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Database: UniProt
Entry: A0A0F0L1K5_9MICO
LinkDB: A0A0F0L1K5_9MICO
Original site: A0A0F0L1K5_9MICO 
ID   A0A0F0L1K5_9MICO        Unreviewed;       380 AA.
AC   A0A0F0L1K5;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=3-methyl-2-oxobutanoate dehydrogenase subunit alpha {ECO:0000313|EMBL:KJL27013.1};
DE            EC=1.2.4.4 {ECO:0000313|EMBL:KJL27013.1};
GN   Name=bkdA_1 {ECO:0000313|EMBL:KJL27013.1};
GN   ORFNames=RL72_00752 {ECO:0000313|EMBL:KJL27013.1};
OS   Microbacterium azadirachtae.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=582680 {ECO:0000313|EMBL:KJL27013.1, ECO:0000313|Proteomes:UP000033448};
RN   [1] {ECO:0000313|EMBL:KJL27013.1, ECO:0000313|Proteomes:UP000033448}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23848 {ECO:0000313|EMBL:KJL27013.1,
RC   ECO:0000313|Proteomes:UP000033448};
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:KJL27013.1}.
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DR   EMBL; JYIT01000059; KJL27013.1; -; Genomic_DNA.
DR   RefSeq; WP_045249485.1; NZ_JYIT01000059.1.
DR   AlphaFoldDB; A0A0F0L1K5; -.
DR   PATRIC; fig|582680.7.peg.779; -.
DR   Proteomes; UP000033448; 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:KJL27013.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033448}.
FT   DOMAIN          61..324
FT                   /note="Dehydrogenase E1 component"
FT                   /evidence="ECO:0000259|Pfam:PF00676"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   380 AA;  41370 MW;  F7BBE5D1D46FC783 CRC64;
     MQQTTPAMSP PRDEDPRALL PRDEPVRLID ETGAAHGDAD YPMPADELLG RAYRGLVEGR
     RINDQANALV RQGRLAVYPS SHGQEACQIA ASMVLGEHDW LFPTYRDSVA VIARGVSPAD
     AMVLLKGDWH SGYDPQEHRV APQTTPLATQ LLHAVGFAQA AKHRGEDTVV LALCGDGSTS
     EGDFHEALNF AAVFHVPVVF FVQNNEFAIS VPLSRQTAAP SLAHKAIGYG VPGQRVDGND
     VAALLAVLGE AVDRARAGGG PSLIEAHTYR MQAHTNADDD TRYRERAEVQ AWVAKDPLTR
     LRAHLTARGL LDDAREQELA DGAETIAAAL RDALNTDADL DPEDLFRFVH SARTPQLQEQ
     WHRLRDELER SAASTEGGDR
//
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