ATR3_STEAL
ID ATR3_STEAL Reviewed; 346 AA.
AC A0A8F4PN06;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2022, sequence version 1.
DT 03-AUG-2022, entry version 3.
DE RecName: Full=O-methyltransferase atr3 {ECO:0000303|PubMed:34154413};
DE EC=2.1.3.- {ECO:0000269|PubMed:34154413};
DE AltName: Full=Atranorin biosynthesis cluster protein 3 {ECO:0000303|PubMed:34154413};
GN Name=atr3 {ECO:0000303|PubMed:34154413};
OS Stereocaulon alpinum (Alpine snow lichen) (Stereocaulon paschale var.
OS alpinum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Lecanoromycetes;
OC OSLEUM clade; Lecanoromycetidae; Lecanorales; Lecanorineae;
OC Stereocaulaceae; Stereocaulon.
OX NCBI_TaxID=350623;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP PATHWAY.
RX PubMed=34154413; DOI=10.1128/mbio.01111-21;
RA Kim W., Liu R., Woo S., Kang K.B., Park H., Yu Y.H., Ha H.H., Oh S.Y.,
RA Yang J.H., Kim H., Yun S.H., Hur J.S.;
RT "Linking a gene cluster to atranorin, a major cortical substance of
RT lichens, through genetic dereplication and heterologous expression.";
RL MBio 12:e0111121-e0111121(2021).
CC -!- FUNCTION: O-methyltransferase; part of the gene cluster that mediates
CC the biosynthesis of atranorin, a depside of polyketide origin that
CC accumulates in the cortical or medullary layers of lichen thalli
CC (PubMed:34154413). Atr3 methylates the carboxyl group of 4-O-
CC demethylbarbatic acid to yield proatranorin I (PubMed:34154413). Atr3
CC is also able to methylate the atr2 product proatranorin III to produce
CC the final compound atranorin (PubMed:34154413). The first step in the
CC pathway is performed by the non-reducing polyketide synthase atr1 that
CC produces 4-O-demethylbarbatic acid composed of two 3-methylorsellinic
CC acid (3MOA) moieties. The pathway continues with the actions of the
CC cytochrome P450 monooygenase atr2 that catalizes the oxidation of c-9
CC and the O-methyltransferase atr3 that performs the methylation of the
CC carboxyl group to yield atranorin, via the proatranorin II and III
CC intermediates if atr2 acts first, or the proatranorin I intermediate if
CC atr3 acts first (PubMed:34154413). {ECO:0000269|PubMed:34154413}.
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000269|PubMed:34154413}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q3J7D1}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. {ECO:0000305}.
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DR EMBL; MZ277877; QXF68951.1; -; Genomic_DNA.
DR UniPathway; UPA00213; -.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR041698; Methyltransf_25.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF13649; Methyltransf_25; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..346
FT /note="O-methyltransferase atr3"
FT /id="PRO_0000455743"
FT BINDING 190..191
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q3J7D1"
FT BINDING 217..218
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q3J7D1"
FT BINDING 218..219
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q3J7D1"
SQ SEQUENCE 346 AA; 38717 MW; 3F2AF174028FB26B CRC64;
MTSVDTMPPP MVRLESQPDD LMGSSDVADV SDLLPGHTNG LEDEVKIPAT NGLKSHPVVT
TGTEKTGVMP PLQPESKKNN KGVPWYHASP NDIDPVTRGL LENYSKIPSD QVQQHVIAIR
EKAWDVYPYP CIGQFLFLNL TINLSPYYPS LVSRLRDQNQ TLLDLGCCFA QDVRKLVSDG
APSQNIYGAD LYGEFMDLGF ELFRDRKTLK STFFPTDILN ERDLLLKGLD GEMDVVYLGL
FLHHFDFETC VKVCTRVTRL LKPKPGSLVM GVQVGSLVGD TKPIPIPSGG ILWRHDIASL
ERVWEEVGAL TGTKWKVEAR LERGKGFGEK WQLEGTRRLG FEVYRL
