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 27-MAR-2024, entry version 123.
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=H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[dihydrolipoyllysine-residue
CC acetyltransferase] + pyruvate = CO2 + N(6)-[(R)-S(8)-
CC acetyldihydrolipoyl]-L-lysyl-[dihydrolipoyllysine-residue
CC acetyltransferase]; 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; 39947.Q654V6; -.
DR PaxDb; 39947-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; WGGSMHM; -.
DR OrthoDB; 166915at2759; -.
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 CDD; cd02000; TPP_E1_PDC_ADC_BCADC; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR InterPro; IPR001017; DH_E1.
DR InterPro; IPR017597; Pyrv_DH_E1_asu_subgrp-y.
DR InterPro; IPR029061; THDP-binding.
DR NCBIfam; TIGR03182; PDH_E1_alph_y; 1.
DR PANTHER; PTHR11516:SF38; PYRUVATE DEHYDROGENASE E1 COMPONENT SUBUNIT ALPHA-2, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11516; PYRUVATE DEHYDROGENASE E1 COMPONENT, ALPHA SUBUNIT BACTERIAL AND ORGANELLAR; 1.
DR Pfam; PF00676; E1_dh; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
PE 2: Evidence at transcript level;
KW 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
//
