ID   MEKOS_HERA2             Reviewed;         283 AA.
AC   A9AWD7;
DT   25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=(+)-O-methylkolavelool synthase {ECO:0000303|Ref.1};
DE            EC=2.1.1.347 {ECO:0000269|Ref.1};
DE   AltName: Full=S-adenosyl-L-methionine:(+)-kolavelool O-methyltransferase {ECO:0000305|Ref.1};
GN   OrderedLocusNames=Haur_2147 {ECO:0000312|EMBL:ABX04787.1};
OS   Herpetosiphon aurantiacus (strain ATCC 23779 / DSM 785 / 114-95).
OC   Bacteria; Chloroflexi; Chloroflexia; Herpetosiphonales; Herpetosiphonaceae;
OC   Herpetosiphon.
OX   NCBI_TaxID=316274;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23779 / DSM 785 / 114-95 {ECO:0000312|Proteomes:UP000000787};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Bryant D.A., Richardson P.;
RT   "Complete sequence of chromosome of Herpetosiphon aurantiacus ATCC 23779.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=ATCC 23779 / DSM 785 / 114-95;
RX   PubMed=25694050; DOI=10.1002/cbic.201402652;
RA   Nakano C., Oshima M., Kurashima N., Hoshino T.;
RT   "Identification of a new diterpene biosynthetic gene cluster that produces
RT   O-methylkolavelool in Herpetosiphon aurantiacus.";
RL   ChemBioChem 16:772-781(2015).
CC   -!- FUNCTION: Involved in the biosynthesis of (+)-O-methylkolavelool.
CC       Catalyzes the addition of a methoxy group to the C-13 position via the
CC       transfer of a methyl group from S-adenosyl-L-methionine to (+)-
CC       kolavelool to form (+)-O-methylkolavelooldaunorubicin.
CC       {ECO:0000269|PubMed:25694050}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(+)-kolavelool + S-adenosyl-L-methionine = (+)-O-
CC         methylkolavelool + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:55968, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:138313, ChEBI:CHEBI:139480;
CC         EC=2.1.1.347; Evidence={ECO:0000269|Ref.1};
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC       {ECO:0000305}.
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DR   EMBL; CP000875; ABX04787.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9AWD7; -.
DR   SMR; A9AWD7; -.
DR   STRING; 316274.Haur_2147; -.
DR   EnsemblBacteria; ABX04787; ABX04787; Haur_2147.
DR   KEGG; hau:Haur_2147; -.
DR   eggNOG; COG2230; Bacteria.
DR   HOGENOM; CLU_039068_6_0_0; -.
DR   OMA; GQDAWCY; -.
DR   BioCyc; HAUR316274:GHYA-2175-MON; -.
DR   BRENDA; 2.1.1.347; 2656.
DR   Proteomes; UP000000787; Chromosome.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   1: Evidence at protein level;
KW   Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..283
FT                   /note="(+)-O-methylkolavelool synthase"
FT                   /id="PRO_0000443954"
FT   BINDING         106
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q8KZ94"
FT   BINDING         129..130
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q8KZ94"
FT   BINDING         151
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q8KZ94"
SQ   SEQUENCE   283 AA;  31572 MW;  271C25426EB62C74 CRC64;
     MTVLSTDIPA PNSPSISDVE AYYDAMGPFY KLIWGDSVHG GYWPAGLEDM SLPEAQEHLT
     NLMIEKTPIK PGQHMLDLGC GTGLPAIRMA SAKQCHVHGL TVAHGQVAEA QATIQAMQMQ
     ELVHINWGNA MELPFEADFF NAAWAFESIF HMPSRLTVLQ EANRVLQAGS YFVLTDIVEV
     KSLSPEQQQI FFPAFQINTL TTKQGYLDLF AQTGFEQLEL IDLTAGIEKT LAHTKLGIEQ
     KRAELAAIYP PEMLGMIEQT WPMVEKIYAE FVRYVLIVAR KRG