ID A0A0K8Q4P7_9MICC Unreviewed; 353 AA.
AC A0A0K8Q4P7;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=AHiyo6_15330 {ECO:0000313|EMBL:GAP54968.1};
OS Arthrobacter sp. Hiyo6.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1588022 {ECO:0000313|EMBL:GAP54968.1, ECO:0000313|Proteomes:UP000037466};
RN [1] {ECO:0000313|Proteomes:UP000037466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hiyo6 {ECO:0000313|Proteomes:UP000037466};
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.
RN [2] {ECO:0000313|EMBL:GAP54968.1, ECO:0000313|Proteomes:UP000037466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hiyo6 {ECO:0000313|EMBL:GAP54968.1,
RC ECO:0000313|Proteomes:UP000037466};
RX PubMed=26764021; DOI=10.1186/s12864-016-2380-4;
RA Hiraoka S., Machiyama A., Ijichi M., Inoue K., Oshima K., Hattori M.,
RA Yoshizawa S., Kogure K., Iwasaki W.;
RT "Genomic and metagenomic analysis of microbes in a soil environment
RT affected by the 2011 Great East Japan Earthquake tsunami.";
RL BMC Genomics 17:53-53(2016).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAP54968.1}.
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DR EMBL; BBUE01000141; GAP54968.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K8Q4P7; -.
DR Proteomes; UP000037466; Unassembled WGS sequence.
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 30..308
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 353 AA; 37787 MW; 3FEE707090A50C17 CRC64;
MDPLPSSEPR PLNAPEPGPP TSEQLRELYS LMAAVRHLDT SAVAWQRQGI IPGYAPELGQ
EAAQVGSGYA VDISRDFVFP TYREMGVARA MGVDMVAYMS THKATWHGGL YDPLKSRLAP
IQAVVAGSVL HAVGWAHGQT LSANGNSDLG AALTYFGDGA SSQGDIHEAM NFAAVMNAPV
VFFVQNNGWA ISVPTERQVA GGSVAARAAG YGMPALRIDG NDVVAVFQST RRALAHCRSG
NGPVLIEAMT YRRGPHSTSD DPGRYRSLDA ERADAGADPL DRFRQRLLAD GIADEQFFKN
AAAAARAEEE QIRTGLQALG PRPGAEMFDL VFQETTPALQ AQAASWREES EHV
//
