ODPB3_ORYSJ
ID ODPB3_ORYSJ Reviewed; 391 AA.
AC Q2QM55; A0A0P0YCA2;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit beta-3, chloroplastic;
DE EC=1.2.4.1;
DE Flags: Precursor;
GN OrderedLocusNames=Os12g0616900, LOC_Os12g42230;
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=16188032; DOI=10.1186/1741-7007-3-20;
RG The rice chromosomes 11 and 12 sequencing consortia;
RT "The sequence of rice chromosomes 11 and 12, rich in disease resistance
RT genes and recent gene duplications.";
RL BMC Biol. 3:20-20(2005).
RN [2]
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 [3]
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 [4]
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 [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: Plastid, chloroplast {ECO:0000305}.
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DR EMBL; DP000011; ABA99864.1; -; Genomic_DNA.
DR EMBL; AP008218; BAF30304.1; -; Genomic_DNA.
DR EMBL; AP014968; BAT18104.1; -; Genomic_DNA.
DR EMBL; AK063753; BAG88853.1; -; mRNA.
DR EMBL; AK101464; BAG95077.1; -; mRNA.
DR RefSeq; XP_015620613.1; XM_015765127.1.
DR AlphaFoldDB; Q2QM55; -.
DR SMR; Q2QM55; -.
DR STRING; 4530.OS12T0616900-01; -.
DR PaxDb; Q2QM55; -.
DR PRIDE; Q2QM55; -.
DR EnsemblPlants; Os12t0616900-01; Os12t0616900-01; Os12g0616900.
DR GeneID; 4352803; -.
DR Gramene; Os12t0616900-01; Os12t0616900-01; Os12g0616900.
DR KEGG; osa:4352803; -.
DR eggNOG; KOG0524; Eukaryota.
DR HOGENOM; CLU_012907_1_1_1; -.
DR InParanoid; Q2QM55; -.
DR OMA; VFFEHVL; -.
DR OrthoDB; 875272at2759; -.
DR Proteomes; UP000000763; Chromosome 12.
DR Proteomes; UP000059680; Chromosome 12.
DR Genevisible; Q2QM55; OS.
DR GO; GO:0009507; C:chloroplast; 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 Gene3D; 3.40.50.920; -; 1.
DR InterPro; IPR027110; PDHB.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR InterPro; IPR033248; Transketolase_C.
DR PANTHER; PTHR11624; PTHR11624; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR Pfam; PF02780; Transketolase_C; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52518; SSF52518; 1.
DR SUPFAM; SSF52922; SSF52922; 1.
PE 2: Evidence at transcript level;
KW Chloroplast; Glycolysis; Oxidoreductase; Plastid; Pyruvate;
KW Reference proteome; Thiamine pyrophosphate; Transit peptide.
FT TRANSIT 1..35
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 36..391
FT /note="Pyruvate dehydrogenase E1 component subunit beta-3,
FT chloroplastic"
FT /id="PRO_0000421375"
FT BINDING 127
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
SQ SEQUENCE 391 AA; 42121 MW; 9ACC7CC81A9D3853 CRC64;
MATAAAASLQ YALHGAASAS AKPRSAAPGR SVRVVAARRS VRARGGAVVA RAAVTASADA
TAESKSGGHE VLLFEALREA LIEEMKEDPT VCVFGEDVGH YGGSYKVTKG LAEMFGDLRV
LDTPIAENSF AGMGVGAAMK GLRPIVEGMN MGFLLLAYNQ ISNNCGMLHY TSGGQFKIPI
VIRGPGGVGR QLGAEHSQRL ESYFQSIPGL QMVACSTPYN AKGLMKAAIR SENPVVLFEH
VLLYNLKEKI PDEEYICCLE EAEMVRPGEH VTILTYSRMR YHVMQAAKTL VNKGYDPEVI
DIRSLKPFDL HTIGNSIKKT HRVLIVEECM RTGGIGASLR SAIIDNFWDY LDAPIMCLSS
QDVPTPYAAT LEDATVVQPA QIVAAVEQIC Q
