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Database: UniProt
Entry: W7F3V2_PLAF8
LinkDB: W7F3V2_PLAF8
Original site: W7F3V2_PLAF8 
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
//
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