OMTA_ASPFN
ID OMTA_ASPFN Reviewed; 418 AA.
AC P55790; B8NHY5; Q00051;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Sterigmatocystin 8-O-methyltransferase;
DE EC=2.1.1.110;
DE Flags: Precursor;
GN Name=omtA; Synonyms=AflP, omt-1; ORFNames=AFLA_139210;
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 [GENOMIC DNA].
RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC 167;
RX PubMed=7557460; DOI=10.1016/0378-1119(95)00397-o;
RA Yu J., Chang P.-K., Payne G.A., Cary J.W., Bhatnagar D., Cleveland T.E.;
RT "Comparison of the omtA genes encoding O-methyltransferases involved in
RT aflatoxin biosynthesis from Aspergillus parasiticus and A. flavus.";
RL Gene 163:121-125(1995).
RN [2]
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).
CC -!- FUNCTION: Involved in the conversion of sterigmatocystin to O-
CC methylsterigmatocystin (OMST) and dihydrosterigmatocystin to dihydro-o-
CC methylsterigmatocystin in the aflatoxin biosynthesis pathway.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-adenosyl-L-methionine + sterigmatocystin = 8-O-
CC methylsterigmatocystin + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:15561, ChEBI:CHEBI:15378, ChEBI:CHEBI:18171,
CC ChEBI:CHEBI:18227, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789;
CC EC=2.1.1.110;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dihydrosterigmatocystin + S-adenosyl-L-methionine = 8-O-
CC methyldihydrosterigmatocystin + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:35767, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:72677, ChEBI:CHEBI:72678;
CC EC=2.1.1.110;
CC -!- PATHWAY: Mycotoxin biosynthesis; aflatoxin biosynthesis.
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}.
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DR EMBL; L25836; AAA32698.1; -; Genomic_DNA.
DR EMBL; EQ963478; EED51156.1; -; Genomic_DNA.
DR RefSeq; XP_002379932.1; XM_002379891.1.
DR AlphaFoldDB; P55790; -.
DR SMR; P55790; -.
DR STRING; 5059.CADAFLAP00007797; -.
DR EnsemblFungi; EED51156; EED51156; AFLA_139210.
DR VEuPathDB; FungiDB:AFLA_139210; -.
DR eggNOG; KOG3178; Eukaryota.
DR OMA; LISHACD; -.
DR UniPathway; UPA00287; -.
DR Proteomes; UP000001875; Unassembled WGS sequence.
DR GO; GO:0047146; F:sterigmatocystin 7-O-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0045122; P:aflatoxin biosynthetic process; IEA:UniProtKB-UniPathway.
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 PROPEP 1..41
FT /evidence="ECO:0000250|UniProtKB:Q12120"
FT /id="PRO_0000021896"
FT CHAIN 42..418
FT /note="Sterigmatocystin 8-O-methyltransferase"
FT /id="PRO_0000021897"
FT REGION 206..225
FT /note="Substrate binding"
FT /evidence="ECO:0000250"
FT ACT_SITE 317
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 170..176
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 254..255
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O04385"
FT BINDING 277
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O04385"
FT BINDING 297..298
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O04385"
FT BINDING 313
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O04385"
SQ SEQUENCE 418 AA; 46776 MW; 413BC8388CCC2CDA CRC64;
MTLPNKAALV GLAHTLSEQV KRYLVTADET KSPEDHKLCI EGERTPSSTE HAQAWEIVRT
CDRIGSLVHG PVPWLLSNAL SHLDSACLAA ATQLNLQDII VDGPSPTSLD TIVTATGVSE
DLLRRILRGC AQRFIFEEVA PDQYAHTDAS KMLRVTGIHA LVGFSCDEVM RSAAYFSNFL
QQTKGKPPSW NVPSPFSLAF DPTKGLFDYY STVDEVRGRR FDLGMGGTEA TKPLVEEMFD
FSSLPEGSTV VDVGGGRGHL SRRVSQKHPH LRFIVQDLPA VIHGVEDTDK VTMMEHDIRR
RNPVRGADVY LLRSILHDYP DAACVEILSN IVTAMDPSKS RILLDEMIMP DLLAQDSQRF
MNQIDMTVVL TLNGKERSTK EWNSLITMVD NRLETEKIWW RKGEEGSHWG VQQLRLRK
