ID A0A177HVG6_9ACTN Unreviewed; 407 AA.
AC A0A177HVG6;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=3-methyl-2-oxobutanoate dehydrogenase subunit alpha {ECO:0000313|EMBL:OAH14932.1};
DE EC=1.2.4.4 {ECO:0000313|EMBL:OAH14932.1};
GN Name=bkdA_2 {ECO:0000313|EMBL:OAH14932.1};
GN ORFNames=STSP_17690 {ECO:0000313|EMBL:OAH14932.1};
OS Streptomyces jeddahensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1716141 {ECO:0000313|EMBL:OAH14932.1, ECO:0000313|Proteomes:UP000077381};
RN [1] {ECO:0000313|EMBL:OAH14932.1, ECO:0000313|Proteomes:UP000077381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G25(2015) {ECO:0000313|Proteomes:UP000077381};
RA Poehlein A., Roettig A., Hiessl S., Hauschild P., Schauer J., Madkour M.H.,
RA Al-Ansari A.M., Almakishah N.H., Steinbuechel A., Daniel R.;
RT "Genome sequence of Streptomyces sp. G25.";
RL Submitted (DEC-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:OAH14932.1}.
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DR EMBL; LOHS01000053; OAH14932.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A177HVG6; -.
DR STRING; 1716141.STSP_17690; -.
DR PATRIC; fig|1716141.3.peg.1854; -.
DR Proteomes; UP000077381; 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:OAH14932.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000077381}.
FT DOMAIN 70..347
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 381..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..407
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 407 AA; 44136 MW; 90F9AF14CF90E561 CRC64;
MKSRSLTVMD QRGAYRPAPP PAWQPRTDPA PLLPDAEPYR VLGTEAARKA EPGLLRRLYA
ELVRGRRYNA QATALTKQGR LAVYPSSTGQ EACQVAAALA LEDRDWLFPS YRDTLAAIAR
GLDPVQALSL LRGDWHTGYD PREHRIAPLC TPLATQLPHA VGLAHAARLK GDDVVALAMV
GDGGTSEGDF HEALNFAAVW QAPVVFLVQN NGFAISVPLA KQTAAPSLAH KAVGYGMPGR
LVDGNDAVAL HEVLTDAVRH ARAGGGPTLV EAVTYRIDAH TNADDATRYR HDEEVEAWRR
HDPIALVERE LTERGLLDED AVREARENAE AMAADLRARM NQEPRLDPMD LFAHVYAEPT
SQLHEQAAQL RAELAAEAPD IPDIADTPDT AGTTPDIADT TLKGTGR
//
