ID A0A132MMT3_9ACTN Unreviewed; 371 AA.
AC A0A132MMT3;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Branched-chain alpha-keto acid dehydrogenase {ECO:0000313|EMBL:KWW99170.1};
DE EC=1.2.4.4 {ECO:0000313|EMBL:KWW99170.1};
GN ORFNames=LI90_804 {ECO:0000313|EMBL:KWW99170.1};
OS Carbonactinospora thermoautotrophica.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Carbonactinosporaceae; Carbonactinospora.
OX NCBI_TaxID=1469144 {ECO:0000313|EMBL:KWW99170.1, ECO:0000313|Proteomes:UP000070188};
RN [1] {ECO:0000313|Proteomes:UP000070188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H1 {ECO:0000313|Proteomes:UP000070188};
RA MacKellar D.C., Lieber L., Norman J., Bolger A., Tobin C., Murray J.W.,
RA Chang R., Ford T., Nguyen P.Q., Woodward J., Permingeat H., Joshi N.S.,
RA Silver P.A., Usadel B., Rutherford A.W., Friesen M., Prell J.;
RT "Physiological reanalysis, assessment of diazotrophy, and genome sequences
RT of multiple isolates of Streptomyces thermoautotrophicus.";
RL Submitted (APR-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:KWW99170.1}.
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DR EMBL; LAXD01000001; KWW99170.1; -; Genomic_DNA.
DR RefSeq; WP_066884287.1; NZ_LAXD01000001.1.
DR AlphaFoldDB; A0A132MMT3; -.
DR STRING; 1469144.LI90_804; -.
DR PATRIC; fig|1469144.10.peg.918; -.
DR OrthoDB; 9766715at2; -.
DR Proteomes; UP000070188; 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:KWW99170.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000070188}.
FT DOMAIN 42..312
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
SQ SEQUENCE 371 AA; 40329 MW; 141705CCF72630B3 CRC64;
MTVLAETSHP LPLEPVQLLD EHGDPADGQV LPPAAQRLQM YRRLVVGRRF DRQAAALTRQ
GRLAVYPSSN GQEACQVGAV LAVRDTDWLF PTYRESVALV TRGIDPVEVL TLLRGDWHCG
YDPYHHRTAP QCTPLATQAL HAVGLAHAAR LAGDDVVALA FVGDGATSEG DCHEALNFAA
VYRAPVVFFV QNNQYAISVP LAKQTAASSL AHKAIGYGMP GRRVDGNDVL AVYRVVRDAV
EHARAGQGPT LVEAVTYRMD AHTNADDASR YRTSAEVDAW RKRDPITRLE RHLRAVGVLD
DAGVAEIAAE AEDFAARLRE RMNTDPVLDP MEMFRHVYAE PTPQLREQAA LLAAELAAEA
EAPVGGVEAR A
//
