ODB2_ARATH
ID ODB2_ARATH Reviewed; 483 AA.
AC Q9M7Z1; O64968; Q9M724;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial;
DE EC=2.3.1.168;
DE AltName: Full=Branched-chain alpha-keto acid dehydrogenase complex component E2;
DE Short=BCE2;
DE Short=BCKAD-E2;
DE Short=BCKADE2;
DE AltName: Full=Dihydrolipoamide acetyltransferase component of branched-chain alpha-keto acid dehydrogenase complex;
DE AltName: Full=Dihydrolipoamide branched chain transacylase;
DE AltName: Full=Dihydrolipoyllysine-residue (2-methylpropanoyl)transferase;
DE AltName: Full=Protein DARK INDUCIBLE 3;
DE Flags: Precursor;
GN Name=BCE2; Synonyms=DIN3, LTA1; OrderedLocusNames=At3g06850;
GN ORFNames=F3E22.1;
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].
RC STRAIN=cv. Columbia;
RA Mooney B.P., Miernyk J.A., Randall D.D.;
RT "Nucleotide sequence of a cDNA encoding the dihydrolipoylacyltransferase
RT (E2) subunit of the branched-chain alpha-keto-acid dehydrogenase complex
RT from Arabidopsis thaliana.";
RL (er) Plant Gene Register PGR98-071(1998).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia; TISSUE=Rosette leaf;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
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.
RN [7]
RP REVIEW.
RX PubMed=2188967; DOI=10.1016/s0021-9258(19)38795-2;
RA Reed L.J., Hackert M.L.;
RT "Structure-function relationships in dihydrolipoamide acyltransferases.";
RL J. Biol. Chem. 265:8971-8974(1990).
RN [8]
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 [9]
RP SUBUNIT.
RX PubMed=10933498; DOI=10.1110/ps.9.7.1334;
RA Mooney B.P., Henzl M.T., Miernyk J.A., Randall D.D.;
RT "The dihydrolipoyl acyltransferase (BCE2) subunit of the plant branched-
RT chain alpha-ketoacid dehydrogenase complex forms a 24-mer core with
RT octagonal symmetry.";
RL Protein Sci. 9:1334-1339(2000).
RN [10]
RP INDUCTION BY DARK AND SUCROSE, AND 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 [11]
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 [12]
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 [13]
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).
RN [14]
RP INDUCTION BY DARK.
RX PubMed=16100230; DOI=10.1093/pcp/pci174;
RA Fujiki Y., Nakagawa Y., Furumoto T., Yoshida S., Biswal B., Ito M.,
RA Watanabe A., Nishida I.;
RT "Response to darkness of late-responsive dark-inducible genes is positively
RT regulated by leaf age and negatively regulated by calmodulin-antagonist-
RT sensitive signalling in Arabidopsis thaliana.";
RL Plant Cell Physiol. 46:1741-1746(2005).
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). Within this complex, the catalytic
CC function of this enzyme is to accept, and to transfer to coenzyme A,
CC acyl groups that are generated by the branched-chain alpha-keto acid
CC decarboxylase component (By similarity). Required during sugar
CC starvation and acts under the control of a sugar-sensing mechanism
CC involving Ser/Thr kinases and phosphatases. {ECO:0000250,
CC ECO:0000269|PubMed:11080291, ECO:0000269|PubMed:11917081}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + 2-methylpropanoyl-
CC CoA = (R)-N(6)-(S(8)-2-methylpropanoyldihydrolipoyl)-L-lysyl-
CC [protein] + CoA; Xref=Rhea:RHEA:18865, Rhea:RHEA-COMP:10475,
CC Rhea:RHEA-COMP:10497, ChEBI:CHEBI:57287, ChEBI:CHEBI:57338,
CC ChEBI:CHEBI:83100, ChEBI:CHEBI:83142; EC=2.3.1.168;
CC -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088; Evidence={ECO:0000250};
CC Note=Binds 1 lipoyl cofactor covalently. {ECO:0000250};
CC -!- SUBUNIT: Forms a 24-polypeptide structural core with octahedral
CC symmetry. {ECO:0000269|PubMed:10933498}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:14671022, ECO:0000269|PubMed:14764908}.
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 (at the protein level). Induced by the
CC calmodulin antagonists trifluoperazine and fluphenazine in darkness.
CC Down-regulated by sucrose in a hexokinase dependent manner (at protein
CC level). Up-regulated by Leucine and its derivative alpha-keto acid
CC (KIC). {ECO:0000269|PubMed:10681595, ECO:0000269|PubMed:11080291,
CC ECO:0000269|PubMed:11418132, ECO:0000269|PubMed:11917081,
CC ECO:0000269|PubMed:16100230}.
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AF038505; AAC16694.1; -; mRNA.
DR EMBL; AF145451; AAF35280.1; -; mRNA.
DR EMBL; AC023912; AAF63813.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74466.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74467.1; -; Genomic_DNA.
