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Database: UniProt
Entry: A0A1E7KDV4_9ACTN
LinkDB: A0A1E7KDV4_9ACTN
Original site: A0A1E7KDV4_9ACTN 
ID   A0A1E7KDV4_9ACTN        Unreviewed;       334 AA.
AC   A0A1E7KDV4;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=2-oxoisovalerate dehydrogenase {ECO:0000313|EMBL:OEV02087.1};
GN   ORFNames=AN217_02140 {ECO:0000313|EMBL:OEV02087.1};
OS   Streptomyces qinglanensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=943816 {ECO:0000313|EMBL:OEV02087.1, ECO:0000313|Proteomes:UP000175829};
RN   [1] {ECO:0000313|EMBL:OEV02087.1, ECO:0000313|Proteomes:UP000175829}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCSIO M10379 {ECO:0000313|EMBL:OEV02087.1,
RC   ECO:0000313|Proteomes:UP000175829};
RX   PubMed=27446038; DOI=10.3389/fmicb.2016.00998;
RA   Tian X., Zhang Z., Yang T., Chen M., Li J., Chen F., Yang J., Li W.,
RA   Zhang B., Zhang Z., Wu J., Zhang C., Long L., Xiao J.;
RT   "Comparative Genomics Analysis of Streptomyces Species Reveals Their
RT   Adaptation to the Marine Environment and Their Diversity at the Genomic
RT   Level.";
RL   Front. Microbiol. 7:998-998(2016).
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:OEV02087.1}.
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DR   EMBL; LJGV01000021; OEV02087.1; -; Genomic_DNA.
DR   RefSeq; WP_019356816.1; NZ_LJGV01000021.1.
DR   AlphaFoldDB; A0A1E7KDV4; -.
DR   PATRIC; fig|943816.4.peg.5519; -.
DR   Proteomes; UP000175829; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
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   Reference proteome {ECO:0000313|Proteomes:UP000175829}.
FT   DOMAIN          14..189
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   334 AA;  35888 MW;  4D38D5EE86C572D3 CRC64;
     MAATGTASAA AQKLPVAKAI NSSLRTALEN DPKVLVMGED VGKLGGVFRV TDGLQKDFGE
     DRVIDTPLAE SGIVGTAIGL ALRGYRPVVE IQFDGFVFPA YDQIVTQLAK MHARALGKIK
     LPVVIRIPYG GGIGAVEHHS ESPEALFAHV AGLKCVSPSN ASDAYWMMQQ AIESDDPVIF
     FEPKRRYWDK GEVDPSAIPA PLHSAQVARQ GSAVTVAAYG PMVKVCLEAA AAAEEEGNSL
     EVVDLRSMSP IDFDTVQRSV EKTGRLVLVH EAPVFLGTGA EIAARITERC FYHLEAPVLR
     VGGFHAPYPP ARLEDEYLPN LDRVLDAVDR ALAY
//
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