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OMT_CURCL
ID   OMT_CURCL               Reviewed;         422 AA.
AC   A0A348AXX3;
DT   12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT   07-NOV-2018, sequence version 1.
DT   03-AUG-2022, entry version 13.
DE   RecName: Full=O-methyltransferase {ECO:0000303|PubMed:29686660};
DE            Short=OMT {ECO:0000303|PubMed:29686660};
DE            EC=2.1.1.- {ECO:0000255|PROSITE-ProRule:PRU01020};
DE   AltName: Full=KK-1 biosynthesis cluster protein OMT {ECO:0000303|PubMed:29686660};
GN   Name=OMT {ECO:0000303|PubMed:29686660}; ORFNames=TRAF135002;
OS   Curvularia clavata.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Curvularia.
OX   NCBI_TaxID=95742;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PATHWAY.
RC   STRAIN=BAUA-2787;
RX   PubMed=29686660; DOI=10.3389/fmicb.2018.00690;
RA   Yoshimi A., Yamaguchi S., Fujioka T., Kawai K., Gomi K., Machida M.,
RA   Abe K.;
RT   "Heterologous Production of a Novel Cyclic Peptide Compound, KK-1, in
RT   Aspergillus oryzae.";
RL   Front. Microbiol. 9:690-690(2018).
CC   -!- FUNCTION: O-methyltransferase; part of the gene cluster that mediates
CC       the biosynthesis of KK-1, a novel cyclic decapeptide compound with
CC       potent antifungal activity (PubMed:29686660). The nonribosomal peptide
CC       synthetase (NRPS) catalyzes the elongation and cyclization of the
CC       decapeptide chain composed of 1 pipecolic acid residue (Pip), 1 alanine
CC       residue (Ala), 1 aspartic acid residue (Asp), 1 isoleucine residue
CC       (Ile), 1 glycine residue (Gly), 1 tyrosine residue (Tyr) and 4 valine
CC       residues (Val) (PubMed:29686660). The Asp, Ile and 3 Val residues are
CC       N-methylated by the 5 methyltransferase domains from the NRPS (found in
CC       modules 3, 5, 6, 7 and 9), whereas the Tyr residue is O-methylated,
CC       probably by the cluster encoded O-methyltransferase OMT
CC       (PubMed:29686660). The other tailoring enzymes from the cluster may be
CC       involved in further modifications leading to the synthesis of KK-1
CC       (Probable). {ECO:0000269|PubMed:29686660, ECO:0000305|PubMed:29686660}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000305|PubMed:29686660}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. Cation-independent O-methyltransferase family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01020}.
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DR   EMBL; LC371755; BBC83956.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A348AXX3; -.
DR   SMR; A0A348AXX3; -.
DR   GO; GO:0008171; F:O-methyltransferase activity; IEA:InterPro.
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; IPR016461; COMT-like.
DR   InterPro; IPR001077; O_MeTrfase_dom.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF00891; Methyltransf_2; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51683; SAM_OMT_II; 1.
PE   3: Inferred from homology;
KW   Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..422
FT                   /note="O-methyltransferase"
FT                   /id="PRO_0000450431"
FT   ACT_SITE        320
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         277
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
SQ   SEQUENCE   422 AA;  47992 MW;  88B64DB720B6B956 CRC64;
     MDPRQSRITE LAIAIKKQTE TLQSLLDSLK VATPSFSVNA NQELPRNAAV QLAQSSILDS
     CTELQDLVEG PLAHVGRIMS PRVHISSALQ AIVHFNIAEK IAKHETISFG EIAKRCKMDV
     DDVKRIMRLA ISYRIFKESH IGFVNHTASS FLIAENLLVR QWISLCCDEF IPAGSFLVPA
     MKKWPSSEEP NETAFALLHK GDSLWEVLKK QPEKAQRFAH GMEYMRTLPP FDINHLFTSL
     NWEIDCEMVL VDVGGSQGSI AEALLRRHPR LRCYVQDLPE TLSKAVVPKD LKGRLEFVSH
     SMFKEQPIKA DVYLLRSILH DWLDGYALQI IRNLIPALEV GSKVIINEIC LPEPNAISAY
     EAQLIRGYDL SMKQQFNSKE RDVHEWETLF RLADRRFKLN RIVNPPGSFL AVLEFEWQPT
     TP
 
 
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