.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_005726.1; -.
3D structure databases
SMR Q72GU1; 6-367.
ModBase Q72GU1.
Enzyme and pathway databases
BioCyc TTHE262724:TT_C1757-MON; -.
Family and domain databases
InterPro IPR001017; DHase_E1.
Graphical view of domain structure.
Pfam PF00676; E1_dh; 1.
Pfam graphical view of domain structure.
BLOCKS Q72GU1.
Genome annotation databases
GeneID 2776443; -.
GenomeReviews AE017221_GR; TT_C1757.
Phylogenomic databases
HOGENOM Q72GU1; -.
Genome annotation databases
CMR Q72GU1; TT_C1757.
Other
ProtoNet Q72GU1.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Magnesium; Metal-binding; Oxidoreductase; Thiamine pyrophosphate.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   367  367     2-oxoisovalerate dehydrogenase subunit alpha. PRO_0000294974
REGION   94    96  3     Thiamine pyrophosphate binding (By similarity). 
REGION   128   131  4     Substrate binding (By similarity). 
REGION   144   146  3     Thiamine pyrophosphate binding (By similarity). 
REGION   174   180  7     Thiamine pyrophosphate binding (By similarity). 
REGION   204   208  5     Thiamine pyrophosphate binding (By similarity). 
METAL   175   175        Magnesium (By similarity). 
METAL   204   204        Magnesium (By similarity). 
METAL   206   206        Magnesium; via carbonyl oxygen (By similarity). 
BINDING   66    66        Substrate (By similarity). 
BINDING   95    95        Substrate (By similarity). 
BINDING   144   144        Substrate (By similarity). 
BINDING   273   273        Thiamine pyrophosphate (By similarity). 
Sequence information
Length: 367 AA [This is the length of the unprocessed precursor] Molecular weight: 41442 Da [This is the MW of the unprocessed precursor] CRC64: 726F33C315656E49 [This is a checksum on the sequence] 
        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
Q72GU1 in FASTA format

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