Reviewed,
UniProtKB/Swiss-Prot P21839 (ODBB_BOVIN)
Last modified
November 3, 2009.
Version 70.
History...
Clusters with 100%,
90%,
50% identity |
Third-party data |
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Names and origin
| Protein names | Recommended name: 2-oxoisovalerate dehydrogenase subunit beta, mitochondrial 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 |
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| Organism | Bos taurus (Bovine) | ||
| Taxonomic identifier | 9913 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos |
Protein attributes
| Sequence length | 392 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
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). |
| Catalytic activity | 3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine = [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + CO2. |
| Subunit structure | Heterodimer of an alpha and a beta chain. |
| Subcellular location |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Mitochondrion |
| Domain | Transit peptide |
| Molecular function | Oxidoreductase |
| PTM | Acetylation |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – 50 | 50 | Mitochondrion | ||||||
| Chain | 51 – 392 | 342 | 2-oxoisovalerate dehydrogenase subunit beta, mitochondrial | PRO_0000020469 | |||||
Amino acid modifications | |||||||||
| Modified residue | 241 | 1 | N6-acetyllysine By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 24 – 46 | 23 | RRLCG…YGAAA → GPGCVARACRGASCSPPRPT GLR Ref.3 | ||||||
| Sequence conflict | 28 | 1 | G → C in AAI18381. Ref.2 | ||||||
| Sequence conflict | 283 | 1 | V → E in AAA51410. Ref.3 | ||||||
| Sequence conflict | 288 | 1 | A → D in AAA30407. Ref.1 | ||||||
| Sequence conflict | 348 | 1 | E → Q in AAA51410. Ref.3 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Isolation and characterization of a complementary DNA clone coding for the E1 beta subunit of the bovine branched-chain alpha-ketoacid dehydrogenase complex: complete amino acid sequence of the precursor protein and its proteolytic processing." Nobukuni Y., Mitsubuchi H., Endo F., Asaka J., Oyama R., Titani K., Matsuda I. Biochemistry 29:1154-1160(1990) [PubMed: 2322554] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE. |
| [2] | NIH - Mammalian Gene Collection (MGC) project Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Fetal pons. |
| [3] | "Cloning and expression in Escherichia coli of mature E1 beta subunit of bovine mitochondrial branched-chain alpha-keto acid dehydrogenase complex. Mapping of the E1 beta-binding region on E2." Wynn R.M., Chuang J.L., Davie J.R., Fisher C.W., Hale M.A., Cox R.P., Chuang D.T. J. Biol. Chem. 267:1881-1887(1992) [PubMed: 1730724] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 24-392. Tissue: Liver. |
Cross-references
Sequence databases | |
|---|---|
| M33323 mRNA. Translation: AAA30407.1. BC118380 mRNA. Translation: AAI18381.1. M81742 mRNA. Translation: AAA51410.1. | |
| IPI | IPI00696901. |
| PIR | A34267. |
| RefSeq | NP_776932.1. |
| UniGene | Bt.5412 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1DTW based on UniProtKB P21953. |
| SMR | P21839. Positions 64-392. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | P21839. |
Genome annotation databases | |
| Ensembl | ENSBTAT00000016044; ENSBTAP00000016044; ENSBTAG00000012096; Bos taurus. [Genome view] |
| GeneID | 282150. |
| KEGG | bta:282150. |
Organism-specific databases | |
| CTD | 282150. |
Phylogenomic databases | |
| HOVERGEN | P21839. |
| OMA | HEATLTS. |
Enzyme and pathway databases | |
| BRENDA | 1.2.4.4. 251. |
Family and domain databases | |
| InterPro | IPR015941. Transketolase-like_C. IPR005475. Transketolase-like_Pyr-bd. IPR005476. Transketolase_C. [Graphical view] |
| Gene3D | G3DSA:3.40.50.920. Transketo_C_like. 1 hit. |
| Pfam | PF02779. Transket_pyr. 1 hit. PF02780. Transketolase_C. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ODBB_BOVIN | ||||||||
| Accession | Primary (citable) accession number: P21839 Secondary accession number(s): Q148F4, Q28047 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||

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