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Database: UniProt
Entry: A0A0M2H1D0_9MICO
LinkDB: A0A0M2H1D0_9MICO
Original site: A0A0M2H1D0_9MICO 
ID   A0A0M2H1D0_9MICO        Unreviewed;       340 AA.
AC   A0A0M2H1D0;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=3-methyl-2-oxobutanoate dehydrogenase subunit beta {ECO:0000313|EMBL:KJL40218.1};
DE            EC=1.2.4.4 {ECO:0000313|EMBL:KJL40218.1};
GN   Name=bkdB_1 {ECO:0000313|EMBL:KJL40218.1};
GN   ORFNames=RS82_03544 {ECO:0000313|EMBL:KJL40218.1};
OS   Microbacterium trichothecenolyticum.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=69370 {ECO:0000313|EMBL:KJL40218.1, ECO:0000313|Proteomes:UP000034098};
RN   [1] {ECO:0000313|EMBL:KJL40218.1, ECO:0000313|Proteomes:UP000034098}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 8608 {ECO:0000313|EMBL:KJL40218.1,
RC   ECO:0000313|Proteomes:UP000034098};
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:KJL40218.1}.
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DR   EMBL; JYJA01000040; KJL40218.1; -; Genomic_DNA.
DR   RefSeq; WP_045301838.1; NZ_JYJA01000040.1.
DR   AlphaFoldDB; A0A0M2H1D0; -.
DR   PATRIC; fig|69370.6.peg.3606; -.
DR   OrthoDB; 3457658at2; -.
DR   Proteomes; UP000034098; 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; cd07036; TPP_PYR_E1-PDHc-beta_like; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   InterPro; IPR033248; Transketolase_C.
DR   PANTHER; PTHR42980:SF1; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT BETA, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR42980; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT BETA-RELATED; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   Pfam; PF02780; Transketolase_C; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000313|EMBL:KJL40218.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034098}.
FT   DOMAIN          20..195
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   340 AA;  36362 MW;  7BAF5B6FE2AC8359 CRC64;
     MSTPTTTATA QAAAPAVQTL PFSRAINAGL RAALAGSDRV LLMGEDIGKL GGVFRVTEGL
     QAEFGEQRVL DTPLAESGLV GTAIGLAMAG FRPVVEIQFD GFVFPAFDQI TTQLAKLTNR
     HEGALQMPVV IRIPYGGHIG AVEHHQESPE AYFTHTAGLR VVSPSTPNDG YWMIQDAISS
     PDPVIFLEPK SKYWQKGEVD TSARALPLHA SRVVRRGTDI TLVGHGAMVT TMLQAAVLAE
     AEGTSIEVID LRSLSPLDYG PILDSVRRTG RMVYAQEAPG FTSLGSEVAA TVMERAFYAL
     EAPVLRVSGF DTPFPPAKLE GAYLPDADRI LEAVDRSLAY
//
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