ID   ODPA_NEOYE              Reviewed;         346 AA.
AC   Q1XDM0;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 1.
DT   25-MAY-2022, entry version 49.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit alpha;
DE            EC=1.2.4.1;
GN   Name=pdhA; Synonyms=odpA;
OS   Neopyropia yezoensis (Susabi-nori) (Pyropia yezoensis).
OG   Plastid; Chloroplast.
OC   Eukaryota; Rhodophyta; Bangiophyceae; Bangiales; Bangiaceae; Neopyropia.
OX   NCBI_TaxID=2788;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=U-51;
RA   Kunimoto M., Morishima K., Yoshikawa M., Fukuda S., Kobayashi T.,
RA   Kobayashi M., Okazaki T., Ohara I., Nakayama I.;
RT   "Whole genome sequence of Porphyra yezoensis chloroplast.";
RL   Submitted (NOV-2003) 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) (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; AP006715; BAE92391.1; -; Genomic_DNA.
DR   RefSeq; YP_536948.1; NC_007932.1.
DR   AlphaFoldDB; Q1XDM0; -.
DR   SMR; Q1XDM0; -.
DR   GeneID; 3978893; -.
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..346
FT                   /note="Pyruvate dehydrogenase E1 component subunit alpha"
FT                   /id="PRO_0000277253"
SQ   SEQUENCE   346 AA;  38637 MW;  F5562613F29D9496 CRC64;
     MSYPKKVQLP LTNYNSTGLN LNKSNLLVLY EDMLLGRNFE DMCAQMYYKG KMFGFVHLYN
     GQEAVSTGVI KLLNPTDYVC STYRDHVHAL SKGVPSKNVM AELFGKETGC SKGRGGSMHI
     FSAPHNFLGG FAFIAEGIPV ATGAAFQSIY RQQVLKETED LRVTACFFGD GTTNNGQFFE
     CLNMAVLWKL PIIFVVENNQ WAIGMAHHRS SSIPEIHKKA EAFGLPGIEV DGMDVLAVRQ
     AAKQAVQRAR QGDGPTLIEA LTYRFRGHSL ADPDELRSRQ EKEAWVARDP IKKLKKYILD
     NEIANIGELN EIQNAVKTEL EQAVKFAISS PEPNMSELKR YLFADN