ID   IND7_STRGR              Reviewed;         237 AA.
AC   A0A0D4BSP3;
DT   22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT   27-MAY-2015, sequence version 1.
DT   03-AUG-2022, entry version 18.
DE   RecName: Full=N-demethylindolmycin N-methyltransferase {ECO:0000303|PubMed:25730866};
DE            EC=2.1.1.328 {ECO:0000269|PubMed:25730866};
GN   Name=ind7 {ECO:0000303|PubMed:25730866};
OS   Streptomyces griseus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 12648 {ECO:0000312|EMBL:AJT38688.1};
RX   PubMed=25730866; DOI=10.1073/pnas.1419964112;
RA   Du Y.L., Alkhalaf L.M., Ryan K.S.;
RT   "In vitro reconstitution of indolmycin biosynthesis reveals the molecular
RT   basis of oxazolinone assembly.";
RL   Proc. Natl. Acad. Sci. U.S.A. 112:2717-2722(2015).
CC   -!- FUNCTION: Involved in the biosynthesis of the antibiotic indolmycin, an
CC       inhibitor of the bacterial tryptophan-tRNA synthetases. Catalyzes the
CC       methylation of N-demethylindolmycin to yield indolmycin, with S-
CC       adenosylmethionine (AdoMet) acting as the methyl donor.
CC       {ECO:0000269|PubMed:25730866}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-demethylindolmycin + S-adenosyl-L-methionine = H(+) +
CC         indolmycin + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:24726,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:91178, ChEBI:CHEBI:91179; EC=2.1.1.328;
CC         Evidence={ECO:0000269|PubMed:25730866};
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene accumulate N-
CC       demethylindolmycin and are unable to produce indolmycin.
CC       {ECO:0000269|PubMed:25730866}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC       {ECO:0000305}.
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DR   EMBL; KM596502; AJT38688.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D4BSP3; -.
DR   SMR; A0A0D4BSP3; -.
DR   KEGG; ag:AJT38688; -.
DR   BioCyc; MetaCyc:MON-19776; -.
DR   BRENDA; 2.1.1.328; 12251.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR041698; Methyltransf_25.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF13649; Methyltransf_25; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   1: Evidence at protein level;
KW   Antibiotic biosynthesis; Methyltransferase; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..237
FT                   /note="N-demethylindolmycin N-methyltransferase"
FT                   /id="PRO_0000442338"
SQ   SEQUENCE   237 AA;  26296 MW;  DCDD4CD383DFDB9A CRC64;
     MHTDWETSES AEDYSRNTAA AQWEPMGYPA VFRSLALATT DSDNAPPILD YGCGPGFVDR
     HVAEKYGRRV IAVDISSSMI DLARSQHSHP LVTYRHVPDS QLDFLGDKEI GGCMSCFVLM
     QMADSDTQVE ICRRIRRTLA PGAMLAVLNT HPDSVGIQFA TLRNGEPDRV YQPGDPMTTV
     LTTDKGVLRL QDYYWRVTDY VHALEAAGFH EVTVEHLPPP PADPTPHPQF LLVRGTA