ID   DES7_STRVZ              Reviewed;         426 AA.
AC   Q9ZGH7;
DT   16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=10-deoxymethynolide desosaminyltransferase {ECO:0000303|PubMed:15161264};
DE            EC=2.4.1.277 {ECO:0000269|PubMed:15161264, ECO:0000269|PubMed:17049185, ECO:0000269|PubMed:20695498};
GN   Name=desVII {ECO:0000303|PubMed:9770448};
OS   Streptomyces venezuelae.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=54571;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 15439 / DSM 41110 / IMRU3627 / M-2140;
RX   PubMed=9770448; DOI=10.1073/pnas.95.21.12111;
RA   Xue Y., Zhao L., Liu H.W., Sherman D.H.;
RT   "A gene cluster for macrolide antibiotic biosynthesis in Streptomyces
RT   venezuelae: architecture of metabolic diversity.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:12111-12116(1998).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=15161264; DOI=10.1021/ja049967j;
RA   Borisova S.A., Zhao L., Melancon C.E. III, Kao C.L., Liu H.W.;
RT   "Characterization of the glycosyltransferase activity of desVII: analysis
RT   of and implications for the biosynthesis of macrolide antibiotics.";
RL   J. Am. Chem. Soc. 126:6534-6535(2004).
RN   [3]
RP   FUNCTION, AND SUBSTRATE SPECIFICITY.
RX   PubMed=16538696; DOI=10.1002/anie.200503195;
RA   Borisova S.A., Zhang C., Takahashi H., Zhang H., Wong A.W., Thorson J.S.,
RA   Liu H.W.;
RT   "Substrate specificity of the macrolide-glycosylating enzyme pair
RT   DesVII/DesVIII: opportunities, limitations, and mechanistic hypotheses.";
RL   Angew. Chem. Int. Ed. 45:2748-2753(2006).
RN   [4]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=ATCC 15439 / DSM 41110 / IMRU3627 / M-2140;
RX   PubMed=17049185; DOI=10.1016/j.gene.2006.08.021;
RA   Hong J.S., Park S.J., Parajuli N., Park S.R., Koh H.S., Jung W.S.,
RA   Choi C.Y., Yoon Y.J.;
RT   "Functional analysis of desVIII homologues involved in glycosylation of
RT   macrolide antibiotics by interspecies complementation.";
RL   Gene 386:123-130(2007).
RN   [5]
RP   FUNCTION, AND SUBSTRATE SPECIFICITY.
RX   PubMed=18548476; DOI=10.1002/cbic.200800155;
RA   Borisova S.A., Kim H.J., Pu X., Liu H.W.;
RT   "Glycosylation of acyclic and cyclic aglycone substrates by macrolide
RT   glycosyltransferase DesVII/DesVIII: analysis and implications.";
RL   ChemBioChem 9:1554-1558(2008).
RN   [6]
RP   FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RC   STRAIN=ATCC 15439 / DSM 41110 / IMRU3627 / M-2140;
RX   PubMed=20695498; DOI=10.1021/bi1007657;
RA   Borisova S.A., Liu H.W.;
RT   "Characterization of glycosyltransferase DesVII and its auxiliary partner
RT   protein DesVIII in the methymycin/picromycin biosynthetic pathway.";
RL   Biochemistry 49:8071-8084(2010).
