ID A0A0K2RNH1_9MICC Unreviewed; 386 AA.
AC A0A0K2RNH1;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=AHiyo8_46810 {ECO:0000313|EMBL:BAS16378.1};
OS Arthrobacter sp. Hiyo8.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1588023 {ECO:0000313|EMBL:BAS16378.1, ECO:0000313|Proteomes:UP000060353};
RN [1] {ECO:0000313|Proteomes:UP000060353}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hiyo8 {ECO:0000313|Proteomes:UP000060353};
RA Hiraoka S., Machiyama A., Iwasaki W.;
RT "Microbial genome analysis of tsunami-affected soil.";
RL Submitted (FEB-2015) 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; AP014719; BAS16378.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K2RNH1; -.
DR STRING; 1588023.AHiyo8_46810; -.
DR KEGG; arh:AHiyo8_46810; -.
DR PATRIC; fig|1588023.3.peg.4883; -.
DR Proteomes; UP000060353; 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};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU365014}.
FT DOMAIN 88..355
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 386 AA; 41950 MW; BFB13F57A494D18E CRC64;
MTISADHEAQ GLADARPDDT EANDQASEVR RKFGISVEDY MLPARHQIQM VDPSGVLKPE
AEQGTEPGHE YPIPGDAELM AAYEQLVVGR RVNDQNSALV RQGRMAVYPS SHGQEACQVA
AALCLREGDW LFPTYRDAVA VMSRGVDPVE TMTIFRGDWH GGYDPTKHKV GIQCTPLTTQ
LLHAVGVAHA AKLRGEDTVV LAMCGDGATS EGDFHEALNF AAVFHLPVIF FVQNNKYAIS
VPLSQQSVAP SLAHKAVGYG MAGERVDGND LVALLAVLDR AVKLAREGSG PLLIEAHTYR
MQAHTNADDA TRYRQDSEVA EWTAKDPISR MTSYLTGRGL LDDDGSTRIA AKAEAVASQL
REGLGEDVPV DPQNLFRFVF STPLRN
//
