ID Q4QC52_LEIMA Unreviewed; 479 AA.
AC Q4QC52;
DT 19-JUL-2005, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2005, sequence version 1.
DT 27-MAR-2024, entry version 91.
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=LMJF_21_1430 {ECO:0000313|EMBL:CAJ04806.1};
OS Leishmania major.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=5664 {ECO:0000313|EMBL:CAJ04806.1, ECO:0000313|Proteomes:UP000000542};
RN [1] {ECO:0000313|EMBL:CAJ04806.1, ECO:0000313|Proteomes:UP000000542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/IL/81/Friedlin {ECO:0000313|Proteomes:UP000000542};
RX PubMed=16020728; DOI=10.1126/science.1112680;
RA Ivens A.C., Peacock C.S., Worthey E.A., Murphy L., Aggarwal G.,
RA Berriman M., Sisk E., Rajandream M.A., Adlem E., Aert R., Anupama A.,
RA Apostolou Z., Attipoe P., Bason N., Bauser C., Beck A., Beverley S.M.,
RA Bianchettin G., Borzym K., Bothe G., Bruschi C.V., Collins M., Cadag E.,
RA Ciarloni L., Clayton C., Coulson R.M., Cronin A., Cruz A.K., Davies R.M.,
RA De Gaudenzi J., Dobson D.E., Duesterhoeft A., Fazelina G., Fosker N.,
RA Frasch A.C., Fraser A., Fuchs M., Gabel C., Goble A., Goffeau A.,
RA Harris D., Hertz-Fowler C., Hilbert H., Horn D., Huang Y., Klages S.,
RA Knights A., Kube M., Larke N., Litvin L., Lord A., Louie T., Marra M.,
RA Masuy D., Matthews K., Michaeli S., Mottram J.C., Muller-Auer S.,
RA Munden H., Nelson S., Norbertczak H., Oliver K., O'neil S., Pentony M.,
RA Pohl T.M., Price C., Purnelle B., Quail M.A., Rabbinowitsch E.,
RA Reinhardt R., Rieger M., Rinta J., Robben J., Robertson L., Ruiz J.C.,
RA Rutter S., Saunders D., Schafer M., Schein J., Schwartz D.C., Seeger K.,
RA Seyler A., Sharp S., Shin H., Sivam D., Squares R., Squares S., Tosato V.,
RA Vogt C., Volckaert G., Wambutt R., Warren T., Wedler H., Woodward J.,
RA Zhou S., Zimmermann W., Smith D.F., Blackwell J.M., Stuart K.D.,
RA Barrell B., Myler P.J.;
RT "The genome of the kinetoplastid parasite, Leishmania major.";
RL Science 309:436-442(2005).
RN [2] {ECO:0000313|EMBL:CAJ04806.1, ECO:0000313|Proteomes:UP000000542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/IL/81/Friedlin {ECO:0000313|Proteomes:UP000000542};
RX PubMed=22038252; DOI=10.1101/gr.122945.111;
RA Rogers M.B., Hilley J.D., Dickens N.J., Wilkes J., Bates P.A.,
RA Depledge D.P., Harris D., Her Y., Herzyk P., Imamura H., Otto T.D.,
RA Sanders M., Seeger K., Dujardin J.C., Berriman M., Smith D.F.,
RA Hertz-Fowler C., Mottram J.C.;
RT "Chromosome and gene copy number variation allow major structural change
RT between species and strains of Leishmania.";
RL Genome Res. 21:2129-2142(2011).
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; FR796417; CAJ04806.1; -; Genomic_DNA.
DR RefSeq; XP_001683096.1; XM_001683044.1.
DR AlphaFoldDB; Q4QC52; -.
DR STRING; 5664.Q4QC52; -.
DR EnsemblProtists; CAJ04806; CAJ04806; LMJF_21_1430.
DR GeneID; 5651703; -.
DR KEGG; lma:LMJF_21_1430; -.
DR VEuPathDB; TriTrypDB:LmjF.21.1430; -.
DR VEuPathDB; TriTrypDB:LMJFC_210024400; -.
DR VEuPathDB; TriTrypDB:LMJLV39_210022400; -.
DR VEuPathDB; TriTrypDB:LMJSD75_210022600; -.
DR eggNOG; KOG1182; Eukaryota.
DR HOGENOM; CLU_029393_1_2_1; -.
DR InParanoid; Q4QC52; -.
DR OMA; DWHTGYD; -.
DR Proteomes; UP000000542; Chromosome 21.
DR GO; GO:0005737; C:cytoplasm; ISO:GeneDB.
DR GO; GO:0005947; C:mitochondrial alpha-ketoglutarate dehydrogenase complex; IBA:GO_Central.
DR GO; GO:0003863; F:3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity; IEA:UniProtKB-EC.
DR GO; GO:0009083; P:branched-chain amino acid catabolic process; IBA:GO_Central.
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:UP000000542};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU365014}.
FT DOMAIN 126..434
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
SQ SEQUENCE 479 AA; 53314 MW; 35B7BA81C363B0FF CRC64;
MFHISRAVRC NALATAIAGR TSLSDAIRQV QKVWNLDFKD GPVITSTLAF NDEPDPAAPI
FHVLDLQGRV FVEDKADSRA AAATPSTVNE AGKMESQSAD VGEVFRYHAE DEMSVITREV
AQGMMSAMLT HNTMDKIMLE AQRQGRISFY MTMFGEEAAV IGAAAGLASN DELFAQYREA
GILTYRGYTI PEFIAQCMGN CECDAKGRQM PIHYGSKRLH AQMVSSPLAT QIPHGAGAGY
AFRLENQALE RRLPAGTLLS TIPEARICAT FFGEGAASEG DFHAGLNFAS TVGSHTLFFV
RNNGYAISTP THSQYMGDGI LSRAVGYGIP AARVDGLDAL AVYHTVRKAR EMILNSHRPV
LVEALTYRLS HHSTSDDSTA YRSRDEIEHF AETFSPIERF EHFVTARGWW TPEQSREVVE
RTRSEVLSEL RRQEKLPAWP VSTLCDDVFE HLTPELERQR TQLVEHYQAH RSIYDQEKL
//
