ID G0NSE9_CAEBE Unreviewed; 430 AA.
AC G0NSE9;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
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};
GN ORFNames=CAEBREN_02420 {ECO:0000313|EMBL:EGT36743.1}, CAEBREN_05328
GN {ECO:0000313|EMBL:EGT36804.1};
OS Caenorhabditis brenneri (Nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=135651 {ECO:0000313|Proteomes:UP000008068};
RN [1] {ECO:0000313|EMBL:EGT36743.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PB2801 {ECO:0000313|EMBL:EGT36743.1};
RG The Caenorhabditis brenneri Sequencing and Analysis Consortium;
RA Wilson R.K.;
RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000008068}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB2801 {ECO:0000313|Proteomes:UP000008068};
RG Caenorhabditis brenneri Sequencing and Analysis Consortium;
RA Wilson R.K.;
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:EGT36743.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB2801 {ECO:0000313|EMBL:EGT36743.1};
RG WormBase Consortium;
RL Submitted (JUL-2011) 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). {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|RuleBase:RU365014};
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; GL379937; EGT36743.1; -; Genomic_DNA.
DR EMBL; GL379938; EGT36804.1; -; Genomic_DNA.
DR STRING; 135651.G0NSE9; -.
DR EnsemblMetazoa; CBN02420.1; CBN02420.1; WBGene00141145.
DR EnsemblMetazoa; CBN05328.1; CBN05328.1; WBGene00144053.
DR eggNOG; KOG1182; Eukaryota.
DR HOGENOM; CLU_029393_1_2_1; -.
DR OMA; EMFEGVY; -.
DR Proteomes; UP000008068; Unassembled WGS sequence.
DR GO; GO:0003863; F:3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity; IEA:UniProtKB-EC.
DR CDD; cd02000; TPP_E1_PDC_ADC_BCADC; 1.
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 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU365014};
KW Reference proteome {ECO:0000313|Proteomes:UP000008068};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU365014};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 89..387
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
SQ SEQUENCE 430 AA; 48677 MW; 20CD566DB418C0CB CRC64;
MHRALLHVSR RAAAVRNLAS TVEGDAFRLS EYSSKYLGHR KAAFTEKLEI INADATPAIP
IYRVTNAVGD VIDKAQDPNF DQETSIKMYK TMTQLNIMDR ILYDSQRQGR ISFYMTSFGE
EGNHVGSAAA LEPQDLIYGQ YREAGVLLWR GYSMESFMNQ CYGNASDLGK GRQMPMHFGT
KDLNFVTISS PLTTQLPQAV GSAYAFKQQK DNDRICVVYF GDGAASEGDA HAAFNFAATL
KAPIIFFCRN NGYAISTPTS EQYGGDGIAG KGPAYGLHTI RVDGNDLLAV YNATKEARRV
ALTNRPVLIE AMTYRLGHHS TSDDSTAYRS AEEVETWGDK DHPITRFNKY ITERGWWNEE
KEKEWQKEVK KRVLTEFAAA EKRKKAHYHD LFEDVYDELP LRLRRQRDEL DAHIAEYKEH
YPMEGLNSKP
//
