ID A0A1I7Y7N0_9BILA Unreviewed; 477 AA.
AC A0A1I7Y7N0;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
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};
OS Steinernema glaseri.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Steinernematidae;
OC Steinernema.
OX NCBI_TaxID=37863 {ECO:0000313|Proteomes:UP000095287, ECO:0000313|WBParaSite:L893_g13501.t1};
RN [1] {ECO:0000313|WBParaSite:L893_g13501.t1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
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 WBParaSite; L893_g13501.t1; L893_g13501.t1; L893_g13501.
DR Proteomes; UP000095287; Unplaced.
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 Thiamine pyrophosphate {ECO:0000256|RuleBase:RU365014};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 138..435
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
SQ SEQUENCE 477 AA; 54143 MW; 98D4BDDA0EB5021A CRC64;
MVKPVELPQS RRRLGSEDVK SFCTELTHSH GSSEGHLRVD DDLXXXXLGR SVAARHIAAA
TSVSAAGRRD YSDEFRLKEY SEKYLGYRKT RFTEKLEVVD SKQVEAFPIY RATDSNGEFI
TPENDPKFSK ELAVKMYESM TFLNTMDKIL YDSQRQGRIS FYMTNFGEEA SHIGSAAALD
PTDLVYGQYR EAGVLMYRGF PLEQFMHQCY GNSMDIGKGK QMPVHYGSAE HHFVTISSPL
TTQMPQAVGS AYAFKRAKND RVVCVYFGDG AASEGDAHAA FNFAATLDCP IIFFCRNNGY
AISTPTAEQY AGDGIAGKGP GYGLHTIRVD GNDLFAVYNA TKEARRLALE NKPVLIEAMT
YRAGHHSTSD DSTAYRTKEE VDSWMEKDNA INRFRKYLER KGWWNEEAEK AWIQQSRKDV
LKAFSYAEKV HKQHPHEMFN GVYAELPEHL RRQQDAMDKH LEEYGEHYPL DQFGVKK
//
