ID   ODPA_PORPU              Reviewed;         344 AA.
AC   P51267;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit alpha;
DE            EC=1.2.4.1;
GN   Name=pdhA; Synonyms=odpA;
OS   Porphyra purpurea (Red seaweed) (Ulva purpurea).
OG   Plastid; Chloroplast.
OC   Eukaryota; Rhodophyta; Bangiophyceae; Bangiales; Bangiaceae; Porphyra.
OX   NCBI_TaxID=2787;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Avonport;
RA   Reith M.E., Munholland J.;
RT   "Complete nucleotide sequence of the Porphyra purpurea chloroplast
RT   genome.";
RL   Plant Mol. Biol. Rep. 13:333-335(1995).
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) (By similarity). {ECO:0000250}.
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   -!- SUBUNIT: Heterodimer of an alpha and a beta chain. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
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DR   EMBL; U38804; AAC08153.1; -; Genomic_DNA.
DR   PIR; S73188; S73188.
DR   RefSeq; NP_053877.1; NC_000925.1.
DR   AlphaFoldDB; P51267; -.
DR   SMR; P51267; -.
DR   GeneID; 809896; -.
DR   GO; GO:0009507; C:chloroplast; 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   3: Inferred from homology;
KW   Chloroplast; Glycolysis; Oxidoreductase; Plastid; Pyruvate;
KW   Thiamine pyrophosphate.
FT   CHAIN           1..344
FT                   /note="Pyruvate dehydrogenase E1 component subunit alpha"
FT                   /id="PRO_0000162215"
SQ   SEQUENCE   344 AA;  38507 MW;  799BD9AFA06FF455 CRC64;
     MSYPKKVELP LTNCNQINLT KHKLLVLYED MLLGRNFEDM CAQMYYKGKM FGFVHLYNGQ
     EAVSTGVIKL LDSKDYVCST YRDHVHALSK GVPSQNVMAE LFGKETGCSR GRGGSMHIFS
     APHNFLGGFA FIAEGIPVAT GAAFQSIYRQ QVLKEPGELR VTACFFGDGT TNNGQFFECL
     NMAVLWKLPI IFVVENNQWA IGMAHHRSSS IPEIHKKAEA FGLPGIEVDG MDVLAVRQVA
     EKAVERARQG QGPTLIEALT YRFRGHSLAD PDELRSRQEK EAWVARDPIK KLKKHILDNQ
     IASSDELNDI QSSVKIDLEQ SVEFAMSSPE PNISELKRYL FADN