ID   ODPA2_ORYSJ             Reviewed;         398 AA.
AC   Q654V6; A0A0P0WUL5;
DT   06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit alpha-2, mitochondrial;
DE            Short=PDHE1-A;
DE            EC=1.2.4.1;
DE   Flags: Precursor;
GN   OrderedLocusNames=Os06g0246500, LOC_Os06g13720; ORFNames=OJ1136_C11.8;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
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         Evidence={ECO:0000250};
CC   -!- SUBUNIT: Tetramer of 2 alpha and 2 beta subunits. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
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DR   EMBL; AP004027; BAD45661.1; -; Genomic_DNA.
DR   EMBL; AP008212; BAF19195.1; -; Genomic_DNA.
DR   EMBL; AP014962; BAS97030.1; -; Genomic_DNA.
DR   EMBL; AK105105; BAG97096.1; -; mRNA.
DR   RefSeq; XP_015641790.1; XM_015786304.1.
DR   AlphaFoldDB; Q654V6; -.
DR   SMR; Q654V6; -.
DR   STRING; 4530.OS06T0246500-01; -.
DR   PaxDb; Q654V6; -.
DR   PRIDE; Q654V6; -.
DR   EnsemblPlants; Os06t0246500-01; Os06t0246500-01; Os06g0246500.
DR   GeneID; 4340640; -.
DR   Gramene; Os06t0246500-01; Os06t0246500-01; Os06g0246500.
DR   KEGG; osa:4340640; -.
DR   eggNOG; KOG0225; Eukaryota.
DR   HOGENOM; CLU_029393_5_2_1; -.
DR   InParanoid; Q654V6; -.
DR   OMA; YRSHGFT; -.
DR   OrthoDB; 871160at2759; -.
DR   Proteomes; UP000000763; Chromosome 6.
DR   Proteomes; UP000059680; Chromosome 6.
DR   Genevisible; Q654V6; OS.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IBA:GO_Central.
DR   GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IBA:GO_Central.
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   Reference proteome; Thiamine pyrophosphate; Transit peptide.
FT   TRANSIT         1..33
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           34..398
FT                   /note="Pyruvate dehydrogenase E1 component subunit alpha-2,
FT                   mitochondrial"
FT                   /id="PRO_0000421369"
SQ   SEQUENCE   398 AA;  43655 MW;  83B60E18C192DCEE CRC64;
     MAAAVVLLRR LRGVTAAPRR AAAALPLTTS VRGVSDSTEP LTIETSVPYK SHIVDPPPRE
     VATTARELAT FFRDMSAMRR AEIAADSLYK AKLIRGFCHL YDGQEAVAVG MEAATTRADA
     IITAYRDHCA YLARGGDLAA LFAELMGRRG GCSRGKGGSM HLYKKDANFY GGHGIVGAQV
     PLGCGLAFAQ RYRKEAAVTF DLYGDGAANQ GQLFEALNMA ALWKLPVVLV CENNHYGMGT
     AEWRASKSPA YYKRGDYVPG LKVDGMDVLA VKQACKFAKQ HALENGPIIL EMDTYRYHGH
     SMSDPGSTYR TRDEIAGIRQ ERDPIERVRK LLLAHDFATT QELKDMEKEI RKQVDTAIAK
     AKESPMPDPS ELFTNVYVND CGLESFGVDR KVVRTVLP