ID A0A0F0LHY2_9MICO Unreviewed; 369 AA.
AC A0A0F0LHY2;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=3-methyl-2-oxobutanoate dehydrogenase subunit alpha {ECO:0000313|EMBL:KJL32822.1};
DE EC=1.2.4.4 {ECO:0000313|EMBL:KJL32822.1};
GN Name=bkdA_1 {ECO:0000313|EMBL:KJL32822.1};
GN ORFNames=RS83_00194 {ECO:0000313|EMBL:KJL32822.1};
OS Microbacterium oxydans.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=82380 {ECO:0000313|EMBL:KJL32822.1, ECO:0000313|Proteomes:UP000033640};
RN [1] {ECO:0000313|EMBL:KJL32822.1, ECO:0000313|Proteomes:UP000033640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BEL4b {ECO:0000313|EMBL:KJL32822.1,
RC ECO:0000313|Proteomes:UP000033640};
RA Corretto E.;
RT "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT metal contaminated environments.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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:KJL32822.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JYIW01000013; KJL32822.1; -; Genomic_DNA.
DR RefSeq; WP_045277668.1; NZ_JYIW01000013.1.
DR AlphaFoldDB; A0A0F0LHY2; -.
DR PATRIC; fig|82380.11.peg.203; -.
DR OrthoDB; 9766715at2; -.
DR Proteomes; UP000033640; Unassembled WGS sequence.
DR GO; GO:0003863; F:3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR CDD; cd02000; TPP_E1_PDC_ADC_BCADC; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR InterPro; IPR001017; DH_E1.
DR InterPro; IPR017596; PdhA/BkdA.
DR InterPro; IPR029061; THDP-binding.
DR NCBIfam; TIGR03181; PDH_E1_alph_x; 1.
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 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:KJL32822.1}.
FT DOMAIN 48..311
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
SQ SEQUENCE 369 AA; 39849 MW; 0621ACF3E20A194B CRC64;
MLHTDMLPRD TAVRLIDEDG TVVADEHYAL PDTPTLLRAY RGLVEGRRIN DQAGALVRQG
RLAVYPSSHG QEACQVAASL AIADTDWLFP TYRDSVAVIA RGVDPADALV LLKGDWHSGY
DVREHRVAPQ ATPLATQLLH AVGFAQAAKH RGEDTVVLAL CGDGATSEGD FHEAMNFAAV
FHVPVVFFVQ NNEFAISVPL SRQTAAPSLA HKAIGYGMPG QRVDGNDVAA VLAVLGEAVE
RARAGGGPSL VEAHTYRMQA HTNADDDTRY RERTEVQAWA ARDPLLRLRA HLTDAGALDN
ETEAQFAAGA EQIATAMRDA LNTDTELDPE DLFRFVTTTR SSQLDEQWAL LRGEIERSES
AATHTGGAA
//
