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