ODBA_CAEEL
ID ODBA_CAEEL Reviewed; 431 AA.
AC O45924;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial;
DE EC=1.2.4.4 {ECO:0000269|PubMed:15340492};
DE AltName: Full=Branched-chain alpha-keto acid dehydrogenase E1 component alpha chain;
DE Flags: Precursor;
GN Name=bckd-1A {ECO:0000312|WormBase:Y39E4A.3a};
GN ORFNames=Y39E4A.3 {ECO:0000312|WormBase:Y39E4A.3a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=15340492; DOI=10.1371/journal.pbio.0020257;
RA Kniazeva M., Crawford Q.T., Seiber M., Wang C.Y., Han M.;
RT "Monomethyl branched-chain fatty acids play an essential role in
RT Caenorhabditis elegans development.";
RL PLoS Biol. 2:E257-E257(2004).
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 for the
CC production of the monomethyl branched-chain fatty acids (mmBCFAs)
CC isopentadecanoate (C15iso) and isoheptadecanoate (C17iso)
CC (PubMed:15340492). {ECO:0000250|UniProtKB:P11178,
CC ECO:0000269|PubMed:15340492}.
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 Evidence={ECO:0000269|PubMed:15340492};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000250|UniProtKB:P12694};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000269|PubMed:15340492}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:P11178}.
CC -!- SIMILARITY: Belongs to the BCKDHA family. {ECO:0000305}.
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DR EMBL; AL021480; CAA16329.2; -; Genomic_DNA.
DR PIR; T26758; T26758.
DR RefSeq; NP_001033376.1; NM_001038287.2.
DR AlphaFoldDB; O45924; -.
DR SMR; O45924; -.
DR BioGRID; 41889; 6.
DR DIP; DIP-25302N; -.
DR IntAct; O45924; 1.
DR STRING; 6239.Y39E4A.3b; -.
DR SwissLipids; SLP:000000190; -.
DR EPD; O45924; -.
DR PaxDb; O45924; -.
DR PeptideAtlas; O45924; -.
DR PRIDE; O45924; -.
DR EnsemblMetazoa; Y39E4A.3a.1; Y39E4A.3a.1; WBGene00012713.
DR EnsemblMetazoa; Y39E4A.3a.2; Y39E4A.3a.2; WBGene00012713.
DR GeneID; 176716; -.
DR UCSC; Y39E4A.3b; c. elegans.
DR CTD; 176716; -.
DR WormBase; Y39E4A.3a; CE33866; WBGene00012713; bckd-1A.
DR eggNOG; KOG1182; Eukaryota.
DR HOGENOM; CLU_029393_1_2_1; -.
DR InParanoid; O45924; -.
DR OMA; GMFRGVN; -.
DR Reactome; R-CEL-389661; Glyoxylate metabolism and glycine degradation.
DR Reactome; R-CEL-70895; Branched-chain amino acid catabolism.
DR UniPathway; UPA00094; -.
DR PRO; PR:O45924; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00012713; Expressed in germ line (C elegans) and 4 other tissues.
DR ExpressionAtlas; O45924; baseline and differential.
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; IBA:GO_Central.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR034616; BCKDH_E1-a.
DR InterPro; IPR001017; DH_E1.
DR InterPro; IPR029061; THDP-binding.
DR PANTHER; PTHR43380:SF1; PTHR43380:SF1; 1.
DR Pfam; PF00676; E1_dh; 1.
DR SUPFAM; SSF52518; SSF52518; 1.
PE 1: Evidence at protein level;
KW Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW Lipid metabolism; Metal-binding; Mitochondrion; Oxidoreductase;
KW Phosphoprotein; Potassium; Reference proteome; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..431
FT /note="2-oxoisovalerate dehydrogenase subunit alpha,
FT mitochondrial"
FT /id="PRO_0000421270"
FT BINDING 140..142
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250|UniProtKB:P12694"
FT BINDING 189
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P12694"
FT BINDING 194
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P12694"
FT BINDING 195
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P12694"
SQ SEQUENCE 431 AA; 49021 MW; A6CAA29B9220AB1C CRC64;
MHRALLNASR RVATVRSMAS TVEGDAFRLS EYSSKYLGHR KAAFTEKLEI VNADDTPALP
IYRVTNAVGD VIDKSQDPNF DEQTSLKMYK TMTQLNIMDR ILYDSQRQGR ISFYMTSFGE
EGNHVGSAAA LEPQDLIYGQ YREAGVLLWR GYTMENFMNQ CYGNADDLGK GRQMPMHFGT
KERNFVTISS PLTTQLPQAV GSAYAFKQQK DNNRIAVVYF GDGAASEGDA HAAFNFAATL
KCPIIFFCRN NGYAISTPTS EQYGGDGIAG KGPAYGLHTI RVDGNDLLAV YNATKEARRV
ALTNRPVLIE AMTYRLGHHS TSDDSTAYRS SDEVQTWGDK DHPITRFKKY ITERGWWNEE
KEMEWQKEVK KRVLTEFAAA EKRKKAHYHD LFEDVYDELP LRLRRQRDEL DAHVAEYKEH
YPMLETLQSK P
