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Protein

2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial

Gene

BCKDHA

Organism
Bos taurus (Bovine)
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).1 Publication

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 bindingi216 – 2161PotassiumBy similarity
Metal bindingi221 – 2211PotassiumBy similarity
Metal bindingi222 – 2221PotassiumBy similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Metal-binding, Potassium, Thiamine pyrophosphate

Enzyme and pathway databases

SABIO-RKP11178.

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
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5555MitochondrionAdd
BLAST
Chaini56 – 4554002-oxoisovalerate dehydrogenase subunit alpha, mitochondrialPRO_0000020464Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei347 – 3471PhosphoserineBy similarity
Modified residuei348 – 3481PhosphothreonineBy similarity
Modified residuei349 – 3491PhosphoserineBy similarity
Modified residuei357 – 3571PhosphoserineBy similarity
Modified residuei366 – 3661N6-acetyllysine; alternateBy similarity
Modified residuei366 – 3661N6-succinyllysine; alternateBy similarity
Modified residuei390 – 3901N6-succinyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP11178.
PRIDEiP11178.

Expressioni

Tissue specificityi

Expressed in kidney (at protein level).1 Publication

Interactioni

Subunit structurei

Heterotetramer of alpha and beta chains.By similarity

Protein-protein interaction databases

IntActiP11178. 1 interaction.
STRINGi9913.ENSBTAP00000021342.

Structurei

3D structure databases

ProteinModelPortaliP11178.
SMRiP11178. Positions 61-455.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni167 – 1693Thiamine pyrophosphate bindingBy similarity

Sequence similaritiesi

Belongs to the BCKDHA family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1182. Eukaryota.
COG1071. LUCA.
HOGENOMiHOG000281337.
HOVERGENiHBG002459.
InParanoidiP11178.
KOiK00166.

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.

P11178-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQGSAKMAMA VAVAVARVWR PSRGLGRTGL PLLRLLGARG LARFHPHRWQ
60 70 80 90 100
QQQHFSSLDD KPQFPGASAE FIDKLEFIQP NVISGIPIYR VMDRQGQIIN
110 120 130 140 150
PSEDPHLPQE KVLKFYKSMT LLNTMDRILY ESQRQGRISF YMTNYGEEGT
160 170 180 190 200
HVGSAAALDD TDLVFGQYRE AGVLMYRDYP LELFMAQCYG NVSDLGKGRQ
210 220 230 240 250
MPVHYGCRER HFVTISSPLA TQIPQAVGAA YAAKRANANR VVICYFGEGA
260 270 280 290 300
ASEGDAHAGF NFAATLECPI IFFCRNNGYA ISTPTSEQYR GDGIAARGPG
310 320 330 340 350
YGILSIRVDG NDVFAVYNAT KEARRRAVAE NQPFLIEAMT YRIGHHSTSD
360 370 380 390 400
DSSAYRSVDE VNYWDKQDHP ISRLRHHLQS RGWWDDEQEK AWRKQSRKKV
410 420 430 440 450
MEAFEQAERK LKPNPSLIFS DVYQEMPAQL RKQQESLARH LQTYGEHYPL

DHFEK
Length:455
Mass (Da):51,678
Last modified:July 1, 1989 - v1
Checksum:i66A7CA6003E0B846
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03759 mRNA. Translation: AAA30595.1.
PIRiA28073. DEBOXA.
RefSeqiNP_776931.1. NM_174506.1.
UniGeneiBt.5287.

Genome annotation databases

GeneIDi282149.
KEGGibta:282149.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03759 mRNA. Translation: AAA30595.1.
PIRiA28073. DEBOXA.
RefSeqiNP_776931.1. NM_174506.1.
UniGeneiBt.5287.

3D structure databases

ProteinModelPortaliP11178.
SMRiP11178. Positions 61-455.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP11178. 1 interaction.
STRINGi9913.ENSBTAP00000021342.

Proteomic databases

PaxDbiP11178.
PRIDEiP11178.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi282149.
KEGGibta:282149.

Organism-specific databases

CTDi593.

Phylogenomic databases

eggNOGiKOG1182. Eukaryota.
COG1071. LUCA.
HOGENOMiHOG000281337.
HOVERGENiHBG002459.
InParanoidiP11178.
KOiK00166.

Enzyme and pathway databases

SABIO-RKP11178.

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...

Entry informationi

Entry nameiODBA_BOVIN
AccessioniPrimary (citable) accession number: P11178
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: June 8, 2016
This is version 116 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. 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.