AFVC_ASPFN
ID AFVC_ASPFN Reviewed; 410 AA.
AC B8N8R1;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=O-methyltransferase afvC {ECO:0000303|PubMed:26209694};
DE EC=2.1.1.- {ECO:0000305|PubMed:26209694};
DE AltName: Full=Aflavarin synthesis protein C {ECO:0000303|PubMed:26209694};
GN Name=afvC {ECO:0000303|PubMed:26209694}; ORFNames=AFLA_108560;
OS Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS / JCM 12722 / SRRC 167).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=332952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC 167;
RX PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT aflatoxin contamination of food and feed.";
RL Genome Announc. 3:E0016815-E0016815(2015).
RN [2]
RP FUNCTION.
RX DOI=10.1021/np50086a008;
RA TePaske M.R., Gloer J.B., Wicklow D.T., Dowd P.F.;
RT "Aflavarin and beta-aflatrem: new anti-insectan metabolites from the
RT sclerotia of Aspergillus flavus.";
RL J. Nat. Prod. 55:1080-1086(1992).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26209694; DOI=10.1128/ec.00092-15;
RA Cary J.W., Han Z., Yin Y., Lohmar J.M., Shantappa S., Harris-Coward P.Y.,
RA Mack B., Ehrlich K.C., Wei Q., Arroyo-Manzanares N., Uka V., Vanhaecke L.,
RA Bhatnagar D., Yu J., Nierman W.C., Johns M.A., Sorensen D., Shen H.,
RA De Saeger S., Diana Di Mavungu J., Calvo A.M.;
RT "Transcriptome analysis of Aspergillus flavus reveals veA-dependent
RT regulation of secondary metabolite gene clusters, including the novel
RT aflavarin cluster.";
RL Eukaryot. Cell 14:983-997(2015).
CC -!- FUNCTION: O-methyltransferase; part of the gene cluster that mediates
CC the biosynthesis of aflavarin, a bicoumarin that exhibits anti-insectan
CC activity against the fungivorous beetle C.hemipterus (Ref.2,
CC PubMed:26209694). {ECO:0000269|PubMed:26209694, ECO:0000269|Ref.2}.
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000305|PubMed:26209694}.
CC -!- INDUCTION: Expression is induced by the developmental and secondary
CC metabolism regulator veA (PubMed:26209694).
CC {ECO:0000269|PubMed:26209694}.
CC -!- DISRUPTION PHENOTYPE: Fails to produce aflavarin (PubMed:26209694).
CC {ECO:0000269|PubMed:26209694}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Cation-independent O-methyltransferase family. COMT
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU01020}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; EQ963475; EED53480.1; -; Genomic_DNA.
DR RefSeq; XP_002376726.1; XM_002376685.1.
DR AlphaFoldDB; B8N8R1; -.
DR SMR; B8N8R1; -.
DR EnsemblFungi; EED53480; EED53480; AFLA_108560.
DR VEuPathDB; FungiDB:AFLA_108560; -.
DR eggNOG; KOG3178; Eukaryota.
DR HOGENOM; CLU_005533_5_2_1; -.
DR OMA; YLRPEIR; -.
DR Proteomes; UP000001875; Unassembled WGS sequence.
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 2: Evidence at transcript level;
KW Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..410
FT /note="O-methyltransferase afvC"
FT /id="PRO_0000436113"
FT ACT_SITE 319
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 253..254
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O04385"
FT BINDING 278
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O04385"
FT BINDING 299..300
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O04385"
FT BINDING 315
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O04385"
SQ SEQUENCE 410 AA; 46385 MW; E55234C5DA9B091B CRC64;
MEVSEERDLY LHSITAALER LNSAASECQS RLLSEHDGSI EDHSANQTAH DNLVQEAYKF
LQIAQGPIDT VATCFERTAH VACARSLLEM GAFEGLPIGG ESRSTKELAE DLSVDEALLA
RLMRNSALFE ETGPNQYRHT PFSEAYLRPE IRAMFRFAMD EHMPAHLKMH EFLKSNSWTE
PTSTSNNPYT YAHDTNGKSM WEYLSERPTR MASFNDGMTL QAMTELWMID LFPWESLSDQ
QPTPTTVVAV DIGGGTGMGI SRIRSYCCSL PGKFILQDQA HVIQSADPRG NGIEKMAYDF
FEEQPIRGAL TYLIRRCLHN WPQESIIQIL KNVAAAMQPE KSRLLIEEII VPDMNAGIEE
GWMDMIMMNL GAKQRTLKEW EEVLALAGFE VRKIYQIPGN CHGLLEVWLK
