ID E4X0I4_OIKDI Unreviewed; 416 AA.
AC E4X0I4;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=GSOID_T00015218001 {ECO:0000313|EMBL:CBY23283.1};
OS Oikopleura dioica (Tunicate).
OC Eukaryota; Metazoa; Chordata; Tunicata; Appendicularia; Copelata;
OC Oikopleuridae; Oikopleura.
OX NCBI_TaxID=34765 {ECO:0000313|EMBL:CBY23283.1};
RN [1] {ECO:0000313|EMBL:CBY23283.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21097902; DOI=10.1126/science.1194167;
RA Denoeud F., Henriet S., Mungpakdee S., Aury J.M., Da Silva C.,
RA Brinkmann H., Mikhaleva J., Olsen L.C., Jubin C., Canestro C.,
RA Bouquet J.M., Danks G., Poulain J., Campsteijn C., Adamski M., Cross I.,
RA Yadetie F., Muffato M., Louis A., Butcher S., Tsagkogeorga G., Konrad A.,
RA Singh S., Jensen M.F., Cong E.H., Eikeseth-Otteraa H., Noel B.,
RA Anthouard V., Porcel B.M., Kachouri-Lafond R., Nishino A., Ugolini M.,
RA Chourrout P., Nishida H., Aasland R., Huzurbazar S., Westhof E., Delsuc F.,
RA Lehrach H., Reinhardt R., Weissenbach J., Roy S.W., Artiguenave F.,
RA Postlethwait J.H., Manak J.R., Thompson E.M., Jaillon O., Du Pasquier L.,
RA Boudinot P., Liberles D.A., Volff J.N., Philippe H., Lenhard B.,
RA Roest Crollius H., Wincker P., Chourrout D.;
RT "Plasticity of animal genome architecture unmasked by rapid evolution of a
RT pelagic tunicate.";
RL Science 330:1381-1385(2010).
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 -!- 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}.
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; FN653020; CBY23283.1; -; Genomic_DNA.
DR AlphaFoldDB; E4X0I4; -.
DR InParanoid; E4X0I4; -.
DR Proteomes; UP000001307; 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:UP000001307};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU365014};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 76..360
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
SQ SEQUENCE 416 AA; 47555 MW; 7A13606E5B99FE28 CRC64;
MLTRTLRKAV RPLVTSVPRS DKFHPSTQSE FINELHMIDP MEIERLPVYR VMDRSGKILR
ENQDPKFTKE QCVKMYKAMI KTNEFDRVMY DAQRQGRVSF YMTNYGEEAA QIGSIAALNP
DDLVYAQYRE AGVIFYRGFT YQQACDQCYG NVDDKGAGRQ MPVHYGSREL DYVTISSPLT
TQLPQAAGSA FALRRAGEKR VVMCYFGEGS ASEGDAHAAF NFAATLNCPV IFFCRNNGFA
ISTPVEDQYN GDGIASRAPG YGMMTIRVDG NDLMAVFNAT VKAREIALSE NRPILIEAIT
YRQGHHSTSD DSSRYRSVDE VNMWQKTDHP ISRFRQYMMT QGWWSMEEDA ALQKSLKKDV
LIFPLVTAEK KKKPSIESMF DDVYDVLTPE LERQKAELMD HLKQYGKHYN MDQFVK
//
