ID I3TTW0_TISMK Unreviewed; 410 AA.
AC I3TTW0;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 54.
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 OrderedLocusNames=TMO_b0190 {ECO:0000313|EMBL:AFK56198.1};
OS Tistrella mobilis (strain KA081020-065).
OG Plasmid pTM2 {ECO:0000313|EMBL:AFK56198.1,
OG ECO:0000313|Proteomes:UP000005258}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Geminicoccales;
OC Geminicoccaceae; Tistrella.
OX NCBI_TaxID=1110502 {ECO:0000313|EMBL:AFK56198.1, ECO:0000313|Proteomes:UP000005258};
RN [1] {ECO:0000313|EMBL:AFK56198.1, ECO:0000313|Proteomes:UP000005258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KA081020-065 {ECO:0000313|Proteomes:UP000005258};
RC PLASMID=Plasmid pTM2 {ECO:0000313|Proteomes:UP000005258};
RX PubMed=22458477; DOI=10.1021/ja301735a;
RA Xu Y., Kersten R.D., Nam S.J., Lu L., Al-Suwailem A.M., Zheng H.,
RA Fenical W., Dorrestein P.C., Moore B.S., Qian P.Y.;
RT "Bacterial biosynthesis and maturation of the didemnin anti-cancer
RT agents.";
RL J. Am. Chem. Soc. 134:8625-8632(2012).
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|ARBA:ARBA00001964,
CC ECO:0000256|RuleBase:RU365014};
CC -!- SIMILARITY: Belongs to the BCKDHA family.
CC {ECO:0000256|RuleBase:RU365014}.
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DR EMBL; CP003238; AFK56198.1; -; Genomic_DNA.
DR RefSeq; WP_014752951.1; NC_017966.1.
DR AlphaFoldDB; I3TTW0; -.
DR KEGG; tmo:TMO_b0190; -.
DR PATRIC; fig|1110502.3.peg.4448; -.
DR HOGENOM; CLU_029393_1_0_5; -.
DR Proteomes; UP000005258; Plasmid pTM2.
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; IPR022593; Oxoisoval_DH_suAlpha_N_dom.
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 Pfam; PF12573; OxoDH_E1alpha_N; 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}; Plasmid {ECO:0000313|EMBL:AFK56198.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005258};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU365014}.
FT DOMAIN 6..45
FT /note="2-oxoisovalerate dehydrogenase E1 alpha subunit N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12573"
FT DOMAIN 83..379
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 410 AA; 44749 MW; 7612077EAC253A00 CRC64;
MSTSEHLSLH VPEPAVRPGD TPDFSTVKIP KAGAVPRPEV DADPEQMRDL AFSIIRVLNR
NGEAVGPWAG ALTDDELLDG LRHMMTLRAF DARMLIAQRQ GKTSFYMQHL GEEAVSCAFR
KALVDGDMNF PTYRQAGLLI AGGYSMVDMM CQIYSNARDP LKGRQLPVMY SSREHGFFTI
SGNLATQFVQ AVGWAMASAI RNDTKIAAAW IGDGSTAESD FHAALVFAST YKAPVVLNVV
NNQWAISTFQ GIARGGSGTF AARGLGFGIP SLRVDGNDYL AVHAVAKWAA ERARRNLGPT
LIEYVTYRVG AHSTSDDPSA YRPKAESTAW PLGDPVIRLK NHLITRGVWS EDRHKQTEAE
ILDTVIAAQK EAESHGTLHA GAKPSARDMF DGVFAEMPAH LRRQRQQAGV
//
