ID A0A1B2I0F5_9PSEU Unreviewed; 358 AA.
AC A0A1B2I0F5;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
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=BBK82_41920 {ECO:0000313|EMBL:ANZ43480.1};
OS Lentzea guizhouensis.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Lentzea.
OX NCBI_TaxID=1586287 {ECO:0000313|EMBL:ANZ43480.1, ECO:0000313|Proteomes:UP000093053};
RN [1] {ECO:0000313|EMBL:ANZ43480.1, ECO:0000313|Proteomes:UP000093053}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DHS C013 {ECO:0000313|EMBL:ANZ43480.1,
RC ECO:0000313|Proteomes:UP000093053};
RA Cao C.;
RT "Complete genome sequence of the Lentzea guizhouensis DHS C013.";
RL Submitted (JUL-2016) 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|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; CP016793; ANZ43480.1; -; Genomic_DNA.
DR RefSeq; WP_065921801.1; NZ_CP016793.1.
DR AlphaFoldDB; A0A1B2I0F5; -.
DR STRING; 1586287.BBK82_41920; -.
DR KEGG; led:BBK82_41920; -.
DR OrthoDB; 9766715at2; -.
DR Proteomes; UP000093053; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR GO; GO:0016624; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor; IEA:InterPro.
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}; Pyruvate {ECO:0000313|EMBL:ANZ43480.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000093053};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU365014}.
FT DOMAIN 40..310
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
SQ SEQUENCE 358 AA; 38326 MW; 55BF30532D173934 CRC64;
MSAGQLKAAI TPARLLDEKG RLVRGAPKPD VEALAEGYRK LVFARRLNEQ CGALVRQGRL
AVYPSSRGQE ACQVACTSVL ADGDWLFPTY RDTAAIAARG VDPVEVLTLL RGDWHCGYDP
NVHKVAPQAT PLATQLLHAV GVGHAARLKG EDTVVMALCG DGATSEGDFH EACNFAAVFR
APVVFFVQNN KYAISVPLAR QSVAPSLAAK AIGYGMPGVR VDGNDLPALE KVLGEAVARA
RAGEGPTLVE ADTYRIESHT NADDASRYRA DDEVSEWLPR DPLLRVRTYL TAVGALDARR
EEEITAAAEE MAAAVRAGVG GETPVDPEEI FAHVHSTPTP QLAEQRAALR AELEFEEA
//
