ID   ELMGT_STROV             Reviewed;         382 AA.
AC   Q9F2F9;
DT   29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 2.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Elloramycin glycosyltransferase ElmGT {ECO:0000305};
DE            EC=2.4.1.331 {ECO:0000269|PubMed:11306350};
GN   Name=elmGT {ECO:0000303|PubMed:11306350};
OS   Streptomyces olivaceus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=47716 {ECO:0000312|EMBL:CAC16413.2};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=Tu 2353;
RX   PubMed=11306350; DOI=10.1016/s1074-5521(01)00010-2;
RA   Blanco G., Patallo E.P., Brana A.F., Trefzer A., Bechthold A., Rohr J.,
RA   Mendez C., Salas J.A.;
RT   "Identification of a sugar flexible glycosyltransferase from Streptomyces
RT   olivaceus, the producer of the antitumor polyketide elloramycin.";
RL   Chem. Biol. 8:253-263(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Tu 2353;
RX   PubMed=11376004; DOI=10.1074/jbc.m101225200;
RA   Patallo E.P., Blanco G., Fischer C., Brana A.F., Rohr J., Mendez C.,
RA   Salas J.A.;
RT   "Deoxysugar methylation during biosynthesis of the antitumor polyketide
RT   elloramycin by Streptomyces olivaceus. Characterization of three
RT   methyltransferase genes.";
RL   J. Biol. Chem. 276:18765-18774(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Tu 2353;
RX   PubMed=18310024; DOI=10.1099/mic.0.2007/014035-0;
RA   Ramos A., Lombo F., Brana A.F., Rohr J., Mendez C., Salas J.A.;
RT   "Biosynthesis of elloramycin in Streptomyces olivaceus requires
RT   glycosylation by enzymes encoded outside the aglycon cluster.";
RL   Microbiology 154:781-788(2008).
RN   [4]
RP   FUNCTION.
RX   PubMed=12444703; DOI=10.1021/np020112z;
RA   Fischer C., Rodriguez L., Patallo E.P., Lipata F., Brana A.F., Mendez C.,
RA   Salas J.A., Rohr J.;
RT   "Digitoxosyltetracenomycin C and glucosyltetracenomycin C, two novel
RT   elloramycin analogues obtained by exploring the sugar donor substrate
RT   specificity of glycosyltransferase ElmGT.";
RL   J. Nat. Prod. 65:1685-1689(2002).
RN   [5]
RP   FUNCTION, AND MUTAGENESIS OF LEU-309 AND ASN-312.
RX   PubMed=19233921; DOI=10.1128/jb.01747-08;
RA   Ramos A., Olano C., Brana A.F., Mendez C., Salas J.A.;
RT   "Modulation of deoxysugar transfer by the elloramycin glycosyltransferase
RT   ElmGT through site-directed mutagenesis.";
RL   J. Bacteriol. 191:2871-2875(2009).
CC   -!- FUNCTION: Glycosyltransferase that transfers an L-rhamnose moiety from
CC       dTDP-L-rhamnose to the elloramycin aglycone 8-demethyl-tetracenomycin C
CC       (8DMTC) in elloramycin biosynthesis, an antitumor polyketide. Possesses
CC       donor substrate flexibility: able to transfer at least 11 different
CC       sugars to 8DMTC, such as NDP-D-glucose, as well as NDP-L-digitoxose,
CC       including both L- and D-isomeric forms of some sugars.
CC       {ECO:0000269|PubMed:11306350, ECO:0000269|PubMed:12444703}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=8-demethyltetracenomycin C + dTDP-beta-L-rhamnose = 8-
CC         demethyl-8-alpha-L-rhamnosyl-tetracenomycin C + dTDP + H(+);
CC         Xref=Rhea:RHEA:42848, ChEBI:CHEBI:15378, ChEBI:CHEBI:31144,
CC         ChEBI:CHEBI:57510, ChEBI:CHEBI:58369, ChEBI:CHEBI:78283;
CC         EC=2.4.1.331; Evidence={ECO:0000269|PubMed:11306350};
CC   -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 28 family.
CC       {ECO:0000305}.
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; AJ300305; CAC16413.2; -; Genomic_DNA.
DR   EMBL; AM900040; CAP12607.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9F2F9; -.
DR   SMR; Q9F2F9; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   KEGG; ag:CAP12607; -.
DR   BioCyc; MetaCyc:MON-18592; -.
DR   BRENDA; 2.4.1.331; 6068.
DR   GO; GO:0016758; F:hexosyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0008194; F:UDP-glycosyltransferase activity; IEA:InterPro.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IDA:UniProtKB.
DR   CDD; cd03784; GT1_Gtf-like; 1.
DR   InterPro; IPR010610; DUF1205.
DR   InterPro; IPR002213; UDP_glucos_trans.
DR   Pfam; PF06722; DUF1205; 1.
PE   1: Evidence at protein level;
KW   Antibiotic biosynthesis; Glycosyltransferase; Transferase.
FT   CHAIN           1..382
FT                   /note="Elloramycin glycosyltransferase ElmGT"
FT                   /id="PRO_0000430712"
FT   MUTAGEN         309
FT                   /note="L->A,V,Y: Increased transfer of L-olivose."
FT                   /evidence="ECO:0000269|PubMed:19233921"
FT   MUTAGEN         309
FT                   /note="L->I: Increased transfer of L-rhamnose."
FT                   /evidence="ECO:0000269|PubMed:19233921"
FT   MUTAGEN         309
FT                   /note="L->M: Increased transfer of D-boivinose."
FT                   /evidence="ECO:0000269|PubMed:19233921"
FT   MUTAGEN         312
FT                   /note="N->S: Increased transfer of L-olivose."
FT                   /evidence="ECO:0000269|PubMed:19233921"
FT   MUTAGEN         312
FT                   /note="N->T,Q: Increased transfer of L-olivose and
FT                   decreased affinity for other deoxysugars."
FT                   /evidence="ECO:0000269|PubMed:19233921"
SQ   SEQUENCE   382 AA;  39465 MW;  8231901E28F66D91 CRC64;
     MRVLAVATPA LGHLFPAVPL LWALRARGDE VLVVTGGDAL RVAEAGLPVV DALPGETLTT
     LFGAYQETDP AFFVALRRSP MTTLRDLAPV LAYLAGRLLE PARRAAERWR PDAILATHGQ
     AAGAVVAAEH GIPLVEHGFG FVRSDGAQEA VRQLLAERLG PAGSEPPPER YFLDIAVPSM
     TSAIEGMSLR AVPYNGGAVL PLSGASVGGR PPRPRVLVTA GTQLLHTHGA GALAWLPEVA
     AGHEAEFLLA AGGADLRDLG RLPPHVRVLD WTPLATVLPT CSAVVHHGGS GTTLAALAAG
     VPQLVSPALA DNHINARAVA DRGAGLETAV PDATTLTALL REPAFAKAAR EVADELRSLP
     APADVAARLH TAFGLPTTQG DA