ID   ODBB1_ARATH             Reviewed;         352 AA.
AC   Q9SAV3; O82450;
DT   29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=2-oxoisovalerate dehydrogenase subunit beta 1, mitochondrial;
DE            EC=1.2.4.4;
DE   AltName: Full=Branched-chain alpha-keto acid dehydrogenase E1 component beta chain;
DE            Short=BCKDE1B;
DE            Short=BCKDH E1-beta;
DE   Flags: Precursor;
GN   Name=BCDH BETA1; OrderedLocusNames=At1g55510; ORFNames=T5A14.9;
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].
RA   Luethy M.H., Miernyk J.A., Randall D.D.;
RT   "The nucleotide sequence of a cDNA encoding the E1 beta-subunit of the
RT   branched-chain alpha-keto acid dehydrogenase from Arabidopsis.";
RL   (er) Plant Gene Register PGR98-133(1998).
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;
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.
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). {ECO:0000250}.
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   -!- SUBUNIT: Heterotetramer of alpha and beta chains. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
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DR   EMBL; AF061638; AAC64005.1; -; mRNA.
DR   EMBL; AC005223; AAD10651.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE33256.1; -; Genomic_DNA.
DR   EMBL; BT024741; ABD59079.1; -; mRNA.
DR   PIR; D96597; D96597.
DR   PIR; T51835; T51835.
DR   RefSeq; NP_175947.1; NM_104426.4.
DR   AlphaFoldDB; Q9SAV3; -.
DR   SMR; Q9SAV3; -.
DR   STRING; 3702.AT1G55510.1; -.
DR   PaxDb; Q9SAV3; -.
DR   PRIDE; Q9SAV3; -.
DR   ProteomicsDB; 238997; -.
DR   EnsemblPlants; AT1G55510.1; AT1G55510.1; AT1G55510.
DR   GeneID; 841998; -.
DR   Gramene; AT1G55510.1; AT1G55510.1; AT1G55510.
DR   KEGG; ath:AT1G55510; -.
DR   Araport; AT1G55510; -.
DR   TAIR; locus:2193889; AT1G55510.
DR   eggNOG; KOG0525; Eukaryota.
DR   HOGENOM; CLU_012907_1_0_1; -.
DR   InParanoid; Q9SAV3; -.
DR   OMA; SEAYYMA; -.
DR   OrthoDB; 1200844at2759; -.
DR   PhylomeDB; Q9SAV3; -.
DR   BioCyc; ARA:AT1G55510-MON; -.
DR   PRO; PR:Q9SAV3; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9SAV3; baseline and differential.
DR   Genevisible; Q9SAV3; 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:0009083; P:branched-chain amino acid catabolic process; IGI:TAIR.
DR   GO; GO:0007584; P:response to nutrient; IBA:GO_Central.
DR   Gene3D; 3.40.50.920; -; 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   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   2: Evidence at transcript level;
KW   Mitochondrion; Oxidoreductase; Reference proteome; Transit peptide.
FT   TRANSIT         1..23
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..352
FT                   /note="2-oxoisovalerate dehydrogenase subunit beta 1,
FT                   mitochondrial"
FT                   /id="PRO_0000422384"
FT   CONFLICT        18
FT                   /note="S -> T (in Ref. 1; AAC64005)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   352 AA;  38735 MW;  B56C692E33ADD428 CRC64;
     MAALLGRSCR KLSFPSLSHG ARRVSTETGK PLNLYSAINQ ALHIALDTDP RSYVFGEDVG
     FGGVFRCTTG LAERFGKNRV FNTPLCEQGI VGFGIGLAAM GNRAIVEIQF ADYIYPAFDQ
     IVNEAAKFRY RSGNQFNCGG LTIRAPYGAV GHGGHYHSQS PEAFFCHVPG IKVVIPRSPR
     EAKGLLLSCI RDPNPVVFFE PKWLYRQAVE EVPEHDYMIP LSEAEVIREG NDITLVGWGA
     QLTVMEQACL DAEKEGISCE LIDLKTLLPW DKETVEASVK KTGRLLISHE APVTGGFGAE
     ISATILERCF LKLEAPVSRV CGLDTPFPLV FEPFYMPTKN KILDAIKSTV NY