ID ODBB2_ARATH Reviewed; 358 AA.
AC Q9LDY2;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 27-MAR-2024, entry version 136.
DE RecName: Full=2-oxoisovalerate dehydrogenase subunit beta 2, mitochondrial;
DE EC=1.2.4.4 {ECO:0000250|UniProtKB:P21953};
DE AltName: Full=Branched-chain alpha-keto acid dehydrogenase E1 component beta chain;
DE Short=BCKDE1B;
DE Short=BCKDH E1-beta;
DE AltName: Full=Protein DARK INDUCIBLE 4;
DE Flags: Precursor;
GN Name=DIN4; OrderedLocusNames=At3g13450; ORFNames=MRP15.11;
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], INDUCTION BY DARK AND SUCROSE, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=10681595; DOI=10.1074/jbc.275.8.6007;
RA Fujiki Y., Sato T., Ito M., Watanabe A.;
RT "Isolation and characterization of cDNA clones for the E1beta and E2
RT subunits of the branched-chain alpha-ketoacid dehydrogenase complex in
RT Arabidopsis.";
RL J. Biol. Chem. 275:6007-6013(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(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;
RA Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP INDUCTION BY SUGAR, AND FUNCTION.
RX PubMed=11080291; DOI=10.1104/pp.124.3.1139;
RA Fujiki Y., Ito M., Nishida I., Watanabe A.;
RT "Multiple signaling pathways in gene expression during sugar starvation.
RT Pharmacological analysis of din gene expression in suspension-cultured
RT cells of Arabidopsis.";
RL Plant Physiol. 124:1139-1148(2000).
RN [7]
RP INDUCTION BY LEUCINE AND KIC.
RX PubMed=11418132; DOI=10.1016/s0014-5793(01)02536-4;
RA Fujiki Y., Ito M., Nishida I., Watanabe A.;
RT "Leucine and its keto acid enhance the coordinated expression of genes for
RT branched-chain amino acid catabolism in Arabidopsis under sugar
RT starvation.";
RL FEBS Lett. 499:161-165(2001).
RN [8]
RP FUNCTION, AND INDUCTION BY SUGAR.
RX PubMed=11917081; DOI=10.1093/pcp/pcf032;
RA Fujiki Y., Ito M., Itoh T., Nishida I., Watanabe A.;
RT "Activation of the promoters of Arabidopsis genes for the branched-chain
RT alpha-keto acid dehydrogenase complex in transgenic tobacco BY-2 cells
RT under sugar starvation.";
RL Plant Cell Physiol. 43:275-280(2002).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=14764908; DOI=10.1104/pp.103.035675;
RA Taylor N.L., Heazlewood J.L., Day D.A., Millar A.H.;
RT "Lipoic acid-dependent oxidative catabolism of alpha-keto acids in
RT mitochondria provides evidence for branched-chain amino acid catabolism in
RT Arabidopsis.";
RL Plant Physiol. 134:838-848(2004).
CC -!- FUNCTION: The branched-chain alpha-keto dehydrogenase complex catalyzes
CC the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It
CC contains multiple copies of three enzymatic components: branched-chain
CC alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and
CC lipoamide dehydrogenase (E3) (By similarity). Required during sugar
CC starvation and acts under the control of a sugar-sensing mechanism
CC involving Ser/Thr kinases and phosphatases (PubMed:11080291,
CC PubMed:11917081). {ECO:0000250|UniProtKB:P21953,
CC ECO:0000269|PubMed:11080291, ECO:0000269|PubMed:11917081}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-methyl-2-oxobutanoate + H(+) + N(6)-[(R)-lipoyl]-L-lysyl-
CC [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] = CO2 +
CC N(6)-[(R)-S(8)-2-methylpropanoyldihydrolipoyl]-L-lysyl-
CC [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase];
CC Xref=Rhea:RHEA:13457, Rhea:RHEA-COMP:10488, Rhea:RHEA-COMP:10489,
CC ChEBI:CHEBI:11851, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:83099, ChEBI:CHEBI:83142; EC=1.2.4.4;
CC Evidence={ECO:0000250|UniProtKB:P21953};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13458;
CC Evidence={ECO:0000250|UniProtKB:P21953};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000250|UniProtKB:P21953};
CC -!- SUBUNIT: Heterotetramer of alpha and beta chains.
CC {ECO:0000250|UniProtKB:P21953}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:P21953}.
CC -!- TISSUE SPECIFICITY: Expressed in the non-photosynthetic organs such as
CC siliques, flowers and roots. {ECO:0000269|PubMed:10681595}.
