ID A0A2S3ZYE1_ARTGL Unreviewed; 381 AA.
AC A0A2S3ZYE1;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
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=CVS27_07010 {ECO:0000313|EMBL:POH74305.1};
OS Arthrobacter glacialis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1664 {ECO:0000313|EMBL:POH74305.1, ECO:0000313|Proteomes:UP000237061};
RN [1] {ECO:0000313|EMBL:POH74305.1, ECO:0000313|Proteomes:UP000237061}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HLT2-12-2 {ECO:0000313|EMBL:POH74305.1,
RC ECO:0000313|Proteomes:UP000237061};
RA Liu Q., Xin Y.-H.;
RT "Arthrobacter sp. nov., from glaciers in China.";
RL Submitted (JAN-2018) 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}.
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:POH74305.1}.
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DR EMBL; PPXC01000004; POH74305.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S3ZYE1; -.
DR Proteomes; UP000237061; 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}; Pyruvate {ECO:0000313|EMBL:POH74305.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000237061};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU365014}.
FT DOMAIN 57..326
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
SQ SEQUENCE 381 AA; 41237 MW; 004CE64E19E1001D CRC64;
MTTHPEFLES QSYMLPSAEP VQLIAADGSE APAKQHKQYK EPYQLPEMAT MLEGYERLVV
GRRVNDQAGA LVRQGRMAVY PSSHGQEACQ VAAVMCLRRS DWLFPTYRDT VAVLGRGVAP
VEAFESLRGD WHSGFNPHDY NTANPTTPLA TQLLHAVGVA HSAKLRGEDT VVLALCGDGA
SSEGDFHEAL NFAAVFHVPV VFLIQNNQYA ISVPLIRQSV APSLAHKAVG YGMPGERVDG
NDLAALLAVL GHAVDRARNG GGPALVEAHT YRMQAHTNAD DSTRYRSDAE VAQWVPKDPL
LRVEKYLHDA GALAAADRER IAVAAEAMAK TLRDGLNAET SVDPLDLFRY VYSEPTPQLR
EQSTLLAAEL AASSATMGAS R
//
