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Protein

Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial

Gene
N/A
Organism
Pisum sativum (Garden pea)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2. It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).

Catalytic activityi

Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2.

Cofactori

Enzyme regulationi

E1 activity is regulated by phosphorylation (inactivation) and dephosphorylation (activation) of the alpha subunit.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Pyruvate, Thiamine pyrophosphate

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial (EC:1.2.4.1)
Short name:
PDHE1-A
OrganismiPisum sativum (Garden pea)
Taxonomic identifieri3888 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeFabeaePisum

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 397Pyruvate dehydrogenase E1 component subunit alpha, mitochondrialPRO_0000020454
Transit peptidei1 – ?MitochondrionSequence Analysis

Keywords - PTMi

Phosphoprotein

Interactioni

Subunit structurei

Tetramer of 2 alpha and 2 beta subunits.By similarity

Protein-protein interaction databases

IntActiP52902. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliP52902.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Keywords - Domaini

Transit peptide

Family and domain databases

Gene3Di3.40.50.970. 1 hit.
InterProiIPR001017. DH_E1.
IPR017597. Pyrv_DH_E1_asu_subgrp-y.
IPR029061. THDP-binding.
[Graphical view]
PfamiPF00676. E1_dh. 1 hit.
[Graphical view]
SUPFAMiSSF52518. SSF52518. 1 hit.
TIGRFAMsiTIGR03182. PDH_E1_alph_y. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P52902-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALSRLSSSS SSSNGSNLFN PFSAAFTLNR PISSDTTATL TIETSLPFTA
60 70 80 90 100
HNCDPPSRSV TTSPSELLSF FRTMALMRRM EIAADSLYKA NLIRGFCHLY
110 120 130 140 150
DGQEAVAVGM EAGTTKKDCI ITAYRDHCTF LGRGGTLLRV YAELMGRRDG
160 170 180 190 200
CSKGKGGSMH FYKKDSGFYG GHGIVGAQVP LGCGLAFGQK YLKDESVTFA
210 220 230 240 250
LYGDGAANQG QLFEALNISA LWDLPAILVC ENNHYGMGTA TWRSAKSPAY
260 270 280 290 300
FKRGDYVPGL KVDGMDALAV KQACKFAKEH ALKNGPIILE MDTYRYHGHS
310 320 330 340 350
MSDPGSTYRT RDEISGVRQE RDPIERVRKL LLSHDIATEK ELKDTEKEVR
360 370 380 390
KEVDEAIAKA KDSPMPDPSD LFSNVYVKGY GVEAFGVDRK EVRVTLP
Length:397
Mass (Da):43,530
Last modified:October 1, 1996 - v1
Checksum:i3C0257CB0032E50B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U51918 mRNA. Translation: AAA97411.1.
PIRiT06531.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U51918 mRNA. Translation: AAA97411.1.
PIRiT06531.

3D structure databases

ProteinModelPortaliP52902.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP52902. 1 interaction.

Chemistry

ChEMBLiCHEMBL2366571.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di3.40.50.970. 1 hit.
InterProiIPR001017. DH_E1.
IPR017597. Pyrv_DH_E1_asu_subgrp-y.
IPR029061. THDP-binding.
[Graphical view]
PfamiPF00676. E1_dh. 1 hit.
[Graphical view]
SUPFAMiSSF52518. SSF52518. 1 hit.
TIGRFAMsiTIGR03182. PDH_E1_alph_y. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. Luethy M.H., Miernyk J.A., Randall D.D.
    Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiODPA_PEA
AccessioniPrimary (citable) accession number: P52902
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: January 7, 2015
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

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 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.