ID   ODPA_PEA                Reviewed;         397 AA.
AC   P52902;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial;
DE            Short=PDHE1-A;
DE            EC=1.2.4.1;
DE   Flags: Precursor;
OS   Pisum sativum (Garden pea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Luethy M.H., Miernyk J.A., Randall D.D.;
RL   Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC       conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple
CC       copies of three enzymatic components: pyruvate dehydrogenase (E1),
CC       dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase
CC       (E3).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue
CC         acetyltransferase] + H(+) + pyruvate = (R)-N(6)-(S(8)-
CC         acetyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue
CC         acetyltransferase] + CO2; Xref=Rhea:RHEA:19189, Rhea:RHEA-COMP:10480,
CC         Rhea:RHEA-COMP:10481, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:83099, ChEBI:CHEBI:83111; EC=1.2.4.1;
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC   -!- ACTIVITY REGULATION: E1 activity is regulated by phosphorylation
CC       (inactivation) and dephosphorylation (activation) of the alpha subunit.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Tetramer of 2 alpha and 2 beta subunits. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
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DR   EMBL; U51918; AAA97411.1; -; mRNA.
DR   PIR; T06531; T06531.
DR   AlphaFoldDB; P52902; -.
DR   SMR; P52902; -.
DR   IntAct; P52902; 1.
DR   BindingDB; P52902; -.
DR   ChEMBL; CHEMBL2366570; -.
DR   ChEMBL; CHEMBL2366571; -.
DR   PRIDE; P52902; -.
DR   BRENDA; 1.2.1.104; 4872.
DR   SABIO-RK; P52902; -.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IEA:InterPro.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR   InterPro; IPR001017; DH_E1.
DR   InterPro; IPR017597; Pyrv_DH_E1_asu_subgrp-y.
DR   InterPro; IPR029061; THDP-binding.
DR   Pfam; PF00676; E1_dh; 1.
DR   SUPFAM; SSF52518; SSF52518; 1.
DR   TIGRFAMs; TIGR03182; PDH_E1_alph_y; 1.
PE   2: Evidence at transcript level;
KW   Glycolysis; Mitochondrion; Oxidoreductase; Phosphoprotein; Pyruvate;
KW   Thiamine pyrophosphate; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..397
FT                   /note="Pyruvate dehydrogenase E1 component subunit alpha,
FT                   mitochondrial"
FT                   /id="PRO_0000020454"
SQ   SEQUENCE   397 AA;  43530 MW;  3C0257CB0032E50B CRC64;
     MALSRLSSSS SSSNGSNLFN PFSAAFTLNR PISSDTTATL TIETSLPFTA HNCDPPSRSV
     TTSPSELLSF FRTMALMRRM EIAADSLYKA NLIRGFCHLY DGQEAVAVGM EAGTTKKDCI
     ITAYRDHCTF LGRGGTLLRV YAELMGRRDG CSKGKGGSMH FYKKDSGFYG GHGIVGAQVP
     LGCGLAFGQK YLKDESVTFA LYGDGAANQG QLFEALNISA LWDLPAILVC ENNHYGMGTA
     TWRSAKSPAY FKRGDYVPGL KVDGMDALAV KQACKFAKEH ALKNGPIILE MDTYRYHGHS
     MSDPGSTYRT RDEISGVRQE RDPIERVRKL LLSHDIATEK ELKDTEKEVR KEVDEAIAKA
     KDSPMPDPSD LFSNVYVKGY GVEAFGVDRK EVRVTLP