ODBA1_ARATH
ID ODBA1_ARATH Reviewed; 472 AA.
AC Q9LPL5; Q9ZT57;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=2-oxoisovalerate dehydrogenase subunit alpha 1, mitochondrial;
DE EC=1.2.4.4;
DE AltName: Full=Branched-chain alpha-keto acid dehydrogenase E1 component alpha chain;
DE Short=BCKDE1A;
DE Short=BCKDH E1-alpha;
DE Flags: Precursor;
GN OrderedLocusNames=At1g21400; ORFNames=F24J8.4;
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 [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 [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-472.
RA Mooney B.P., Miernyk J.A., Randall D.D.;
RT "Nucleotide sequence of a cDNA encoding the E1 alpha subunit of the
RT branched-chain alpha-keto acid dehydrogenase complex from Arabidopsis
RT thaliana.";
RL (er) Plant Gene Register PGR98-168(1998).
RN [5]
RP FUNCTION, 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).
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. {ECO:0000250, ECO:0000269|PubMed:11418132}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue (2-
CC methylpropanoyl)transferase] + 3-methyl-2-oxobutanoate + H(+) = (R)-
CC N(6)-(S(8)-2-methylpropanoyldihydrolipoyl)-L-lysyl-
CC [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] + CO2;
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 -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000250};
CC -!- SUBUNIT: Heterotetramer of alpha and beta chains. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
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:11418132}.
CC -!- MISCELLANEOUS: Bound potassium ions stabilize the protein structure.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the BCKDHA family. {ECO:0000305}.
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DR EMBL; AC015447; AAF87894.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30099.1; -; Genomic_DNA.
DR EMBL; AY099615; AAM20466.1; -; mRNA.
DR EMBL; BT000269; AAN15588.1; -; mRNA.
DR EMBL; AF077955; AAC69851.1; -; mRNA.
DR PIR; A86347; A86347.
DR PIR; T51858; T51858.
DR RefSeq; NP_173562.1; NM_101992.5.
DR AlphaFoldDB; Q9LPL5; -.
DR SMR; Q9LPL5; -.
DR BioGRID; 23978; 1.
DR STRING; 3702.AT1G21400.1; -.
DR iPTMnet; Q9LPL5; -.
DR PaxDb; Q9LPL5; -.
DR PRIDE; Q9LPL5; -.
DR ProteomicsDB; 238907; -.
DR EnsemblPlants; AT1G21400.1; AT1G21400.1; AT1G21400.
DR GeneID; 838739; -.
DR Gramene; AT1G21400.1; AT1G21400.1; AT1G21400.
DR KEGG; ath:AT1G21400; -.
DR Araport; AT1G21400; -.
DR TAIR; locus:2027072; AT1G21400.
DR eggNOG; KOG1182; Eukaryota.
DR HOGENOM; CLU_029393_1_1_1; -.
DR InParanoid; Q9LPL5; -.
DR PhylomeDB; Q9LPL5; -.
DR PRO; PR:Q9LPL5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LPL5; baseline and differential.
DR Genevisible; Q9LPL5; AT.
DR GO; GO:0005947; C:mitochondrial alpha-ketoglutarate dehydrogenase complex; IBA:GO_Central.
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 InterPro; IPR001017; DH_E1.
DR InterPro; IPR029061; THDP-binding.
DR Pfam; PF00676; E1_dh; 1.
DR SUPFAM; SSF52518; SSF52518; 1.
PE 2: Evidence at transcript level;
KW Metal-binding; Mitochondrion; Oxidoreductase; Potassium;
KW Reference proteome; Thiamine pyrophosphate; Transit peptide.
FT TRANSIT 1..56
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 57..472
FT /note="2-oxoisovalerate dehydrogenase subunit alpha 1,
FT mitochondrial"
FT /id="PRO_0000422382"
FT BINDING 185..187
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 234
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 239
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 240
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT CONFLICT 322..329
FT /note="RSIRVDGN -> PKHPVWDGT (in Ref. 4; AAC69851)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 472 AA; 53488 MW; B499EE174579D13A CRC64;
MAIWFARSKT LVSSLRHNLN LSTILIKRDY SHRPIFYTTS QLSSTAYLSP FGSLRHESTA
VETQADHLVQ QIDEVDAQEL DFPGGKVGYT SEMKFIPESS SRRIPCYRVL DEDGRIIPDS
DFIPVSEKLA VRMYEQMATL QVMDHIFYEA QRQGRISFYL TSVGEEAINI ASAAALSPDD
VVLPQYREPG VLLWRGFTLE EFANQCFGNK ADYGKGRQMP IHYGSNRLNY FTISSPIATQ
LPQAAGVGYS LKMDKKNACT VTFIGDGGTS EGDFHAGLNF AAVMEAPVVF ICRNNGWAIS
THISEQFRSD GIVVKGQAYG IRSIRVDGND ALAVYSAVRS AREMAVTEQR PVLIEMMTYR
VGHHSTSDDS TKYRAADEIQ YWKMSRNPVN RFRKWVEDNG WWSEEDESKL RSNARKQLLQ
AIQAAEKWEK QPLTELFNDV YDVKPKNLEE QELGLKELVK KQPQDYPPGF HV
