ODPB2_ARATH
ID ODPB2_ARATH Reviewed; 406 AA.
AC Q9C6Z3; O24458;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit beta-2, chloroplastic;
DE EC=1.2.4.1;
DE Flags: Precursor;
GN Name=PDH-E1 BETA; Synonyms=E1-BETA-1; OrderedLocusNames=At1g30120;
GN ORFNames=T2H7.8;
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].
RC STRAIN=cv. Columbia;
RX PubMed=9393637; DOI=10.1016/s0005-2728(97)00059-5;
RA Johnston M.L., Luethy M.H., Miernyk J.A., Randall D.D.;
RT "Cloning and molecular analyses of the Arabidopsis thaliana plastid
RT pyruvate dehydrogenase subunits.";
RL Biochim. Biophys. Acta 1321:200-206(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 Q9C6Z3; Q9LYC1: GID1B; NbExp=3; IntAct=EBI-4436231, EBI-963686;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
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DR EMBL; U80186; AAB86804.1; -; mRNA.
DR EMBL; AC074176; AAG50862.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31181.1; -; Genomic_DNA.
DR EMBL; AF361583; AAK32751.1; -; mRNA.
DR EMBL; AY093988; AAM16249.1; -; mRNA.
DR EMBL; AK221898; BAD94262.1; -; mRNA.
DR EMBL; AY087733; AAM65270.1; -; mRNA.
DR PIR; C86425; C86425.
DR RefSeq; NP_174304.1; NM_102751.5.
DR AlphaFoldDB; Q9C6Z3; -.
DR SMR; Q9C6Z3; -.
DR BioGRID; 25126; 20.
DR IntAct; Q9C6Z3; 9.
DR STRING; 3702.AT1G30120.1; -.
DR PaxDb; Q9C6Z3; -.
DR PRIDE; Q9C6Z3; -.
DR ProteomicsDB; 238918; -.
DR EnsemblPlants; AT1G30120.1; AT1G30120.1; AT1G30120.
DR GeneID; 839891; -.
DR Gramene; AT1G30120.1; AT1G30120.1; AT1G30120.
DR KEGG; ath:AT1G30120; -.
DR Araport; AT1G30120; -.
DR TAIR; locus:2202476; AT1G30120.
DR eggNOG; KOG0524; Eukaryota.
DR HOGENOM; CLU_012907_1_1_1; -.
DR InParanoid; Q9C6Z3; -.
DR OMA; PCLFVET; -.
DR OrthoDB; 875272at2759; -.
DR PhylomeDB; Q9C6Z3; -.
DR BioCyc; ARA:AT1G30120-MON; -.
DR PRO; PR:Q9C6Z3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C6Z3; baseline and differential.
DR Genevisible; Q9C6Z3; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0010240; C:plastid pyruvate dehydrogenase complex; TAS: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:0006633; P:fatty acid biosynthetic process; TAS:TAIR.
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 Chloroplast; Glycolysis; Oxidoreductase; Plastid; Pyruvate;
KW Reference proteome; Thiamine pyrophosphate; Transit peptide.
FT TRANSIT 1..44
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 45..406
FT /note="Pyruvate dehydrogenase E1 component subunit beta-2,
FT chloroplastic"
FT /id="PRO_0000421371"
FT BINDING 142
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT CONFLICT 271
FT /note="V -> I (in Ref. 1; AAM65270 and 6; AAB86804)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 406 AA; 44245 MW; 6C9F31F3D4290513 CRC64;
MSSIIHGAGA ATTTLSTFNS VDSKKLFVAP SRTNLSVRSQ RYIVAGSDAS KKSFGSGLRV
RHSQKLIPNA VATKEADTSA STGHELLLFE ALQEGLEEEM DRDPHVCVMG EDVGHYGGSY
KVTKGLADKF GDLRVLDTPI CENAFTGMGI GAAMTGLRPV IEGMNMGFLL LAFNQISNNC
GMLHYTSGGQ FTIPVVIRGP GGVGRQLGAE HSQRLESYFQ SIPGIQMVAC STPYNAKGLM
KAAIRSENPV ILFEHVLLYN LKEKIPDEDY VCNLEEAEMV RPGEHITILT YSRMRYHVMQ
AAKTLVNKGY DPEVIDIRSL KPFDLHTIGN SVKKTHRVLI VEECMRTGGI GASLTAAINE
NFHDYLDAPV MCLSSQDVPT PYAGTLEEWT VVQPAQIVTA VEQLCQ
