ID   ODPA_PORYE              Reviewed;         346 AA.
AC   Q1XDM0;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 1.
DT   16-JUN-2009, entry version 19.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit alpha;
DE            EC=1.2.4.1;
GN   Name=pdhA; Synonyms=odpA;
OS   Porphyra yezoensis.
OG   Plastid; Chloroplast.
OC   Eukaryota; Rhodophyta; Bangiophyceae; Bangiales; Bangiaceae; Porphyra.
OX   NCBI_TaxID=2788;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=U-51; TISSUE=Gametophyte;
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
CC       multiple copies of three enzymatic components: pyruvate
CC       dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and
CC       lipoamide dehydrogenase (E3) (By similarity).
CC   -!- CATALYTIC ACTIVITY: Pyruvate + [dihydrolipoyllysine-residue
CC       acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue
CC       acetyltransferase] S-acetyldihydrolipoyllysine + CO(2).
CC   -!- COFACTOR: Thiamine pyrophosphate.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta chain (By similarity).
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AP006715; BAE92391.1; -; Genomic_DNA.
DR   RefSeq; YP_536948.1; -.
DR   GeneID; 3978893; -.
DR   BRENDA; 1.2.4.1; 257472.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring...; IEA:EC.
DR   GO; GO:0006096; P:glycolysis; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR001017; DH_E1.
DR   InterPro; IPR017597; Pyrv_DH_E1_asu_subgrp-y.
DR   Pfam; PF00676; E1_dh; 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       Pyruvate dehydrogenase E1 component
FT                                subunit alpha.
FT                                /FTId=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
//