ID   IND1_STRGR              Reviewed;         329 AA.
AC   A0A0D4BS77;
DT   28-MAR-2018, integrated into UniProtKB/Swiss-Prot.
DT   27-MAY-2015, sequence version 1.
DT   03-AUG-2022, entry version 19.
DE   RecName: Full=Indolepyruvate C-methyltransferase {ECO:0000303|PubMed:809439};
DE            EC=2.1.1.47 {ECO:0000269|PubMed:25730866, ECO:0000269|PubMed:809439};
DE   AltName: Full=S-adenosylmethionine: indolepyruvate 3-methyltransferase {ECO:0000303|PubMed:809439};
GN   Name=ind1 {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:AJT38682.1};
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).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY
RP   REGULATION.
RX   PubMed=809439; DOI=10.1016/s0021-9258(19)40889-2;
RA   Speedie M.K., Hornemann U., Floss H.G.;
RT   "Isolation and characterization of tryptophan transaminase and
RT   indolepyruvate C-methyltransferase. Enzymes involved in indolmycin
RT   biosynthesis in Streptomyces griseus.";
RL   J. Biol. Chem. 250:7819-7825(1975).
CC   -!- FUNCTION: Involved in the biosynthesis of the antibiotic indolmycin, an
CC       inhibitor of the bacterial tryptophan-tRNA synthetases. Catalyzes the
CC       transfer of a methyl group from S-adenosyl-L-methionine to position 3
CC       of the aliphatic side chain of (indol-3-yl)pyruvate to yield 3-
CC       methylindolepyruvate. {ECO:0000269|PubMed:25730866,
CC       ECO:0000269|PubMed:809439}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=indole-3-pyruvate + S-adenosyl-L-methionine = (R)-3-(indol-3-
CC         yl)-2-oxobutanoate + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:12112, ChEBI:CHEBI:15378, ChEBI:CHEBI:17640,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:91180; EC=2.1.1.47;
CC         Evidence={ECO:0000269|PubMed:25730866, ECO:0000269|PubMed:809439};
CC   -!- ACTIVITY REGULATION: Strongly inhibited by the thiol reagents p-
CC       chloromercuribenzoate and N-ethylmaleimide. Partially inhibited by o-
CC       phenanthroline and 2,2'-dipyridyl. Competitively inhibited by L-
CC       tryptophan and indolmycin. {ECO:0000269|PubMed:809439}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=4.8 uM for indolepyruvate (at 30 degrees Celsius and pH 7.6)
CC         {ECO:0000269|PubMed:809439};
CC         KM=12 uM for S-adenosylmethionine (at 30 degrees Celsius and pH 7.6)
CC         {ECO:0000269|PubMed:809439};
CC       pH dependence:
CC         Optimum pH is 7.5-8.5. Loss of methyltransferase activity at pH 5.5
CC         and below. {ECO:0000269|PubMed:809439};
CC   -!- DISRUPTION PHENOTYPE: Cells laking this gene are unable to produce
CC       indolmycenate. {ECO:0000269|PubMed:25730866}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC       {ECO:0000305}.
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DR   EMBL; KM596502; AJT38682.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D4BS77; -.
DR   SMR; A0A0D4BS77; -.
DR   KEGG; ag:AJT38682; -.
DR   BioCyc; MetaCyc:MON-19774; -.
DR   GO; GO:0030747; F:indolepyruvate C-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR041698; Methyltransf_25.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR036388; WH-like_DNA-bd_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..329
FT                   /note="Indolepyruvate C-methyltransferase"
FT                   /id="PRO_0000443563"
SQ   SEQUENCE   329 AA;  35840 MW;  03C3EDBA8CD0A4F9 CRC64;
     MTRTDFAQSA VASIFTGAIA SHAAVLADDL GLFDALAKGK LRNRDLDRSP WLRNRIRISG
     ALEALCRVGA VQRCTDGYEL TDVGTELAGQ VPVFRLWLGG YASVLAGQIS IGADPATGVH
     GGIVAESSGA IGARYLDETI VNLLESLRPE GRICDIGCGT GARLLRVCRR VNQPGIGYDL
     SAKAVEAARE TVDEARRIGV DIDVRQGDAT ALTQDHPDVD IVTQAFMTHH IAPDEYCAAV
     LRSYRSRFPR ARYLVIFDTV PSQDSEEPEI FAPGFDYIHA LQNMEPRSRG AARRMFTEAG
     YICREEVELA VPNSYAWVLE MRDREGPAS