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Reviewed, UniProtKB/Swiss-Prot P21839 (ODBB_BOVIN)

Last modified November 3, 2009. Version 70. 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

Names and origin

Protein namesRecommended 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
Name: BCKDHB
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length392 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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

Mitochondrion matrix.

Ontologies

Keywords
   Cellular componentMitochondrion
   DomainTransit peptide
   Molecular functionOxidoreductase
   PTMAcetylation
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

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

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 5050Mitochondrion
Chain51 – 3923422-oxoisovalerate dehydrogenase subunit beta, mitochondrial
PRO_0000020469

Amino acid modifications

Modified residue2411N6-acetyllysine By similarity

Experimental info

Sequence conflict24 – 4623RRLCG…YGAAA → GPGCVARACRGASCSPPRPT GLR Ref.3
Sequence conflict281G → C in AAI18381. Ref.2
Sequence conflict2831V → E in AAA51410. Ref.3
Sequence conflict2881A → D in AAA30407. Ref.1
Sequence conflict3481E → Q in AAA51410. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P21839-1 [UniParc].

Last modified October 3, 2006. Version 2.
Checksum: 4E3ABC39ED54281A

FASTA39242,935
        10         20         30         40         50         60 
MAAVAAFAGW LLRLRAAGAD GPWRRLCGAG LSRGFLQSAS AYGAAAQRRQ VAHFTFQPDP 

        70         80         90        100        110        120 
EPVEYGQTQK MNLFQAVTSA LDNSLAKDPT AVIFGEDVAF GGVFRCTVGL RDKYGKDRVF 

       130        140        150        160        170        180 
NTPLCEQGIV GFGIGIAVTG ATAIAEIQFA DYIFPAFDQI VNEAAKYRYR SGDLFNCGSL 

       190        200        210        220        230        240 
TIRSPWGCVG HGALYHSQSP EAFFAHCPGI KVVVPRSPFQ AKGLLLSCIE DKNPCIFFEP 

       250        260        270        280        290        300 
KILYRAAVEQ VPVEPYNIPL SQAEVIQEGS DVTLVAWGTQ VHVIREVAAM AQEKLGVSCE 

       310        320        330        340        350        360 
VIDLRTILPW DVDTVCKSVI KTGRLLVSHE APLTGGFASE ISSTVQEECF LNLEAPISRV 

       370        380        390 
CGYDTPFPHI FEPFYIPDKW KCYDALRKMI NY 

« Hide

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.
IPIIPI00696901.
PIRA34267.
RefSeqNP_776932.1.
UniGeneBt.5412

3D structure databases

HSSPHSSP built from PDB template 1DTW based on UniProtKB P21953.
SMRP21839. Positions 64-392.
ModBaseSearch...

Protein-protein interaction databases

STRINGP21839.

Genome annotation databases

EnsemblENSBTAT00000016044; ENSBTAP00000016044; ENSBTAG00000012096; Bos taurus. [Genome view]
GeneID282150.
KEGGbta:282150.

Organism-specific databases

CTD282150.

Phylogenomic databases

HOVERGENP21839.
OMAHEATLTS.

Enzyme and pathway databases

BRENDA1.2.4.4. 251.

Family and domain databases

InterProIPR015941. 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]
ProtoNetSearch...

Entry information

Entry nameODBB_BOVIN
AccessionPrimary (citable) accession number: P21839
Secondary accession number(s): Q148F4, Q28047
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: October 3, 2006
Last modified: November 3, 2009
This is version 70 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information