ID   GRA3_CLAGR              Reviewed;         450 AA.
AC   E9KMQ4;
DT   10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT   05-APR-2011, sequence version 1.
DT   03-AUG-2022, entry version 26.
DE   RecName: Full=Grayanic acid biosynthesis cluster O-methyltransferase {ECO:0000303|PubMed:21289108};
DE            EC=2.1.1.- {ECO:0000305|PubMed:21289108};
OS   Cladonia grayi (Gray's cup lichen).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Lecanoromycetes;
OC   OSLEUM clade; Lecanoromycetidae; Lecanorales; Lecanorineae; Cladoniaceae;
OC   Cladonia.
OX   NCBI_TaxID=27339;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX   PubMed=21289108; DOI=10.3852/10-335;
RA   Armaleo D., Sun X., Culberson C.;
RT   "Insights from the first putative biosynthetic gene cluster for a lichen
RT   depside and depsidone.";
RL   Mycologia 103:741-754(2011).
RN   [2]
RP   FUNCTION.
RX   DOI=10.1016/0147-5975(92)90041-O;
RA   Culberson C., Armaleo D.;
RT   "Induction of a complete secondary-product pathway in a cultured lichen
RT   fungus.";
RL   Exp. Mycol. 16:52-63(1992).
CC   -!- FUNCTION: Non-reducing polyketide synthase; part of the gene cluster
CC       that mediates the biosynthesis of orcinol depsidone grayanic acid
CC       (GRA), the only major secondary metabolite known in C.grayi
CC       (PubMed:21289108). The first step consists in the ring and depside
CC       synthesis by PKS16 leading to 4-O-demethylsphaerophorin, involving
CC       different orcinol-like rings, one with acetyl CoA and the other with
CC       octanoyl CoA as the starter (Probable). Further depsidone formation by
CC       the GRA cluster-specific cytochrome P450 leads to 4-O-demethylgrayanic
CC       acid (Probable). Finally, the cluster specific O-methyltransferase
CC       probably converts the 4-O-demethylgrayanic acid into grayanic acid
CC       (Probable). {ECO:0000269|PubMed:21289108, ECO:0000305|PubMed:21289108,
CC       ECO:0000305|Ref.2}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000305|PubMed:21289108}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. Cation-independent O-methyltransferase family. COMT
CC       subfamily. {ECO:0000305}.
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DR   EMBL; GU930713; ADM79461.1; -; Genomic_DNA.
DR   BioCyc; MetaCyc:MON-21841; -.
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   Pfam; PF00891; Methyltransf_2; 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..450
FT                   /note="Grayanic acid biosynthesis cluster O-
FT                   methyltransferase"
FT                   /id="PRO_0000445369"
FT   REGION          408..432
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        301
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         254
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
SQ   SEQUENCE   450 AA;  50314 MW;  B3C18F12CBB5AB87 CRC64;
     MISEIAKLAA LVLTNTVKVD DFLQSSKLPP PTFHEDGPID LGLSPEVEAA RVAAIESSLR
     LHDLLXGPVE LIRPTVNAXS LEAIYKYDVA SKVPIHGEIP IIELAXQCKM NEPDLRRILR
     FAIIHHRVFQ EPRKGIITHS AASRRLVEDS AARDGLGLQF DDAWQSFARG FSLAHNTDKS
     VFEYMEAHPE KAKRFAGAMS SFSSYRGHGP EYLARGFPWA SLGTKTVVDV GGSEGKYSIA
     LAKSFPQLKF IVQDLPAVVR AVNAKRPIPL ELEDRVTFME HDMFTEQPVS ADVYMFRFVF
     HDWPDKYVVN ILRRLIPALK PGARIIISDS ILPEPNTLSE LYERKIRALD MVMLSFFNSR
     ERERDDWERV CQEVDPRFKF VDAWVPEGAA LGIIEAVWQP EPTMEXPKAI ESDESSSTGV
     XDSAKGIKGM ESNGRNGXIS VTCVDDVDVN