ODPB1_ARATH
ID ODPB1_ARATH Reviewed; 363 AA.
AC Q38799; Q9LSM8;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 06-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit beta-1, mitochondrial;
DE Short=PDHE1-B;
DE EC=1.2.4.1;
DE AltName: Full=Protein MACCI-BOU;
DE Flags: Precursor;
GN Name=PDH2; Synonyms=MAB1; OrderedLocusNames=At5g50850; ORFNames=K16E14.1;
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], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=8061040; DOI=10.1016/0005-2728(94)90171-6;
RA Luethy M.H., Miernyk J.A., Randall D.D.;
RT "The nucleotide and deduced amino acid sequences of a cDNA encoding the E1
RT beta-subunit of the Arabidopsis thaliana mitochondrial pyruvate
RT dehydrogenase complex.";
RL Biochim. Biophys. Acta 1187:95-98(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
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;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=14671022; DOI=10.1105/tpc.016055;
RA Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J.,
RA Millar A.H.;
RT "Experimental analysis of the Arabidopsis mitochondrial proteome highlights
RT signaling and regulatory components, provides assessment of targeting
RT prediction programs, and indicates plant-specific mitochondrial proteins.";
RL Plant Cell 16:241-256(2004).
RN [6]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-247 AND LYS-254, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND CLEAVAGE OF TRANSIT PEPTIDE AFTER
RP TYR-29.
RX PubMed=25732537; DOI=10.1093/jxb/erv064;
RA Carrie C., Venne A.S., Zahedi R.P., Soll J.;
RT "Identification of cleavage sites and substrate proteins for two
RT mitochondrial intermediate peptidases in Arabidopsis thaliana.";
RL J. Exp. Bot. 66:2691-2708(2015).
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).
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 -!- SUBUNIT: Tetramer of 2 alpha and 2 beta subunits. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:14671022, ECO:0000305|PubMed:25732537}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, immature rosettes, and mature
CC rosettes. {ECO:0000269|PubMed:8061040}.
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DR EMBL; U09137; AAA52225.1; -; mRNA.
DR EMBL; AB026637; BAA98121.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96001.1; -; Genomic_DNA.
DR EMBL; AY070728; AAL50070.1; -; mRNA.
DR EMBL; BT000839; AAN38676.1; -; mRNA.
DR RefSeq; NP_199898.1; NM_124463.4.
DR AlphaFoldDB; Q38799; -.
DR SMR; Q38799; -.
DR BioGRID; 20403; 5.
DR IntAct; Q38799; 2.
DR STRING; 3702.AT5G50850.1; -.
DR iPTMnet; Q38799; -.
DR MetOSite; Q38799; -.
DR SWISS-2DPAGE; Q38799; -.
DR PaxDb; Q38799; -.
DR PRIDE; Q38799; -.
DR ProteomicsDB; 238917; -.
DR EnsemblPlants; AT5G50850.1; AT5G50850.1; AT5G50850.
DR GeneID; 835157; -.
DR Gramene; AT5G50850.1; AT5G50850.1; AT5G50850.
DR KEGG; ath:AT5G50850; -.
DR Araport; AT5G50850; -.
DR TAIR; locus:2152745; AT5G50850.
DR eggNOG; KOG0524; Eukaryota.
DR HOGENOM; CLU_012907_1_1_1; -.
DR InParanoid; Q38799; -.
DR OMA; YRGYRPV; -.
DR OrthoDB; 875272at2759; -.
DR PhylomeDB; Q38799; -.
DR BioCyc; ARA:AT5G50850-MON; -.
DR PRO; PR:Q38799; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q38799; baseline and differential.
DR Genevisible; Q38799; AT.
DR GO; GO:0005967; C:mitochondrial pyruvate dehydrogenase complex; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0005730; C:nucleolus; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
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 1: Evidence at protein level;
KW Glycolysis; Isopeptide bond; Mitochondrion; Oxidoreductase; Pyruvate;
KW Reference proteome; Thiamine pyrophosphate; Transit peptide;
KW Ubl conjugation.
FT TRANSIT 1..29
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:25732537"
FT CHAIN 30..363
FT /note="Pyruvate dehydrogenase E1 component subunit beta-1,
FT mitochondrial"
FT /id="PRO_0000020462"
FT BINDING 92
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT CROSSLNK 247
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:17272265"
FT CROSSLNK 254
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:17272265"
FT CONFLICT 334
FT /note="M -> I (in Ref. 1; AAA52225)"
FT /evidence="ECO:0000305"
FT CONFLICT 337
FT /note="A -> T (in Ref. 1; AAA52225)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 363 AA; 39176 MW; D044E3A336D4EC52 CRC64;
MLGILRQRAI DGASTLRRTR FALVSARSYA AGAKEMTVRD ALNSAIDEEM SADPKVFVMG
EEVGQYQGAY KITKGLLEKY GPERVYDTPI TEAGFTGIGV GAAYAGLKPV VEFMTFNFSM
QAIDHIINSA AKSNYMSAGQ INVPIVFRGP NGAAAGVGAQ HSQCYAAWYA SVPGLKVLAP
YSAEDARGLL KAAIRDPDPV VFLENELLYG ESFPISEEAL DSSFCLPIGK AKIEREGKDV
TIVTFSKMVG FALKAAEKLA EEGISAEVIN LRSIRPLDRA TINASVRKTS RLVTVEEGFP
QHGVCAEICA SVVEESFSYL DAPVERIAGA DVPMPYAANL ERLALPQIED IVRASKRACY
RSK
