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P52902

- ODPA_PEA

UniProt

P52902 - ODPA_PEA

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Protein

Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial

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

Thiamine pyrophosphate.

Enzyme regulationi

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

GO - Molecular functioni

  1. pyruvate dehydrogenase (acetyl-transferring) activity Source: UniProtKB-EC

GO - Biological processi

  1. glycolytic process Source: UniProtKB-KW
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

  1. mitochondrion Source: UniProtKB-KW
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

Proteomic databases

ProMEXiP52902.

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:
EMBL
GenBank
DDBJ
Links Updated
U51918 mRNA. Translation: AAA97411.1.
PIRiT06531.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U51918 mRNA. Translation: AAA97411.1 .
PIRi T06531.

3D structure databases

ProteinModelPortali P52902.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P52902. 1 interaction.

Chemistry

ChEMBLi CHEMBL2366571.

Proteomic databases

ProMEXi P52902.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 3.40.50.970. 1 hit.
InterProi IPR001017. DH_E1.
IPR017597. Pyrv_DH_E1_asu_subgrp-y.
IPR029061. THDP-binding.
[Graphical view ]
Pfami PF00676. E1_dh. 1 hit.
[Graphical view ]
SUPFAMi SSF52518. SSF52518. 1 hit.
TIGRFAMsi TIGR03182. PDH_E1_alph_y. 1 hit.
ProtoNeti Search...

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: October 29, 2014
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program