ID A0A3E2YP89_9ACTN Unreviewed; 400 AA.
AC A0A3E2YP89;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=3-methyl-2-oxobutanoate dehydrogenase subunit alpha {ECO:0000313|EMBL:RGC67554.1};
DE EC=1.2.4.4 {ECO:0000313|EMBL:RGC67554.1};
GN Name=bkdA2 {ECO:0000313|EMBL:RGC67554.1};
GN ORFNames=C5N14_17395 {ECO:0000313|EMBL:RGC67554.1};
OS Micromonospora sp. MW-13.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=2094022 {ECO:0000313|EMBL:RGC67554.1, ECO:0000313|Proteomes:UP000258607};
RN [1] {ECO:0000313|EMBL:RGC67554.1, ECO:0000313|Proteomes:UP000258607}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MW13 {ECO:0000313|EMBL:RGC67554.1,
RC ECO:0000313|Proteomes:UP000258607};
RA Jahanshah G., Miess H., Busche T., Ruckert C., Kalinowski J.,
RA Rokni-Zadeh H., Gross H.;
RT "Draft Genome Sequence of Micromonospora sp. MW-13, a Bacterical Strain
RT Isolated from the Rhizosphere of Wheat in Iran with antibacterial and
RT possibly plant growth promotion properties.";
RL Submitted (MAY-2018) 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:RGC67554.1}.
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DR EMBL; QKKX01000033; RGC67554.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3E2YP89; -.
DR Proteomes; UP000258607; 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:RGC67554.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000258607}.
FT DOMAIN 75..359
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 400 AA; 43333 MW; 31C391001617D5B2 CRC64;
MTTTPQAVRR ASPRTRPPAK KKPTKAPAGE QATTDPAAAL LPQPEPVRLL DPDGTPLPAR
ADYPEPPVEA LRELYRRMVV GRRFDTQATA LTKQGRLAVY PSARGQEACQ VGAVLAVRDT
DWVFPTYRES MALVSRGIDP VEVLTLLRGD WHCGYDPAQR HTAPQCTPLA TQCVHAAGLA
YGEAHQGRDT VALAFVGDGA TSEGDFHEGV NFAAVFKAPV VFFVQNNKYA ISVPLSRQTA
APSLAYKGVG YGVPSEQVDG NDPVAVLAVL TRAVEHARSG QGPFLVEAHT YRMEPHTNAD
DATRYRDAAE VDTWRDRDPV ARLEAYLRTR GALDDAAVAA IADEAEAYAA DLRARMNAQP
AVDPLSLFDH VYAEPTPQLV EQRELVRTEL AAAAEPEDGR
//