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Database: UniProt
Entry: A0A3E2YP89_9ACTN
LinkDB: A0A3E2YP89_9ACTN
Original site: A0A3E2YP89_9ACTN 
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
//
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