GenomeNet

Database: UniProt
Entry: K4R154_STRDJ
LinkDB: K4R154_STRDJ
Original site: K4R154_STRDJ 
ID   K4R154_STRDJ            Unreviewed;       337 AA.
AC   K4R154;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   SubName: Full=1-deoxy-D-xylulose-5-phosphate synthase {ECO:0000313|EMBL:CCK26852.1};
DE            EC=2.2.1.7 {ECO:0000313|EMBL:CCK26852.1};
GN   Name=korB {ECO:0000313|EMBL:CCK26852.1};
GN   ORFNames=BN159_2473 {ECO:0000313|EMBL:CCK26852.1};
OS   Streptomyces davaonensis (strain DSM 101723 / JCM 4913 / KCC S-0913 / 768).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1214101 {ECO:0000313|EMBL:CCK26852.1, ECO:0000313|Proteomes:UP000008043};
RN   [1] {ECO:0000313|EMBL:CCK26852.1, ECO:0000313|Proteomes:UP000008043}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 101723 / JCM 4913 / KCC S-0913 / 768
RC   {ECO:0000313|Proteomes:UP000008043};
RX   PubMed=23043000; DOI=10.1128/JB.01592-12;
RA   Jankowitsch F., Schwarz J., Ruckert C., Gust B., Szczepanowski R., Blom J.,
RA   Pelzer S., Kalinowski J., Mack M.;
RT   "Genome sequence of the bacterium Streptomyces davawensis JCM 4913 and
RT   heterologous production of the unique antibiotic roseoflavin.";
RL   J. Bacteriol. 194:6818-6827(2012).
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; HE971709; CCK26852.1; -; Genomic_DNA.
DR   RefSeq; WP_015657246.1; NC_020504.1.
DR   AlphaFoldDB; K4R154; -.
DR   STRING; 1214101.BN159_2473; -.
DR   KEGG; sdv:BN159_2473; -.
DR   PATRIC; fig|1214101.3.peg.2511; -.
DR   eggNOG; COG1013; Bacteria.
DR   HOGENOM; CLU_048564_1_0_11; -.
DR   OrthoDB; 9775140at2; -.
DR   Proteomes; UP000008043; Chromosome.
DR   GO; GO:0008661; F:1-deoxy-D-xylulose-5-phosphate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   CDD; cd03375; TPP_OGFOR; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR   PANTHER; PTHR48084:SF4; 2-OXOGLUTARATE OXIDOREDUCTASE SUBUNIT KORB; 1.
DR   PANTHER; PTHR48084; 2-OXOGLUTARATE OXIDOREDUCTASE SUBUNIT KORB-RELATED; 1.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008043};
KW   Transferase {ECO:0000313|EMBL:CCK26852.1}.
FT   DOMAIN          51..198
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   337 AA;  36667 MW;  EDFE4BBAB3EEF2DE CRC64;
     MRLELSARDF KSDQEVRWCP GCGDYAILSA VQGFMPEVGV ARENIVFISG IGCSSRFPYY
     MNTYGMHSIH GRAPAIATGL AVSRPDLSVW VVTGDGDALS IGGNHLIHAL RRNVNLKILL
     FNNRIYGLTK GQYSPTSELG KITKSTPMGS LDAPFNPVSL AIGAEASFVA RTVDSDRKHL
     TEVLRAAHRH PGTALVEIYQ NCNIFNDGAF EVLKDKQQAQ ESVIRLEHGR PILFGTDGAK
     GVVRDPATGD LQVVDVTQDN EHRVLIHDAH ADSPTTAFAL SRLADPQTLH HTPIGVFRDI
     ERPVYDTTMA DQLEAAVQQN GKGDLAAVLA GSDTWSR
//
DBGET integrated database retrieval system