ID A0A171B0P8_9ACTN Unreviewed; 326 AA.
AC A0A171B0P8;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=2-oxoisovalerate dehydrogenase {ECO:0000313|EMBL:GAT84206.1};
GN ORFNames=STXM2123_4907 {ECO:0000313|EMBL:GAT84206.1};
OS Streptomyces sp. F-3.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1840095 {ECO:0000313|EMBL:GAT84206.1, ECO:0000313|Proteomes:UP000078145};
RN [1] {ECO:0000313|EMBL:GAT84206.1, ECO:0000313|Proteomes:UP000078145}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wang L.S., Gao P.J., Liu L., Zhang H.Q., Cheng Z., Sun X.M.;
RT "Streptomyces sp. F-3 geneom sequencing.";
RL Submitted (MAY-2016) 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:GAT84206.1}.
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DR EMBL; BDDR01000040; GAT84206.1; -; Genomic_DNA.
DR RefSeq; WP_067398143.1; NZ_BDDR01000040.1.
DR AlphaFoldDB; A0A171B0P8; -.
DR STRING; 1840095.STXM2123_4907; -.
DR OrthoDB; 3457658at2; -.
DR Proteomes; UP000078145; 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:UP000078145}.
FT DOMAIN 6..181
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 326 AA; 35682 MW; A53E4C1459D1C048 CRC64;
MAAEKMALAK AINESLRRAL ESDPKVLIMG EDVGKLGGVF RVTDGLYKDF GEERVIDTPL
AESGIIGTAI GLALRGYRPV AEIQFDGFVF PAYDQIVTQL AKMHARALGK VKLPVVVRIP
YGGGIGAVEH HSESPEALFA HVAGLKIVSP SNASDAYWML QQAIQSDDPV IFFEPKRRYW
DKGEVNTEAI PGPLHKARVV REGTDLTLVA YGPMVKLCQE VADAAAEEGK SLEVVDLRSV
SPLDFDTIQA SVEKTRRLVV VHEAPVFFGT GAEIAARITE RCFYHLEAPV LRVGGYHAPY
PPARLEETYL PDLDRVLDAV DRSLAY
//
