ID A5JZB6_PLAVS Unreviewed; 431 AA.
AC A5JZB6;
DT 10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 10-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 76.
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=PVX_122460 {ECO:0000313|EMBL:EDL47327.1};
OS Plasmodium vivax (strain Salvador I).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX NCBI_TaxID=126793 {ECO:0000313|EMBL:EDL47327.1, ECO:0000313|Proteomes:UP000008333};
RN [1] {ECO:0000313|EMBL:EDL47327.1, ECO:0000313|Proteomes:UP000008333}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Salvador I {ECO:0000313|EMBL:EDL47327.1,
RC ECO:0000313|Proteomes:UP000008333};
RX PubMed=18843361; DOI=10.1038/nature07327;
RA Carlton J.M., Adams J.H., Silva J.C., Bidwell S.L., Lorenzi H., Caler E.,
RA Crabtree J., Angiuoli S.V., Merino E.F., Amedeo P., Cheng Q., Coulson R.M.,
RA Crabb B.S., Del Portillo H.A., Essien K., Feldblyum T.V.,
RA Fernandez-Becerra C., Gilson P.R., Gueye A.H., Guo X., Kang'a S.,
RA Kooij T.W., Korsinczky M., Meyer E.V., Nene V., Paulsen I., White O.,
RA Ralph S.A., Ren Q., Sargeant T.J., Salzberg S.L., Stoeckert C.J.,
RA Sullivan S.A., Yamamoto M.M., Hoffman S.L., Wortman J.R., Gardner M.J.,
RA Galinski M.R., Barnwell J.W., Fraser-Liggett C.M.;
RT "Comparative genomics of the neglected human malaria parasite Plasmodium
RT vivax.";
RL Nature 455:757-763(2008).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EDL47327.1}.
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DR EMBL; AAKM01000001; EDL47327.1; -; Genomic_DNA.
DR RefSeq; XP_001617054.1; XM_001617004.1.
DR AlphaFoldDB; A5JZB6; -.
DR STRING; 126793.A5JZB6; -.
DR EnsemblProtists; EDL47327; EDL47327; PVX_122460.
DR GeneID; 5476713; -.
DR KEGG; pvx:PVX_122460; -.
DR VEuPathDB; PlasmoDB:PVX_122460; -.
DR InParanoid; A5JZB6; -.
DR OMA; EMFEGVY; -.
DR PhylomeDB; A5JZB6; -.
DR Proteomes; UP000008333; Chromosome 14.
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:UP000008333};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU365014}.
FT DOMAIN 91..386
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
SQ SEQUENCE 431 AA; 49651 MW; 0C97CBC0FDCC53CC CRC64;
MRNVVQKYLC RKNNFPGFCS KRNVCTLSQK KNLSAYKIYT DGLLHSEFST ELKTTNEVNR
LPIFRVLDTE GNLLDGHNAP FEEEEIVKLY KQMVEFSIWD EIFYGIQRQG RISFYIVNDG
EEGIQFGLGK VLTPDDHLYC QYRETGILLS RGFDYADIIN QLFGNKYDEG KGRQMCICYT
SKKLNIHTIT TPLASQLSHA AGCGYALKLK NEKAVAATFC GDGSSSEGDF YAALNFAAVR
ESQTMFICKN NLYAISTSIK DQYRGDGVAP RALALGIESV RVDGNDLFAT YLAAKKMREI
CTEESKPVFM EFMAYRYGHH STSDDSSLYR PKEENDAWKK EGVHPISRLF LYLKNKKLYT
DKDDELHRKA IKEKVLKELK KHESIKRYNI VGGLFENVYH EEDWNLKEQR ESFEQFFKQH
KGCYDTSKFE G
//
