ID W7F3V2_PLAF8 Unreviewed; 429 AA.
AC W7F3V2;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 31.
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=PFBG_04397 {ECO:0000313|EMBL:EUR66817.1};
OS Plasmodium falciparum (isolate 7G8).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=57266 {ECO:0000313|EMBL:EUR66817.1, ECO:0000313|Proteomes:UP000030688};
RN [1] {ECO:0000313|Proteomes:UP000030688}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7G8 {ECO:0000313|Proteomes:UP000030688};
RG The Broad Institute Genome Sequencing Platform;
RA Volkman S.K., Daily J.P., Sarr O., Ndiaye D., Ndir O., Mboup S., Lukens A.,
RA Stange-Thomann N., Mauceli E., Gnerre S., Jaffe D., Zainoun J.,
RA Wiegand R.C., Birren B., Galagan J., Lander E., Wirth D.F.;
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EUR66817.1, ECO:0000313|Proteomes:UP000030688}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7G8 {ECO:0000313|EMBL:EUR66817.1,
RC ECO:0000313|Proteomes:UP000030688};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Neafsey D., Cheeseman I., Volkman S., Adams J., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Plasmodium falciparum 7G8.";
RL Submitted (FEB-2013) 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|RuleBase:RU365014}.
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DR EMBL; KE123632; EUR66817.1; -; Genomic_DNA.
DR AlphaFoldDB; W7F3V2; -.
DR EnsemblProtists; EUR66817; EUR66817; PFBG_04397.
DR VEuPathDB; PlasmoDB:Pf7G8_130017100; -.
DR Proteomes; UP000030688; 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 Thiamine pyrophosphate {ECO:0000256|RuleBase:RU365014}.
FT DOMAIN 91..384
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
SQ SEQUENCE 429 AA; 49839 MW; DBFC2A01A98F9AD3 CRC64;
MRNIVQKYLQ RNSTKLFNRT SVFNLYKKCN FSGYKIYSDG LVHSEFSTEL KTVNEVIKMP
IYRILDTNGH LLDGHEAPFK DEEVLKIYKD MVEFSIWDEI FYGIQRQGRI SFYIVNEGEE
GLQFGMGKAL SVDDHLYCQY RETGVLLSRG FTYTDILNQL FGTKYDEGKG RQMCICYTKK
DLNIHTITTP LGSQLSHAAG CGYALKLKNQ KAVAVTYCGD GSSSEGDFYA ALNFASVRQS
QTMFVCKNNL YAISTSIKDQ YRGDGIAPRA LALGIESIRV DGNDLFASYL ATKKLRDICI
QESKPVFIEF MSYRYGHHST SDDSSLYRPK EENEAWRQEG VHPINRIFLY LKNKNLYSEK
EDQEHRKSVK ENVLKELKKY ESVKRYNIVG GLFEDVYHEE DWNIKEQREN FEQFFKENKH
NYDTSKFEP
//