ID   ODPB2_ORYSJ             Reviewed;         376 AA.
AC   Q0J0H4; A0A0P0XPJ5;
DT   06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit beta-2, mitochondrial;
DE            Short=PDHE1-B;
DE            EC=1.2.4.1;
DE   Flags: Precursor;
GN   OrderedLocusNames=Os09g0509200, LOC_Os09g33500; ORFNames=OsJ_29962;
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; AP008215; BAF25541.1; -; Genomic_DNA.
DR   EMBL; AP014965; BAT08892.1; -; Genomic_DNA.
DR   EMBL; CM000146; EEE70023.1; -; Genomic_DNA.
DR   EMBL; AK069525; BAG91472.1; -; mRNA.
DR   RefSeq; XP_015612322.1; XM_015756836.1.
DR   AlphaFoldDB; Q0J0H4; -.
DR   SMR; Q0J0H4; -.
DR   STRING; 4530.OS09T0509200-01; -.
DR   PaxDb; Q0J0H4; -.
DR   PRIDE; Q0J0H4; -.
DR   EnsemblPlants; Os09t0509200-01; Os09t0509200-01; Os09g0509200.
DR   GeneID; 4347531; -.
DR   Gramene; Os09t0509200-01; Os09t0509200-01; Os09g0509200.
DR   KEGG; osa:4347531; -.
DR   eggNOG; KOG0524; Eukaryota.
DR   InParanoid; Q0J0H4; -.
DR   OMA; LPLDTCF; -.
DR   OrthoDB; 875272at2759; -.
DR   Proteomes; UP000000763; Chromosome 9.
DR   Proteomes; UP000007752; Chromosome 9.
DR   Proteomes; UP000059680; Chromosome 9.
DR   ExpressionAtlas; Q0J0H4; baseline and differential.
DR   Genevisible; Q0J0H4; OS.
DR   GO; GO:0005967; C:mitochondrial pyruvate dehydrogenase complex; IBA:GO_Central.
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   Glycolysis; Mitochondrion; Oxidoreductase; Pyruvate; Reference proteome;
KW   Thiamine pyrophosphate; Transit peptide.
FT   TRANSIT         1..36
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           37..376
FT                   /note="Pyruvate dehydrogenase E1 component subunit beta-2,
FT                   mitochondrial"
FT                   /id="PRO_0000421374"
FT   BINDING         99
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   376 AA;  40251 MW;  53CF7C6FB2189741 CRC64;
     MLGAARRQLG SGPMLGQVLR RLRPATAAAA DAARAYSAAA KEMTVREALN SALDEEMSAD
     PSVFLMGEEV GEYQGAYKIS KGLLDKYGPE RVLDTPITEA GFTGIAVGAA YQGLRPVVEF
     MTFNFSMQAI DHIINSAAKS NYMSAGQISV PIVFRGPNGA AAGVGAQHSQ CYAAWYAHVP
     GLKVLVPYSA EDARGLLKAA IRDPDPVVFL ENELLYGESF PISAEVLDSS FALPIGKAKI
     EREGKDVTIT AYSKMVGYAL QAADILSKEG ISAEVINLRS IRPLDRATIN ASVRKTNRLV
     TIEESFPQHG IGAEICMSVV EESFEYLDAP VERIAGADVP MPYAANLERM AVPQVDDIVR
     AAKRACYRAV PMAATA