CC -!- DEVELOPMENTAL STAGE: Barely detected in non senescent green leaves,
CC accumulated slightly at the early stage of leaf senescence and strongly
CC expressed at the late stage of leaf senescence.
CC {ECO:0000269|PubMed:10681595}.
CC -!- INDUCTION: By dark treatment. Down-regulated by sucrose in a hexokinase
CC dependent manner. Up-regulated by Leucine and its derivative alpha-keto
CC acid (KIC). {ECO:0000269|PubMed:10681595, ECO:0000269|PubMed:11080291,
CC ECO:0000269|PubMed:11418132, ECO:0000269|PubMed:11917081}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF145452; AAF35281.1; -; mRNA.
DR EMBL; AP000603; BAB01752.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75357.1; -; Genomic_DNA.
DR EMBL; BT024889; ABD85160.1; -; mRNA.
DR EMBL; AK229269; BAF01133.1; -; mRNA.
DR RefSeq; NP_187954.1; NM_112191.3.
DR AlphaFoldDB; Q9LDY2; -.
DR SMR; Q9LDY2; -.
DR STRING; 3702.Q9LDY2; -.
DR PaxDb; 3702-AT3G13450-1; -.
DR ProteomicsDB; 238998; -.
DR EnsemblPlants; AT3G13450.1; AT3G13450.1; AT3G13450.
DR GeneID; 820547; -.
DR Gramene; AT3G13450.1; AT3G13450.1; AT3G13450.
DR KEGG; ath:AT3G13450; -.
DR Araport; AT3G13450; -.
DR TAIR; AT3G13450; DIN4.
DR eggNOG; KOG0525; Eukaryota.
DR HOGENOM; CLU_012907_1_0_1; -.
DR InParanoid; Q9LDY2; -.
DR OMA; LPLDTCF; -.
DR OrthoDB; 364at2759; -.
DR PhylomeDB; Q9LDY2; -.
DR BioCyc; ARA:AT3G13450-MONOMER; -.
DR BioCyc; MetaCyc:AT3G13450-MONOMER; -.
DR PRO; PR:Q9LDY2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LDY2; baseline and differential.
DR Genevisible; Q9LDY2; AT.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0003863; F:3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009083; P:branched-chain amino acid catabolic process; IGI:TAIR.
DR GO; GO:0043617; P:cellular response to sucrose starvation; IEP:UniProtKB.
DR GO; GO:0009646; P:response to absence of light; IEP:UniProtKB.
DR GO; GO:0009744; P:response to sucrose; IEP:UniProtKB.
DR CDD; cd07036; TPP_PYR_E1-PDHc-beta_like; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 1.
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; PTHR42980:SF1; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT BETA, MITOCHONDRIAL; 1.
DR PANTHER; PTHR42980; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT BETA-RELATED; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR Pfam; PF02780; Transketolase_C; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE 1: Evidence at protein level;
KW Metal-binding; Mitochondrion; Oxidoreductase; Potassium;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..16
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 17..358
FT /note="2-oxoisovalerate dehydrogenase subunit beta 2,
FT mitochondrial"
FT /id="PRO_0000422385"
FT BINDING 119
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /ligand_note="ligand shared with alpha subunit"
FT /evidence="ECO:0000250|UniProtKB:P21953"
FT BINDING 145
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:P21953"
FT BINDING 147
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:P21953"
FT BINDING 148
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:P21953"
FT BINDING 198
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:P21953"
FT BINDING 200
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:P21953"
SQ SEQUENCE 358 AA; 39419 MW; 3F708CBEC7D82C1B CRC64;
MAAALVRRFC RGSSFPVSGH GYRMLSTVEN VSESGKSMNL YSAINQALHI ALETDPRSYV
FGEDVGFGGV FRCTTGLAER FGKSRVFNTP LCEQGIVGFG IGLAAMGNRV IAEIQFADYI
FPAFDQIVNE AAKFRYRSGN QFNCGGLTIR APYGAVGHGG HYHSQSPEAF FCHVPGIKVV
IPRSPREAKG LLLSSIRDPN PVVFFEPKWL YRQAVEDVPE DDYMIPLSEA EVMREGSDIT
LVGWGAQLTI MEQACLDAEN EGISCELIDL KTLIPWDKEI VETSVRKTGR LLISHEAPVT
GGFGAEIAAT IVERCFLRLE APVSRVCGLD TPFPLVFEPF YMPTKNKILD AIRSTVNY
//
