ID   A0A0P4R485_9ACTN        Unreviewed;       344 AA.
AC   A0A0P4R485;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=Putative branched-chain alpha-keto acid dehydrogenase E1 component beta subunit {ECO:0000313|EMBL:GAO07298.1};
GN   Name=bkdB {ECO:0000313|EMBL:GAO07298.1};
GN   ORFNames=TPA0598_02_05370 {ECO:0000313|EMBL:GAO07298.1};
OS   Streptomyces lydicamycinicus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1546107 {ECO:0000313|EMBL:GAO07298.1, ECO:0000313|Proteomes:UP000048965};
RN   [1] {ECO:0000313|Proteomes:UP000048965}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 110027 {ECO:0000313|Proteomes:UP000048965};
RA   Komaki H., Ichikawa N., Katano-Makiyama Y., Hosoyama A., Hashimoto M.,
RA   Uohara A., Kitahashi Y., Ohji S., Kimura A., Yamazoe A., Igarashi Y.,
RA   Fujita N.;
RT   "Whole genome shotgun sequence of Streptomyces sp. NBRC 110027.";
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:GAO07298.1, ECO:0000313|Proteomes:UP000048965}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 110027 {ECO:0000313|EMBL:GAO07298.1,
RC   ECO:0000313|Proteomes:UP000048965};
RX   PubMed=26380643; DOI=10.1186/s40793-015-0046-5;
RA   Komaki H., Ichikawa N., Hosoyama A., Fujita N., Igarashi Y.;
RT   "Draft genome sequence of marine-derived Streptomyces sp. TP-A0598, a
RT   producer of anti-MRSA antibiotic lydicamycins.";
RL   Stand. Genomic Sci. 10:58-58(2015).
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:GAO07298.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BBNO01000002; GAO07298.1; -; Genomic_DNA.
DR   RefSeq; WP_042151122.1; NZ_BBNO01000002.1.
DR   AlphaFoldDB; A0A0P4R485; -.
DR   OrthoDB; 3457658at2; -.
DR   Proteomes; UP000048965; 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:UP000048965}.
FT   DOMAIN          13..188
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   344 AA;  37131 MW;  F0F6C30B3F1D60E8 CRC64;
     MTTTAPATAR KPATMAQALT RALRDAMADD PSVHVMGEDV GTLGGVFRVT DGLAKEFGED
     RCTDTALAEA GILGTAVGMA MYGLRPVVEM QFDAFAYPAF EQLISHVARM RNRTQGALTM
     PLTIRVPYGG GIGGVEHHSD SSEAYYLATP GLQVVTPATV EDAYGLLRAA IASDDPVVFL
     EPKRLYWSKA DWSPDAPTEV APLGQAEIRR RGSSATLITY GPSLPVCMEA AEAARAEGWD
     LEVVDLRSLM PFDDETVCAS VRRTGRAVVV HESNGFGGPG GEIAARITER CFHHLEAPVL
     RVAGFDIPYP PPMLERHHLP GVDRILDTVA RLQWESDWTE GRGE
//