ID Q2LDG6_UROPR Unreviewed; 65 AA.
AC Q2LDG6;
DT 21-FEB-2006, integrated into UniProtKB/TrEMBL.
DT 21-FEB-2006, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=2-oxoisovalerate dehydrogenase subunit alpha {ECO:0000256|RuleBase:RU365014};
DE EC=1.2.4.4 {ECO:0000256|RuleBase:RU365014};
DE AltName: Full=Branched-chain alpha-keto acid dehydrogenase E1 component alpha chain {ECO:0000256|RuleBase:RU365014};
DE Flags: Fragment;
OS Urocitellus parryii (Arctic ground squirrel) (Spermophilus parryii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Urocitellus.
OX NCBI_TaxID=9999 {ECO:0000313|EMBL:ABC59809.1};
RN [1] {ECO:0000313|EMBL:ABC59809.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=16464973; DOI=10.1152/physiolgenomics.00260.2005;
RA Yan J., Burman A., Nichols C., Alila L., Showe L.C., Showe M.K.,
RA Boyer B.B., Barnes B.M., Marr T.G.;
RT "Detection of differential gene expression in brown adipose tissue of
RT hibernating arctic ground squirrels with mouse microarrays.";
RL Physiol. Genomics 25:346-353(2006).
CC -!- FUNCTION: Together with BCKDHB forms the heterotetrameric E1 subunit of
CC the mitochondrial branched-chain alpha-ketoacid dehydrogenase (BCKD)
CC complex. The BCKD complex catalyzes the multi-step oxidative
CC decarboxylation of alpha-ketoacids derived from the branched-chain
CC amino-acids valine, leucine and isoleucine producing CO2 and acyl-CoA
CC which is subsequently utilized to produce energy. The E1 subunit
CC catalyzes the first step with the decarboxylation of the alpha-ketoacid
CC forming an enzyme-product intermediate. A reductive acylation mediated
CC by the lipoylamide cofactor of E2 extracts the acyl group from the E1
CC active site for the next step of the reaction.
CC {ECO:0000256|ARBA:ARBA00037052, ECO:0000256|RuleBase:RU365014}.
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:0000256|ARBA:ARBA00043720};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13458;
CC Evidence={ECO:0000256|ARBA:ARBA00043720};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|RuleBase:RU365014};
CC -!- SIMILARITY: Belongs to the BCKDHA family.
CC {ECO:0000256|ARBA:ARBA00008646, ECO:0000256|RuleBase:RU365014}.
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DR EMBL; DQ334051; ABC59809.1; -; mRNA.
DR AlphaFoldDB; Q2LDG6; -.
DR GO; GO:0003863; F:3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.970; -; 1.
DR InterPro; IPR001017; DH_E1.
DR InterPro; IPR029061; THDP-binding.
DR PANTHER; PTHR43380; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43380:SF1; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR Pfam; PF00676; E1_dh; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
PE 2: Evidence at transcript level;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU365014}; Potassium {ECO:0000256|ARBA:ARBA00022958};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU365014};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 2..65
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABC59809.1"
FT NON_TER 65
FT /evidence="ECO:0000313|EMBL:ABC59809.1"
SQ SEQUENCE 65 AA; 6727 MW; 26245A953A916F17 CRC64;
GCNERHFVTI SSPLATQIPQ AVGAAYAAKR ANANRVVICY FGEGAASEGD AHAGFNFAAT
LECPI
//
