ID   OLES_STRAT              Reviewed;         356 AA.
AC   Q9RR29;
DT   23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=Glucose-1-phosphate thymidylyltransferase {ECO:0000303|PubMed:10770761};
DE            EC=2.7.7.24 {ECO:0000250|UniProtKB:P61887};
GN   Name=oleS {ECO:0000303|PubMed:10770761};
OS   Streptomyces antibioticus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1890;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PATHWAY.
RC   STRAIN=ATCC 11891 / DSM 40868 / BCRC 11580 / NCIMB 11506 / PSA 205
RC   {ECO:0000312|EMBL:AAD55453.1};
RX   PubMed=10770761; DOI=10.1128/aac.44.5.1266-1275.2000;
RA   Aguirrezabalaga I., Olano C., Allende N., Rodriguez L., Brana A.F.,
RA   Mendez C., Salas J.A.;
RT   "Identification and expression of genes involved in biosynthesis of L-
RT   oleandrose and its intermediate L-olivose in the oleandomycin producer
RT   Streptomyces antibioticus.";
RL   Antimicrob. Agents Chemother. 44:1266-1275(2000).
CC   -!- FUNCTION: Involved in the biosynthesis of the two 2,6-deoxysugars,
CC       dTDP-L-oleandrose and dTDP-D-desosamine, attached to the macrolactone
CC       ring oleandolide to produce the aglycone antibiotic oleandomycin
CC       (PubMed:10770761). Catalyzes the formation of dTDP-glucose from
CC       deoxythymidine triphosphate (dTTP) and glucose 1-phosphate (By
CC       similarity). {ECO:0000250|UniProtKB:P61887,
CC       ECO:0000269|PubMed:10770761}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-D-glucose 1-phosphate + dTTP + H(+) = diphosphate +
CC         dTDP-alpha-D-glucose; Xref=Rhea:RHEA:15225, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:37568, ChEBI:CHEBI:57477,
CC         ChEBI:CHEBI:58601; EC=2.7.7.24;
CC         Evidence={ECO:0000250|UniProtKB:P61887};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P61887};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P61887};
CC   -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000305|PubMed:10770761}.
CC   -!- SIMILARITY: Belongs to the glucose-1-phosphate thymidylyltransferase
CC       family. {ECO:0000305}.
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DR   EMBL; AF055579; AAD55453.1; -; Genomic_DNA.
DR   PIR; T51105; T51105.
DR   AlphaFoldDB; Q9RR29; -.
DR   SMR; Q9RR29; -.
DR   BioCyc; MetaCyc:MON-17069; -.
DR   GO; GO:0008879; F:glucose-1-phosphate thymidylyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd04189; G1P_TT_long; 1.
DR   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR005908; G1P_thy_trans_l.
DR   InterPro; IPR005835; NTP_transferase_dom.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   Pfam; PF00483; NTP_transferase; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
DR   TIGRFAMs; TIGR01208; rmlA_long; 1.
PE   3: Inferred from homology;
KW   Antibiotic biosynthesis; Magnesium; Metal-binding; Nucleotidyltransferase;
KW   Transferase.
FT   CHAIN           1..356
FT                   /note="Glucose-1-phosphate thymidylyltransferase"
FT                   /id="PRO_0000444208"
FT   BINDING         107
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P61887"
FT   BINDING         221
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P61887"
SQ   SEQUENCE   356 AA;  38142 MW;  BEEE178A3A9A10BE CRC64;
     MKALVLAGGS GTRLRPITHT SAKQLVAVAN KPVLFYGLEA IAAAGITDVG LIVGDTAGEV
     PRAVGDGAKF GLDITYIEQS RPLGLAHAVL IAHTYLGDDD FVMYLGDNFI VGGIDDLVRT
     FRDGRRPAAR ILLTHVSDPS GFGVAELDDD GRVVGLEEKP RHPKSDLALV GVYFFTPAIH
     EAVRAIEPSW RGELEITHAI QHLIDNGADI QSMVIEGYWK DTGNVADMLE VNRTVLEDLE
     PRIEGTVDEH TVVIGRVVVG EGARVTNSRI MGPAIIGAGP EISDSYIGPF TSVGDNCRIT
     GSEMEFSIML AESAITGVRR IEGSLIGRNV QVTQSLHAPN AHRFVLGDHS KVEIQS