FSA4_FUSSF
ID FSA4_FUSSF Reviewed; 359 AA.
AC A0A0E3VJW8;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 24-JUN-2015, sequence version 1.
DT 03-AUG-2022, entry version 18.
DE RecName: Full=Methyltransferase fsa4 {ECO:0000303|PubMed:25770422};
DE EC=2.1.1.- {ECO:0000305|PubMed:25770422};
DE AltName: Full=Fusarisetin A biosynthesis protein 4 {ECO:0000303|PubMed:25770422};
GN Name=fsa4 {ECO:0000303|PubMed:25770422};
OS Fusarium sp. (strain FN080326).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=1608308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE, AND
RP PATHWAY.
RX PubMed=25770422; DOI=10.1016/j.bbrc.2015.03.011;
RA Kato N., Nogawa T., Hirota H., Jang J.H., Takahashi S., Ahn J.S., Osada H.;
RT "A new enzyme involved in the control of the stereochemistry in the decalin
RT formation during equisetin biosynthesis.";
RL Biochem. Biophys. Res. Commun. 460:210-215(2015).
RN [2]
RP FUNCTION.
RX PubMed=28401214; DOI=10.1039/c7cc01929g;
RA Li X., Zheng Q., Yin J., Liu W., Gao S.;
RT "Chemo-enzymatic synthesis of equisetin.";
RL Chem. Commun. (Camb.) 53:4695-4697(2017).
RN [3]
RP FUNCTION.
RX PubMed=29972614; DOI=10.1002/anie.201805050;
RA Kato N., Nogawa T., Takita R., Kinugasa K., Kanai M., Uchiyama M.,
RA Osada H., Takahashi S.;
RT "Control of the stereochemical course of [4+2] cycloaddition during trans-
RT decalin formation by Fsa2-family enzymes.";
RL Angew. Chem. Int. Ed. 57:9754-9758(2018).
RN [4]
RP FUNCTION.
RX PubMed=34121297; DOI=10.1002/anie.202106186;
RA Fujiyama K., Kato N., Re S., Kinugasa K., Watanabe K., Takita R.,
RA Nogawa T., Hino T., Osada H., Sugita Y., Takahashi S., Nagano S.;
RT "Molecular basis for two stereoselective Diels-Alderases that produce
RT decalin skeletons*.";
RL Angew. Chem. Int. Ed. 60:22401-22410(2021).
CC -!- FUNCTION: Methyltransferase; part of the gene cluster that mediates the
CC biosynthesis of HIV-1 integrase inhibitor equisetin and of fusarisetin
CC A, both trans-fused decalin-containing tetramic acids showing also
CC antimicrobial activity (PubMed:25770422). The PKS module of fsa1
CC together with the enoylreductase fsa3 catalyze the formation of the
CC polyketide unit which is then conjugated to L-serine by the
CC condensation domain of the fsa1 NRPS module (PubMed:25770422). Activity
CC of the Dieckmann cyclase domain (RED) results in release of the
CC Dieckmann product intermediate (PubMed:25770422). Diels-Alderase fsa2
CC is involved in endo-selective Diels-Alder cycloaddition to form the
CC decalin ring, leading to the production of N-desmethylequisetin also
CC called trichosetin (PubMed:25770422, PubMed:28401214, PubMed:29972614,
CC PubMed:34121297). Subsequent N-methylation is carried out by fsa4 to
CC give equisetin (PubMed:25770422). The enzymatic gene responsible for
CC the conversion of equisetin to fusarisetin A has not been identified
CC yet and is probably located outside of the fsa cluster
CC (PubMed:28401214). {ECO:0000269|PubMed:25770422,
CC ECO:0000269|PubMed:28401214, ECO:0000269|PubMed:29972614,
CC ECO:0000269|PubMed:34121297}.
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:25770422}.
CC -!- DISRUPTION PHENOTYPE: Results in the loss of production of equisetin
CC and fusarisetin A (PubMed:25770422). {ECO:0000269|PubMed:25770422}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Cation-independent O-methyltransferase family.
CC {ECO:0000305}.
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DR EMBL; LC025956; BAR40286.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0E3VJW8; -.
DR SMR; A0A0E3VJW8; -.
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 PIRSF; PIRSF005739; O-mtase; 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..359
FT /note="Methyltransferase fsa4"
FT /id="PRO_0000441299"
FT BINDING 198..199
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O04385"
FT BINDING 224
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 248..249
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O04385"
FT BINDING 264
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O04385"
FT BINDING 265
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
SQ SEQUENCE 359 AA; 39665 MW; 47AB0D6FBF4465DB CRC64;
MSSILSRYPE AETPVHGYFY SMVELAVVRV FVQHQIFDAI ADDGTSIEEL ATKTGMELNL
LERLSNFLVA SKVLSSPKPG FIGLPSETKM FQQRRAKLFY SHIFDAFMGS AVKWPQYLQN
NGLAEPQKSN RSPFGLGAGY PDKSFYDVLE MMPERAQAFN STMAIGLGDM PITGIYDFSW
VAAHSGTDPE RTLIVDVGGG KGQAIKAIVE ETPSIPASAC VLQDLPNVIK DVPEEEGILN
QVQKVGSSFF DKQPTKGALV YYIRRVLNDW PDDECVTILK NIREACASDS RLLISENLLP
DEPSVSLAAA DLWMMNFAGK RRNVRMFNDL ASRSGFEISS IAKDKTSNSA VIEMLPVQI