DR EMBL; AK316767; BAH19487.1; -; mRNA.
DR EMBL; AK317408; BAH20078.1; -; mRNA.
DR EMBL; AY086441; AAM63444.1; -; mRNA.
DR PIR; T52136; T52136.
DR RefSeq; NP_187341.1; NM_111565.6.
DR RefSeq; NP_850527.1; NM_180196.3.
DR AlphaFoldDB; Q9M7Z1; -.
DR SMR; Q9M7Z1; -.
DR BioGRID; 5204; 7.
DR STRING; 3702.AT3G06850.1; -.
DR PaxDb; Q9M7Z1; -.
DR PRIDE; Q9M7Z1; -.
DR ProteomicsDB; 238906; -.
DR EnsemblPlants; AT3G06850.1; AT3G06850.1; AT3G06850.
DR EnsemblPlants; AT3G06850.2; AT3G06850.2; AT3G06850.
DR GeneID; 819869; -.
DR Gramene; AT3G06850.1; AT3G06850.1; AT3G06850.
DR Gramene; AT3G06850.2; AT3G06850.2; AT3G06850.
DR KEGG; ath:AT3G06850; -.
DR Araport; AT3G06850; -.
DR TAIR; locus:2083358; AT3G06850.
DR eggNOG; KOG0558; Eukaryota.
DR HOGENOM; CLU_016733_10_0_1; -.
DR InParanoid; Q9M7Z1; -.
DR OMA; HPCIMAP; -.
DR OrthoDB; 854035at2759; -.
DR PhylomeDB; Q9M7Z1; -.
DR PRO; PR:Q9M7Z1; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M7Z1; baseline and differential.
DR Genevisible; Q9M7Z1; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0016407; F:acetyltransferase activity; IDA:TAIR.
DR GO; GO:0004147; F:dihydrolipoamide branched chain acyltransferase activity; TAS:TAIR.
DR GO; GO:0043754; F:dihydrolipoyllysine-residue (2-methylpropanoyl)transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0031405; F:lipoic acid binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; HDA:TAIR.
DR GO; GO:0043617; P:cellular response to sucrose starvation; IEP:UniProtKB.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009646; P:response to absence of light; IEP:UniProtKB.
DR GO; GO:0009744; P:response to sucrose; IEP:UniProtKB.
DR Gene3D; 3.30.559.10; -; 1.
DR Gene3D; 4.10.320.10; -; 1.
DR InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR036625; E3-bd_dom_sf.
DR InterPro; IPR004167; PSBD.
DR InterPro; IPR011053; Single_hybrid_motif.
DR Pfam; PF00198; 2-oxoacid_dh; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF02817; E3_binding; 1.
DR SUPFAM; SSF47005; SSF47005; 1.
DR SUPFAM; SSF51230; SSF51230; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00189; LIPOYL; 1.
DR PROSITE; PS51826; PSBD; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Lipoyl; Mitochondrion;
KW Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..75
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 76..483
FT /note="Lipoamide acyltransferase component of branched-
FT chain alpha-keto acid dehydrogenase complex, mitochondrial"
FT /id="PRO_0000422386"
FT DOMAIN 76..150
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT DOMAIN 183..220
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01170"
FT ACT_SITE 453
FT /evidence="ECO:0000255"
FT ACT_SITE 457
FT /evidence="ECO:0000255"
FT MOD_RES 116
FT /note="N6-lipoyllysine"
FT /evidence="ECO:0000250, ECO:0000255|PROSITE-
FT ProRule:PRU01066"
FT CONFLICT 68
FT /note="A -> R (in Ref. 2; AAF35280)"
FT /evidence="ECO:0000305"
FT CONFLICT 412
FT /note="P -> L (in Ref. 1; AAC16694)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 483 AA; 52706 MW; C454CA5B8F7C5357 CRC64;
MIARRIWRSH RFLRPFSSSS VCSPPFRVPE YLSQSSSSPA SRPFFVHPPT LMKWGGGSRS
WFSNEAMATD SNSGLIDVPL AQTGEGIAEC ELLKWFVKEG DSVEEFQPLC EVQSDKATIE
ITSRFKGKVA LISHSPGDII KVGETLVRLA VEDSQDSLLT TDSSEIVTLG GSKQGTENLL
GALSTPAVRN LAKDLGIDIN VITGTGKDGR VLKEDVLRFS DQKGFVTDSV SSEHAVIGGD
SVSTKASSNF EDKTVPLRGF SRAMVKTMTM ATSVPHFHFV EEINCDSLVE LKQFFKENNT
DSTIKHTFLP TLIKSLSMAL TKYPFVNSCF NAESLEIILK GSHNIGVAMA TEHGLVVPNI
KNVQSLSLLE ITKELSRLQH LAANNKLNPE DVTGGTITLS NIGAIGGKFG SPLLNLPEVA
IIALGRIEKV PKFSKEGTVY PASIMMVNIA ADHRVLDGAT VARFCCQWKE YVEKPELLML
QMR
