ODBB_BOVIN
ID ODBB_BOVIN Reviewed; 392 AA.
AC P21839; Q148F4; Q28047;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=2-oxoisovalerate dehydrogenase subunit beta, 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=BCKDHB;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=2322554; DOI=10.1021/bi00457a009;
RA Nobukuni Y., Mitsubuchi H., Endo F., Asaka J., Oyama R., Titani K.,
RA Matsuda I.;
RT "Isolation and characterization of a complementary DNA clone coding for the
RT E1 beta subunit of the bovine branched-chain alpha-ketoacid dehydrogenase
RT complex: complete amino acid sequence of the precursor protein and its
RT proteolytic processing.";
RL Biochemistry 29:1154-1160(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal pons;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 24-392.
RC TISSUE=Liver;
RX PubMed=1730724; DOI=10.1016/s0021-9258(18)46029-2;
RA Wynn R.M., Chuang J.L., Davie J.R., Fisher C.W., Hale M.A., Cox R.P.,
RA Chuang D.T.;
RT "Cloning and expression in Escherichia coli of mature E1 beta subunit of
RT bovine mitochondrial branched-chain alpha-keto acid dehydrogenase complex.
RT Mapping of the E1 beta-binding region on E2.";
RL J. Biol. Chem. 267:1881-1887(1992).
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).
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 2 alpha and 2 beta chains. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
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DR EMBL; M33323; AAA30407.1; -; mRNA.
DR EMBL; BC118380; AAI18381.1; -; mRNA.
DR EMBL; M81742; AAA51410.1; -; mRNA.
DR PIR; A34267; A34267.
DR RefSeq; NP_776932.1; NM_174507.2.
DR AlphaFoldDB; P21839; -.
DR SMR; P21839; -.
DR PRIDE; P21839; -.
DR Ensembl; ENSBTAT00000016044; ENSBTAP00000016044; ENSBTAG00000012096.
DR GeneID; 282150; -.
DR KEGG; bta:282150; -.
DR CTD; 594; -.
DR VEuPathDB; HostDB:ENSBTAG00000012096; -.
DR VGNC; VGNC:97245; BCKDHB.
DR GeneTree; ENSGT00940000156533; -.
DR InParanoid; P21839; -.
DR OMA; SEAYYMA; -.
DR OrthoDB; 1200844at2759; -.
DR SABIO-RK; P21839; -.
DR Proteomes; UP000009136; Chromosome 9.
DR Bgee; ENSBTAG00000012096; Expressed in rumen papilla and 106 other tissues.
DR GO; GO:0005947; C:mitochondrial alpha-ketoglutarate dehydrogenase complex; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
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; IBA:GO_Central.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Lipid metabolism; Mitochondrion;
KW Oxidoreductase; Reference proteome; Transit peptide.
FT TRANSIT 1..50
FT /note="Mitochondrion"
FT CHAIN 51..392
FT /note="2-oxoisovalerate dehydrogenase subunit beta,
FT mitochondrial"
FT /id="PRO_0000020469"
FT MOD_RES 232
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q6P3A8"
FT MOD_RES 241
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P21953"
FT CONFLICT 24..46
FT /note="RRLCGAGLSRGFLQSASAYGAAA -> GPGCVARACRGASCSPPRPTGLR
FT (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 28
FT /note="G -> C (in Ref. 2; AAI18381)"
FT /evidence="ECO:0000305"
FT CONFLICT 283
FT /note="V -> E (in Ref. 3; AAA51410)"
FT /evidence="ECO:0000305"
FT CONFLICT 288
FT /note="A -> D (in Ref. 1; AAA30407)"
FT /evidence="ECO:0000305"
FT CONFLICT 348
FT /note="E -> Q (in Ref. 3; AAA51410)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 392 AA; 42935 MW; 4E3ABC39ED54281A CRC64;
MAAVAAFAGW LLRLRAAGAD GPWRRLCGAG LSRGFLQSAS AYGAAAQRRQ VAHFTFQPDP
EPVEYGQTQK MNLFQAVTSA LDNSLAKDPT AVIFGEDVAF GGVFRCTVGL RDKYGKDRVF
NTPLCEQGIV GFGIGIAVTG ATAIAEIQFA DYIFPAFDQI VNEAAKYRYR SGDLFNCGSL
TIRSPWGCVG HGALYHSQSP EAFFAHCPGI KVVVPRSPFQ AKGLLLSCIE DKNPCIFFEP
KILYRAAVEQ VPVEPYNIPL SQAEVIQEGS DVTLVAWGTQ VHVIREVAAM AQEKLGVSCE
VIDLRTILPW DVDTVCKSVI KTGRLLVSHE APLTGGFASE ISSTVQEECF LNLEAPISRV
CGYDTPFPHI FEPFYIPDKW KCYDALRKMI NY