CC   -!- FUNCTION: Involved in the biosynthesis of the macrolide antibiotics
CC       methymycin, neomethymycin, narbomycin, and pikromycin. Catalyzes the
CC       attachment of dTDP-D-desosamine onto 12- and 14-membered macrolactone
CC       rings 10-deoxymethynolide and narbonolide to produce 10-deoxymethymycin
CC       (YC-17) and narbomycin. DesVII is unique among glycosyltransferases in
CC       that it requires an additional protein component, DesVIII, for its
CC       activity. DesVII can recognize and process not only cyclic substrates
CC       of different ring size, but also a variety of linear substrates albeit
CC       with reduced, but measurable activities (PubMed:18548476). Both L-
CC       sugars and D-sugars are recognized as substrates and variant
CC       substitutions at C-3 and C-4 are tolerated, but deoxygenation at C-6 is
CC       required (PubMed:16538696). {ECO:0000269|PubMed:15161264,
CC       ECO:0000269|PubMed:16538696, ECO:0000269|PubMed:17049185,
CC       ECO:0000269|PubMed:18548476, ECO:0000269|PubMed:20695498}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=10-deoxymethynolide + dTDP-alpha-D-desosamine = 10-
CC         deoxymethymycin + dTDP + H(+); Xref=Rhea:RHEA:31627,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29461, ChEBI:CHEBI:58369,
CC         ChEBI:CHEBI:63260, ChEBI:CHEBI:63307; EC=2.4.1.277;
CC         Evidence={ECO:0000269|PubMed:15161264, ECO:0000269|PubMed:17049185,
CC         ECO:0000269|PubMed:20695498};
CC   -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000305|PubMed:20695498}.
CC   -!- SUBUNIT: Forms a complex with DesVIII. {ECO:0000269|PubMed:20695498}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene are not able to produce
CC       glycosylated macrolides. {ECO:0000269|PubMed:15161264}.
CC   -!- MISCELLANEOUS: DesVIII assists the folding of the DesVII polypeptide.
CC       However, unlike chaperones, it remains bound to DesVII during
CC       catalysis, forming a tight DesVII/DesVIII complex. Although the
CC       formation of the DesVII/DesVIII complex is essential for the catalytic
CC       activity, DesVIII is unlikely to be involved in catalysis directly.
CC       {ECO:0000269|PubMed:20695498}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 28 family.
CC       {ECO:0000305}.
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DR   EMBL; AF079762; AAC68677.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9ZGH7; -.
DR   SMR; Q9ZGH7; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   KEGG; ag:AAC68677; -.
DR   BioCyc; MetaCyc:MON-18406; -.
DR   BRENDA; 2.4.1.277; 6106.
DR   BRENDA; 2.4.1.278; 6106.
DR   BRENDA; 2.4.1.328; 6106.
DR   GO; GO:0016758; F:hexosyltransferase activity; IMP:UniProtKB.
DR   GO; GO:0008194; F:UDP-glycosyltransferase activity; IEA:InterPro.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IMP:UniProtKB.
DR   CDD; cd03784; GT1_Gtf-like; 1.
DR   InterPro; IPR010610; DUF1205.
DR   InterPro; IPR030953; Glycosyl_450act.
DR   InterPro; IPR002213; UDP_glucos_trans.
DR   Pfam; PF06722; DUF1205; 1.
DR   TIGRFAMs; TIGR04516; glycosyl_450act; 1.
PE   1: Evidence at protein level;
KW   Antibiotic biosynthesis; Glycosyltransferase; Transferase.
FT   CHAIN           1..426
FT                   /note="10-deoxymethynolide desosaminyltransferase"
FT                   /id="PRO_0000435701"
SQ   SEQUENCE   426 AA;  46423 MW;  5FF9BAA10754396D CRC64;
     MRVLLTSFAH HTHYYGLVPL AWALLAAGHE VRVASQPALT DTITGSGLAA VPVGTDHLIH
     EYRVRMAGEP RPNHPAIAFD EARPEPLDWD HALGIEAILA PYFHLLANND SMVDDLVDFA
     RSWQPDLVLW EPTTYAGAVA AQVTGAAHAR VLWGPDVMGS ARRKFVALRD RQPPEHREDP
     TAEWLTWTLD RYGASFEEEL LTGQFTIDPT PPSLRLDTGL PTVGMRYVPY NGTSVVPDWL
     SEPPARPRVC LTLGVSAREV LGGDGVSQGD ILEALADLDI ELVATLDASQ RAEIRNYPKH
     TRFTDFVPMH ALLPSCSAII HHGGAGTYAT AVINAVPQVM LAELWDAPVK ARAVAEQGAG
     FFLPPAELTP QAVRDAVVRI LDDPSVATAA HRLREETFGD PTPAGIVPEL ERLAAQHRRP
     PADARH