ID   NOVM_STRNV              Reviewed;         379 AA.
AC   Q9L9F5;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=L-demethylnoviosyl transferase;
DE            EC=2.4.1.302 {ECO:0000269|PubMed:12680772};
DE   AltName: Full=Novobiocin biosynthesis protein M;
GN   Name=novM;
OS   Streptomyces niveus (Streptomyces spheroides).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=193462;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 23965 / DSM 40292 / JCM 4252 / NBRC 12917 / NCIMB 11891 / NRRL
RC   2449;
RX   PubMed=10770754; DOI=10.1128/aac.44.5.1214-1222.2000;
RA   Steffensky M., Muhlenweg A., Wang Z.X., Li S.M., Heide L.;
RT   "Identification of the novobiocin biosynthetic gene cluster of Streptomyces
RT   spheroides NCIB 11891.";
RL   Antimicrob. Agents Chemother. 44:1214-1222(2000).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND PATHWAY.
RC   STRAIN=ATCC 23965 / DSM 40292 / JCM 4252 / NBRC 12917 / NCIMB 11891 / NRRL
RC   2449;
RX   PubMed=12680772; DOI=10.1021/bi0340088;
RA   Freel Meyers C.L., Oberthur M., Anderson J.W., Kahne D., Walsh C.T.;
RT   "Initial characterization of novobiocic acid noviosyl transferase activity
RT   of NovM in biosynthesis of the antibiotic novobiocin.";
RL   Biochemistry 42:4179-4189(2003).
RN   [3]
RP   FUNCTION.
RC   STRAIN=ATCC 23965 / DSM 40292 / JCM 4252 / NBRC 12917 / NCIMB 11891 / NRRL
RC   2449;
RX   PubMed=12633109; DOI=10.1021/ol0341086;
RA   Albermann C., Soriano A., Jiang J., Vollmer H., Biggins J.B., Barton W.A.,
RA   Lesniak J., Nikolov D.B., Thorson J.S.;
RT   "Substrate specificity of NovM: implications for novobiocin biosynthesis
RT   and glycorandomization.";
RL   Org. Lett. 5:933-936(2003).
RN   [4]
RP   FUNCTION.
RC   STRAIN=ATCC 23965 / DSM 40292 / JCM 4252 / NBRC 12917 / NCIMB 11891 / NRRL
RC   2449;
RX   PubMed=15218104; DOI=10.1073/pnas.0403526101;
RA   Pi N., Meyers C.L., Pacholec M., Walsh C.T., Leary J.A.;
RT   "Mass spectrometric characterization of a three-enzyme tandem reaction for
RT   assembly and modification of the novobiocin skeleton.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:10036-10041(2004).
CC   -!- FUNCTION: Catalyzes the transfer of L-noviose from dTDP-4-O-demethyl-
CC       beta-L-noviose to the phenolic oxygen of novobiocic acid, creating the
CC       full ABC ring system in the novobiocin biosynthesis pathway. Novobiocin
CC       is an aminocoumarin family antibiotic that targets bacterial DNA
CC       gyrases. Also shows activity with variant coumarin aglycones,
CC       suggesting it may be a promiscuous catalyst for noviosylation of a
CC       range of planar scaffolds. Does not show activity with TDP-L-rhamnose.
CC       {ECO:0000269|PubMed:12633109, ECO:0000269|PubMed:12680772,
CC       ECO:0000269|PubMed:15218104}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dTDP-4-O-demethyl-beta-L-noviose + novobiocic acid =
CC         desmethyldescarbamoylnovobiocin + dTDP + H(+); Xref=Rhea:RHEA:36695,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:58369, ChEBI:CHEBI:73953,
CC         ChEBI:CHEBI:73957, ChEBI:CHEBI:74153; EC=2.4.1.302;
CC         Evidence={ECO:0000269|PubMed:12680772};
CC   -!- ACTIVITY REGULATION: Inhibited by TDP-L-rhamnose, the sugar donor that
CC       most closely structurally resembles the natural substrate dTDP-beta-L-
CC       noviose. {ECO:0000269|PubMed:12680772}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=32 uM for novobiocic acid {ECO:0000269|PubMed:12680772};
CC         Note=kcat is 313 min(-1) with novobiocic acid as substrate.;
CC   -!- PATHWAY: Antibiotic biosynthesis; novobiocin biosynthesis.
CC       {ECO:0000269|PubMed:12680772}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 28 family.
CC       {ECO:0000305}.
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DR   EMBL; AF170880; AAF67506.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9L9F5; -.
DR   SMR; Q9L9F5; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   KEGG; ag:AAF67506; -.
DR   BioCyc; MetaCyc:MON-18054; -.
DR   SABIO-RK; Q9L9F5; -.
DR   UniPathway; UPA01035; -.
DR   GO; GO:0016758; F:hexosyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0008194; F:UDP-glycosyltransferase activity; IEA:InterPro.
DR   GO; GO:0043642; P:novobiocin 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.
DR   Pfam; PF00201; UDPGT; 1.
PE   1: Evidence at protein level;
KW   Antibiotic biosynthesis; Glycosyltransferase; Transferase.
FT   CHAIN           1..379
FT                   /note="L-demethylnoviosyl transferase"
FT                   /id="PRO_0000424000"
SQ   SEQUENCE   379 AA;  39698 MW;  A0ACCBD03FF401C5 CRC64;
     MRVLLTSLPG IGHLFPMVPL GWALQAAGHT VLVATDREFL PVVTGAGLSA TAVLDPVDPV
     ELFKPVEPFG DPLSPAERTG HRCAEAGVRA LPAMRALVDV WHPDLVIAEP MELAGPAAAT
     NAGVPWVRHS YGLIPPGPLL SVAAEVLDAE LAVLGLSALA KPARTIDVCP DSLRPSDGVA
     TVPMRYVPYN GPAGVPDWLL AGPPARPRVC LTLGTSLPRR DPHVAPLWRL LLDELVALGQ
     EVVIAIDESH RPLLGHLPDG VRAARIPLCD LLPTCTAIVH HGGSGSTMAA ASFGVPQLVV
     PHFADHFTNA ERLTAVGAGL SLPHDTDDLA RISAACELIT GDGPHRAISR RLADENARRP
     TPAVVAEGLA AEQRSMTPA