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Protein

2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial

Gene

Y39E4A.3

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 3 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) (By similarity). Required for the production of the monomethyl branched-chain fatty acids (mmBCFAs) isopentadecanoate (C15iso) and isoheptadecanoate (C17iso).By similarity1 Publication

Catalytic activityi

3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine = [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + CO2.1 Publication

Cofactori

Pathwayi: fatty acid biosynthesis

This protein is involved in the pathway fatty acid biosynthesis, which is part of Lipid metabolism.1 Publication
View all proteins of this organism that are known to be involved in the pathway fatty acid biosynthesis and in Lipid metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi189 – 1891PotassiumBy similarity
Metal bindingi194 – 1941PotassiumBy similarity
Metal bindingi195 – 1951PotassiumBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Keywords - Ligandi

Metal-binding, Potassium

Enzyme and pathway databases

ReactomeiR-CEL-389661. Glyoxylate metabolism and glycine degradation.
R-CEL-70895. Branched-chain amino acid catabolism.
UniPathwayiUPA00094.

Chemistry

SwissLipidsiSLP:000000190.

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
Gene namesi
ORF Names:Y39E4A.3
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome III

Organism-specific databases

WormBaseiY39E4A.3a; CE33866; WBGene00012713.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 4312-oxoisovalerate dehydrogenase subunit alpha, mitochondrialPRO_0000421270
Transit peptidei1 – ?MitochondrionSequence analysis

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiO45924.
PaxDbiO45924.
PRIDEiO45924.

Expressioni

Gene expression databases

ExpressionAtlasiO45924. baseline and differential.

Interactioni

Protein-protein interaction databases

BioGridi41889. 3 interactions.
DIPiDIP-25302N.
IntActiO45924. 1 interaction.
MINTiMINT-1048223.
STRINGi6239.Y39E4A.3b.

Structurei

3D structure databases

ProteinModelPortaliO45924.
SMRiO45924. Positions 42-423.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni140 – 1423Thiamine pyrophosphate bindingBy similarity

Sequence similaritiesi

Belongs to the BCKDHA family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1182. Eukaryota.
COG1071. LUCA.
GeneTreeiENSGT00530000063174.
HOGENOMiHOG000281337.
InParanoidiO45924.
KOiK00166.
OMAiDWIFPSY.
OrthoDBiEOG7WT41H.

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.

O45924-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHRALLNASR RVATVRSMAS TVEGDAFRLS EYSSKYLGHR KAAFTEKLEI
60 70 80 90 100
VNADDTPALP IYRVTNAVGD VIDKSQDPNF DEQTSLKMYK TMTQLNIMDR
110 120 130 140 150
ILYDSQRQGR ISFYMTSFGE EGNHVGSAAA LEPQDLIYGQ YREAGVLLWR
160 170 180 190 200
GYTMENFMNQ CYGNADDLGK GRQMPMHFGT KERNFVTISS PLTTQLPQAV
210 220 230 240 250
GSAYAFKQQK DNNRIAVVYF GDGAASEGDA HAAFNFAATL KCPIIFFCRN
260 270 280 290 300
NGYAISTPTS EQYGGDGIAG KGPAYGLHTI RVDGNDLLAV YNATKEARRV
310 320 330 340 350
ALTNRPVLIE AMTYRLGHHS TSDDSTAYRS SDEVQTWGDK DHPITRFKKY
360 370 380 390 400
ITERGWWNEE KEMEWQKEVK KRVLTEFAAA EKRKKAHYHD LFEDVYDELP
410 420 430
LRLRRQRDEL DAHVAEYKEH YPMLETLQSK P
Length:431
Mass (Da):49,021
Last modified:June 1, 2003 - v2
Checksum:iA6CAA29B9220AB1C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL021480 Genomic DNA. Translation: CAA16329.2.
PIRiT26758.
RefSeqiNP_001033376.1. NM_001038287.2.
NP_001033377.1. NM_001038288.4.
UniGeneiCel.22981.

Genome annotation databases

EnsemblMetazoaiY39E4A.3a; Y39E4A.3a; WBGene00012713.
GeneIDi176716.
KEGGicel:CELE_Y39E4A.3.
UCSCiY39E4A.3b. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL021480 Genomic DNA. Translation: CAA16329.2.
PIRiT26758.
RefSeqiNP_001033376.1. NM_001038287.2.
NP_001033377.1. NM_001038288.4.
UniGeneiCel.22981.

3D structure databases

ProteinModelPortaliO45924.
SMRiO45924. Positions 42-423.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi41889. 3 interactions.
DIPiDIP-25302N.
IntActiO45924. 1 interaction.
MINTiMINT-1048223.
STRINGi6239.Y39E4A.3b.

Chemistry

SwissLipidsiSLP:000000190.

Proteomic databases

EPDiO45924.
PaxDbiO45924.
PRIDEiO45924.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiY39E4A.3a; Y39E4A.3a; WBGene00012713.
GeneIDi176716.
KEGGicel:CELE_Y39E4A.3.
UCSCiY39E4A.3b. c. elegans.

Organism-specific databases

CTDi176716.
WormBaseiY39E4A.3a; CE33866; WBGene00012713.

Phylogenomic databases

eggNOGiKOG1182. Eukaryota.
COG1071. LUCA.
GeneTreeiENSGT00530000063174.
HOGENOMiHOG000281337.
InParanoidiO45924.
KOiK00166.
OMAiDWIFPSY.
OrthoDBiEOG7WT41H.

Enzyme and pathway databases

UniPathwayiUPA00094.
ReactomeiR-CEL-389661. Glyoxylate metabolism and glycine degradation.
R-CEL-70895. Branched-chain amino acid catabolism.

Miscellaneous databases

NextBioi893714.
PROiO45924.

Gene expression databases

ExpressionAtlasiO45924. baseline and differential.

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. "Genome sequence of the nematode C. elegans: a platform for investigating biology."
    The C. elegans sequencing consortium
    Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Bristol N2.
  2. "Monomethyl branched-chain fatty acids play an essential role in Caenorhabditis elegans development."
    Kniazeva M., Crawford Q.T., Seiber M., Wang C.Y., Han M.
    PLoS Biol. 2:E257-E257(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY.

Entry informationi

Entry nameiODBA_CAEEL
AccessioniPrimary (citable) accession number: O45924
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 6, 2013
Last sequence update: June 1, 2003
Last modified: May 11, 2016
This is version 108 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.