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Database: UniProt
Entry: A0A2U3BWM7_9ACTN
LinkDB: A0A2U3BWM7_9ACTN
Original site: A0A2U3BWM7_9ACTN 
ID   A0A2U3BWM7_9ACTN        Unreviewed;       341 AA.
AC   A0A2U3BWM7;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   SubName: Full=Alpha-ketoacid dehydrogenase subunit beta {ECO:0000313|EMBL:PWI41173.1};
GN   ORFNames=CK485_27940 {ECO:0000313|EMBL:PWI41173.1};
OS   Streptomyces sp. ICBB 8177.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=563922 {ECO:0000313|EMBL:PWI41173.1, ECO:0000313|Proteomes:UP000245673};
RN   [1] {ECO:0000313|EMBL:PWI41173.1, ECO:0000313|Proteomes:UP000245673}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ICBB 8177 {ECO:0000313|EMBL:PWI41173.1,
RC   ECO:0000313|Proteomes:UP000245673};
RX   PubMed=29773836; DOI=10.1038/s41598-018-26179-w;
RA   Pavlikova M., Kamenik Z., Janata J., Kadlcik S., Kuzma M., Najmanova L.;
RT   "Novel pathway of 3-hydroxyanthranilic acid formation in limazepine
RT   biosynthesis reveals evolutionary relation between phenazines and
RT   pyrrolobenzodiazepines.";
RL   Sci. Rep. 8:7810-7810(2018).
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:PWI41173.1}.
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DR   EMBL; NSKH01000024; PWI41173.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2U3BWM7; -.
DR   OrthoDB; 3457658at2; -.
DR   Proteomes; UP000245673; 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:UP000245673}.
FT   DOMAIN          17..192
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   341 AA;  36580 MW;  634FA7B6FC390A72 CRC64;
     MGTATAPAPA PATRKPATMA QALRQAMRDA LAEDRDVHVM GEDVGTLGGV FRVTDGLAAE
     FGPERVTDTP LAEAGILGTA VGMAMYGLRP VVEMQFDAFA YPAMEQLISH VSRMRNRTRG
     TLPMPITIRV PYGGGIGGVE HHSDSSEAYY LHTPGLHVVT PATVADAYGL LRAAIASDDP
     VVFLEPKRLY WGKADWSADA PETVPPLGRA VVRRAGTSAT LITYGPSVPV CLEAAEAARQ
     EGWDLEVVDL RSLMPFDDET VCASVRRTGR AVVVHESAGF CGTGAEIAAR VSERCFHHLE
     APVLRVAGFD IPYPPPMLER HHLPGVDRVL DAVARLQWEG N
//
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