ODPB3_ARATH
ID ODPB3_ARATH Reviewed; 406 AA.
AC O64688; Q8LAI3;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit beta-3, chloroplastic;
DE EC=1.2.4.1;
DE Flags: Precursor;
GN Name=E1-BETA-2; OrderedLocusNames=At2g34590; ORFNames=T31E10.7;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Behal R.H., Oliver D.J.;
RT "A second gene encoding the plastidic pyruvate dehydrogenase beta subunit
RT in Arabidopsis thaliana.";
RL (er) Plant Gene Register PGR99-136(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Kim C.J., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
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 -!- INTERACTION:
CC O64688; Q9LYC1: GID1B; NbExp=3; IntAct=EBI-25520038, EBI-963686;
CC O64688; Q84MB2: TIFY8; NbExp=3; IntAct=EBI-25520038, EBI-4426557;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
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DR EMBL; AF167983; AAD47282.1; -; mRNA.
DR EMBL; AC004077; AAC26685.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08996.1; -; Genomic_DNA.
DR EMBL; BT025968; ABG25057.1; -; mRNA.
DR EMBL; AY087792; AAM65328.1; -; mRNA.
DR PIR; E84758; E84758.
DR RefSeq; NP_181006.1; NM_129013.3.
DR AlphaFoldDB; O64688; -.
DR SMR; O64688; -.
DR BioGRID; 3370; 17.
DR IntAct; O64688; 2.
DR STRING; 3702.AT2G34590.1; -.
DR PaxDb; O64688; -.
DR PRIDE; O64688; -.
DR ProteomicsDB; 250792; -.
DR EnsemblPlants; AT2G34590.1; AT2G34590.1; AT2G34590.
DR GeneID; 818024; -.
DR Gramene; AT2G34590.1; AT2G34590.1; AT2G34590.
DR KEGG; ath:AT2G34590; -.
DR Araport; AT2G34590; -.
DR TAIR; locus:2062351; AT2G34590.
DR eggNOG; KOG0524; Eukaryota.
DR HOGENOM; CLU_012907_1_1_1; -.
DR InParanoid; O64688; -.
DR OMA; PYSLFAH; -.
DR OrthoDB; 875272at2759; -.
DR PhylomeDB; O64688; -.
DR BioCyc; ARA:AT2G34590-MON; -.
DR PRO; PR:O64688; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O64688; baseline and differential.
DR Genevisible; O64688; AT.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; HDA:TAIR.
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 GO; GO:0048868; P:pollen tube development; IMP:TAIR.
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 1: Evidence at protein level;
KW Chloroplast; Glycolysis; Oxidoreductase; Plastid; Pyruvate;
KW Reference proteome; Thiamine pyrophosphate; Transit peptide.
FT TRANSIT 1..70
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 71..406
FT /note="Pyruvate dehydrogenase E1 component subunit beta-3,
FT chloroplastic"
FT /id="PRO_0000421372"
FT BINDING 142
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT CONFLICT 108
FT /note="V -> A (in Ref. 5; AAM65328)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 406 AA; 44015 MW; 1F17DB5B4CB3D453 CRC64;
MSAILQGAGA ATALSPFNSI DSNKLVAPSR SSLSVRSKRY IVAGSDSKSF GSSLVARRSE
PLIPNAVTTK ADTAASSTSS KPGHELLLFE ALQEGLEEEM DRDPHVCVMG EDVGHYGGSY
KVTKGLADKF GDLRVLDTPI CENAFTGMGI GAAMTGLRPV IEGMNMGFLL LAFNQISNNC
GMLHYTSGGQ FTIPVVIRGP GGVGRQLGAE HSQRLESYFQ SIPGIQMVAC STPYNAKGLM
KAAIRSENPV ILFEHVLLYN LKESIPDEEY ICNLEEAEMV RPGEHITILT YSRMRYHVMQ
AAKTLVNKGY DPEVIDIRSL KPFDLYTIGN SVKKTHRVLI VEECMRTGGI GASLTAAINE
NFHDYLDAPV MCLSSQDVPT PYAGTLEEWT VVQPAQIVTA VEQLCQ
