Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial

Gene

Bckdha

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

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

Cofactori

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi203 – 2031PotassiumBy similarity
Metal bindingi208 – 2081PotassiumBy similarity
Metal bindingi209 – 2091PotassiumBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Metal-binding, Potassium, Thiamine pyrophosphate

Names & Taxonomyi

Protein namesi
Recommended name:
2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial (EC:1.2.4.4)
Alternative name(s):
Branched-chain alpha-keto acid dehydrogenase E1 component alpha chain
Short name:
BCKDE1A
Short name:
BCKDH E1-alpha
Gene namesi
Name:Bckdha
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:107701. Bckdha.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4242MitochondrionBy similarityAdd
BLAST
Chaini43 – 4424002-oxoisovalerate dehydrogenase subunit alpha, mitochondrialPRO_0000020467Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei334 – 3341PhosphoserineCombined sources
Modified residuei335 – 3351PhosphothreonineCombined sources
Modified residuei336 – 3361PhosphoserineCombined sources
Modified residuei344 – 3441PhosphoserineCombined sources
Modified residuei353 – 3531N6-acetyllysine; alternateCombined sources
Modified residuei353 – 3531N6-succinyllysine; alternateCombined sources
Modified residuei377 – 3771N6-succinyllysineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP50136.
MaxQBiP50136.
PaxDbiP50136.
PeptideAtlasiP50136.
PRIDEiP50136.

2D gel databases

SWISS-2DPAGEP50136.

PTM databases

iPTMnetiP50136.
PhosphoSiteiP50136.

Interactioni

Subunit structurei

Heterotetramer of alpha and beta chains.By similarity

Protein-protein interaction databases

IntActiP50136. 4 interactions.
MINTiMINT-4105779.
STRINGi10090.ENSMUSP00000071292.

Structurei

3D structure databases

ProteinModelPortaliP50136.
SMRiP50136. Positions 48-442.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni154 – 1563Thiamine pyrophosphate bindingBy similarity

Sequence similaritiesi

Belongs to the BCKDHA family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1182. Eukaryota.
COG1071. LUCA.
HOVERGENiHBG002459.
InParanoidiP50136.
PhylomeDBiP50136.

Family and domain databases

Gene3Di3.40.50.970. 1 hit.
InterProiIPR001017. DH_E1.
IPR029061. THDP-binding.
[Graphical view]
PfamiPF00676. E1_dh. 1 hit.
[Graphical view]
SUPFAMiSSF52518. SSF52518. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P50136-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSAAKIWRPS RGLRQAALLL LGRSGVRGLA RSHPSRQQQQ QFPSLDDKPQ
60 70 80 90 100
FPGASAEFVD KLEFIQPNVI SGIPIYRVMD RQGQIINPSE DPHLPQEEVL
110 120 130 140 150
KFYRSMTLLN TMDRILYESQ REGRISFYMT NYGEEGTHVG SAAALERTDL
160 170 180 190 200
VFGQYREAGV LMYRDYPLEL FMSQCYGNVN DPGKGRQMPV HYGCKERHFV
210 220 230 240 250
TISSPLATQI PQAVGAAYAA KRANANRIVI CYFGEGAASE GDAHAGFNFA
260 270 280 290 300
ATLECPIIFF CRNNGYAIST PTSEQYRGDG IAARGPGYGI KSIRVDGNDV
310 320 330 340 350
FAVYNATKEA RRRAVAENQP FLIEAMTYRI GHHSTSDDSS AYRSVDEVNY
360 370 380 390 400
WDKQDHPISR LRQYLLNQGW WDEEQEKAWR KQSRKKVMEA FEQAERKLKP
410 420 430 440
NPSLLFSDVY QEMPAQLRRQ QESLARHLQT YGEHYPLDHF EK
Length:442
Mass (Da):50,371
Last modified:October 1, 1996 - v1
Checksum:i3388213D88BC7C92
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L47335 mRNA. Translation: AAB38422.1.
PIRiS71881.
UniGeneiMm.25848.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L47335 mRNA. Translation: AAB38422.1.
PIRiS71881.
UniGeneiMm.25848.

3D structure databases

ProteinModelPortaliP50136.
SMRiP50136. Positions 48-442.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP50136. 4 interactions.
MINTiMINT-4105779.
STRINGi10090.ENSMUSP00000071292.

PTM databases

iPTMnetiP50136.
PhosphoSiteiP50136.

2D gel databases

SWISS-2DPAGEP50136.

Proteomic databases

EPDiP50136.
MaxQBiP50136.
PaxDbiP50136.
PeptideAtlasiP50136.
PRIDEiP50136.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

MGIiMGI:107701. Bckdha.

Phylogenomic databases

eggNOGiKOG1182. Eukaryota.
COG1071. LUCA.
HOVERGENiHBG002459.
InParanoidiP50136.
PhylomeDBiP50136.

Miscellaneous databases

PROiP50136.
SOURCEiSearch...

Family and domain databases

Gene3Di3.40.50.970. 1 hit.
InterProiIPR001017. DH_E1.
IPR029061. THDP-binding.
[Graphical view]
PfamiPF00676. E1_dh. 1 hit.
[Graphical view]
SUPFAMiSSF52518. SSF52518. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Effects of insulin on the regulation of branched-chain alpha-keto acid dehydrogenase E1 alpha subunit gene expression."
    Costeas P.A., Chinsky J.M.
    Biochem. J. 318:85-92(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6J.
    Tissue: Liver.
  2. "Mitochondrial phosphoproteome revealed by an improved IMAC method and MS/MS/MS."
    Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.
    Mol. Cell. Proteomics 6:669-676(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  4. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-334, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-334; THR-335; SER-336 AND SER-344, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  6. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-353 AND LYS-377, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  7. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-353, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiODBA_MOUSE
AccessioniPrimary (citable) accession number: P50136
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 6, 2016
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Bound potassium ions stabilize the protein structure.By similarity

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.