ID F0W9Z2_9STRA Unreviewed; 685 AA.
AC F0W9Z2;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 37.
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 Name=AlNc14C42G3548 {ECO:0000313|EMBL:CCA17960.1};
GN ORFNames=ALNC14_041030 {ECO:0000313|EMBL:CCA17960.1};
OS Albugo laibachii Nc14.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Albuginales; Albuginaceae; Albugo.
OX NCBI_TaxID=890382 {ECO:0000313|EMBL:CCA17960.1};
RN [1] {ECO:0000313|EMBL:CCA17960.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21750662; DOI=10.1371/journal.pbio.1001094;
RA Kemen E., Gardiner A., Schultz-Larsen T., Kemen A.C., Balmuth A.L.,
RA Robert-Seilaniantz A., Bailey K., Holub E., Studholme D.J., Maclean D.,
RA Jones J.D.;
RT "Gene gain and loss during evolution of obligate parasitism in the white
RT rust pathogen of Arabidopsis thaliana.";
RL PLoS Biol. 9:e1001094-e1001094(2011).
RN [2] {ECO:0000313|EMBL:CCA17960.1}
RP NUCLEOTIDE SEQUENCE.
RA MacLean D.;
RL Submitted (FEB-2011) 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; FR824087; CCA17960.1; -; Genomic_DNA.
DR AlphaFoldDB; F0W9Z2; -.
DR EnsemblProtists; CCA17960; CCA17960; ALNC14_041030.
DR HOGENOM; CLU_019919_1_0_1; -.
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 Coiled coil {ECO:0000256|SAM:Coils};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU365014};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU365014}.
FT DOMAIN 48..340
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
FT REGION 326..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 556..578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 469..496
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 685 AA; 77535 MW; 33DC3A29BCF20B53 CRC64;
MFRVPLPHES AKFEEDVGTP PLLDLEGNLT DTTSTPTMKQ NTTVQSYRKM ICMKTMDSIL
YDAQRQGRIS FYMTCYGEEA VSFGTAAALN TSDVVFAQYR EPGVLMWRGF HYQDFADQCF
GNNDGHGKGR QMPVHYGSKP LSYHTISSPL ATQIPHAVGA AYALKLSRED RIAVCYLGEG
AASEGDFHAG LNAAATRDCP VLFVVRNNGY AISTPRSDQY RGDGIATRGI GYGIAFARVD
GNDLLAVYET TTRARKFILE NNKPMMLELM CYRTGHHSTS DDSTRYRPDI EMSSSKECFD
PILRVKRYLI KHGWWSEAQD SILQETERNK MSKKRKQKND DRQQRKKKSG DAIMYKDLAS
KKEHVRELAK GRRWKQIKQL YGEKMVIRAK NCTKKKWIGY VHKCIKDLEK TLSKQTPAFL
AMQILEQNGY GAVKSSIAPI DNESKMISSG TTERLDGEES RGAEEVAQLR LTEEQRMKIE
EKRKEALARR KELSNKLNPA PRNTCSEKPQ EVTHFALDSL EQELQAATEI FQSDISDHSG
DVLEKSYREI VHYSVSTEEA HQPVPTTDDE SEKPQALPTR DTPLAVSLSQ EILAATAIIE
WEEQQEQDHR NTCYGSSLHI VPITDDEMEL LPPDPSNDMG LSINPMRGVW RQTRKKISRP
PNLEKARGMS KTTLHTCKLS SITNF
//
