ID   ODPA1_ORYSJ             Reviewed;         390 AA.
AC   Q6Z5N4; A0A0P0VP76;
DT   06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit alpha-1, mitochondrial;
DE            Short=PDHE1-A;
DE            EC=1.2.4.1;
DE   Flags: Precursor;
GN   OrderedLocusNames=Os02g0739600, LOC_Os02g50620;
GN   ORFNames=OsJ_08320, P0684F11.25;
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 GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
RN   [5]
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; AP005112; BAD16048.1; -; Genomic_DNA.
DR   EMBL; AP008208; BAF09982.1; -; Genomic_DNA.
DR   EMBL; AP014958; BAS80837.1; -; Genomic_DNA.
DR   EMBL; CM000139; EAZ24558.1; -; Genomic_DNA.
DR   EMBL; AK098950; BAG93828.1; -; mRNA.
DR   RefSeq; XP_015626335.1; XM_015770849.1.
DR   AlphaFoldDB; Q6Z5N4; -.
DR   SMR; Q6Z5N4; -.
DR   STRING; 4530.OS02T0739600-01; -.
DR   iPTMnet; Q6Z5N4; -.
DR   PaxDb; Q6Z5N4; -.
DR   PRIDE; Q6Z5N4; -.
DR   EnsemblPlants; Os02t0739600-01; Os02t0739600-01; Os02g0739600.
DR   GeneID; 4330673; -.
DR   Gramene; Os02t0739600-01; Os02t0739600-01; Os02g0739600.
DR   KEGG; osa:4330673; -.
DR   eggNOG; KOG0225; Eukaryota.
DR   HOGENOM; CLU_029393_5_2_1; -.
DR   InParanoid; Q6Z5N4; -.
DR   OMA; EFAIKHA; -.
DR   OrthoDB; 871160at2759; -.
DR   Proteomes; UP000000763; Chromosome 2.
DR   Proteomes; UP000007752; Chromosome 2.
DR   Proteomes; UP000059680; Chromosome 2.
DR   Genevisible; Q6Z5N4; 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..15
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           16..390
FT                   /note="Pyruvate dehydrogenase E1 component subunit alpha-1,
FT                   mitochondrial"
FT                   /id="PRO_0000421368"
FT   REGION          293..312
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   390 AA;  42702 MW;  113810FFCD093CDD CRC64;
     MAAAILLRRV PPARAQATAL IAARSISDST APLTIETSVP FTSHIVDPPS RDVTTTPAEL
     LTFFRDMSVM RRMEIAADSL YKAKLIRGFC HLYDGQEAVA VGMEAAITRS DSIITAYRDH
     CTYLARGGDL VSAFAELMGR QAGCSRGKGG SMHFYKKDAN FYGGHGIVGA QVPLGCGLAF
     AQKYRKEETA TFALYGDGAA NQGQLFEALN ISALWKLPAI LVCENNHYGM GTAEWRAAKS
     PAYYKRGDYV PGLKVDGMDV LAVKQACKFA KEHAIANGPI VLEMDTYRYH GHSMSDPGST
     YRTRDEISGV RQERDPIERV RKLILAHDLA TAAELKDMEK EIRKEVDDAI AKAKESPMPD
     TSELFTNVYV KGFGVESFGA DRKELRATLP