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Demethylsterigmatocystin 6-O-methyltransferase (EC 2.1.1.109) (Aflatoxin biosynthesis protein O) (O-methyltransferase I) (mt-I)

 AFLO_ASPPU              Reviewed;         386 AA.
Q9UQY0; A0A0F0HZ60; Q6UEF8;
01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 2.
25-OCT-2017, entry version 66.
RecName: Full=Demethylsterigmatocystin 6-O-methyltransferase {ECO:0000305|PubMed:10543813};
EC=2.1.1.109 {ECO:0000269|PubMed:10543813, ECO:0000269|PubMed:16349476};
AltName: Full=Aflatoxin biosynthesis protein O {ECO:0000303|PubMed:15006741};
AltName: Full=O-methyltransferase I {ECO:0000303|PubMed:10543813};
Short=mt-I {ECO:0000303|PubMed:10543813};
Name=aflO {ECO:0000303|PubMed:15006741};
Synonyms=dmtA {ECO:0000303|PubMed:10543813},
omtB {ECO:0000303|PubMed:10806361}; ORFNames=P875_00052999-2;
Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 /
SU-1).
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
NCBI_TaxID=1403190;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PROTEIN SEQUENCE OF 2-47,
FUNCTION, PATHWAY, AND CATALYTIC ACTIVITY.
STRAIN=NIAH-26;
PubMed=10543813;
Motomura M., Chihaya N., Shinozawa T., Hamasaki T., Yabe K.;
"Cloning and characterization of the O-methyltransferase I gene (dmtA)
from Aspergillus parasiticus associated with the conversions of
demethylsterigmatocystin to sterigmatocystin and
dihydrodemethylsterigmatocystin to dihydrosterigmatocystin in
aflatoxin biosynthesis.";
Appl. Environ. Microbiol. 65:4987-4994(1999).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1;
PubMed=10806361; DOI=10.1016/S0378-1119(00)00126-8;
Yu J., Woloshuk C.P., Bhatnagar D., Cleveland T.E.;
"Cloning and characterization of avfA and omtB genes involved in
aflatoxin biosynthesis in three Aspergillus species.";
Gene 248:157-167(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1;
Yu J., Fedorova N., Yin Y., Losada L., Zafar N., Taujale R.,
Ehrlich K.C., Bhatnagar D., Cleveland T.E., Bennett J.W.,
Nierman W.C.;
"Draft genome sequence of Aspergillus parasiticus SU-1.";
Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
[4]
FUNCTION.
PubMed=1339261;
Skory C.D., Chang P.K., Cary J., Linz J.E.;
"Isolation and characterization of a gene from Aspergillus parasiticus
associated with the conversion of versicolorin A to sterigmatocystin
in aflatoxin biosynthesis.";
Appl. Environ. Microbiol. 58:3527-3537(1992).
[5]
FUNCTION.
PubMed=8434913;
Keller N.P., Dischinger H.C. Jr., Bhatnager D., Cleveland T.E.,
Ullah A.H.J.;
"Purification of a 40-kilodalton methyltransferase active in the
aflatoxin biosynthetic pathway.";
Appl. Environ. Microbiol. 59:479-484(1993).
[6]
FUNCTION.
PubMed=8368836;
Yabe K., Matsuyama Y., Ando Y., Nakajima H., Hamasaki T.;
"Stereochemistry during aflatoxin biosynthesis: conversion of
norsolorinic acid to averufin.";
Appl. Environ. Microbiol. 59:2486-2492(1993).
[7]
FUNCTION.
PubMed=8368837;
Yabe K., Hamasaki T.;
"Stereochemistry during aflatoxin biosynthesis: cyclase reaction in
the conversion of versiconal to versicolorin B and racemization of
versiconal hemiacetal acetate.";
Appl. Environ. Microbiol. 59:2493-2500(1993).
[8]
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND CATALYTIC ACTIVITY.
PubMed=16349476;
Yabe K., Matsushima K., Koyama T., Hamasaki T.;
"Purification and characterization of O-methyltransferase I involved
in conversion of demethylsterigmatocystin to sterigmatocystin and of
dihydrodemethylsterigmatocystin to dihydrosterigmatocystin during
aflatoxin biosynthesis.";
Appl. Environ. Microbiol. 64:166-171(1998).
[9]
FUNCTION.
PubMed=10584035;
Zhou R., Linz J.E.;
"Enzymatic function of the nor-1 protein in aflatoxin biosynthesis in
Aspergillus parasiticus.";
Appl. Environ. Microbiol. 65:5639-5641(1999).
[10]
FUNCTION.
PubMed=11055914; DOI=10.1128/AEM.66.11.4715-4719.2000;
Chang P.K., Yu J., Ehrlich K.C., Boue S.M., Montalbano B.G.,
Bhatnagar D., Cleveland T.E.;
"adhA in Aspergillus parasiticus is involved in conversion of 5'-
hydroxyaverantin to averufin.";
Appl. Environ. Microbiol. 66:4715-4719(2000).
[11]
FUNCTION.
PubMed=16256699; DOI=10.1006/bioo.2001.1216;
Hitchman T.S., Schmidt E.W., Trail F., Rarick M.D., Linz J.E.,
Townsend C.A.;
"Hexanoate synthase, a specialized type I fatty acid synthase in
aflatoxin B1 biosynthesis.";
Bioorg. Chem. 29:293-307(2001).
[12]
FUNCTION.
PubMed=11996570; DOI=10.1021/ja012185v;
Udwary D.W., Casillas L.K., Townsend C.A.;
"Synthesis of 11-hydroxyl O-methylsterigmatocystin and the role of a
cytochrome P-450 in the final step of aflatoxin biosynthesis.";
J. Am. Chem. Soc. 124:5294-5303(2002).
[13]
REVIEW, FUNCTION, PATHWAY, AND NOMENCLATURE.
PubMed=15006741; DOI=10.1128/AEM.70.3.1253-1262.2004;
Yu J., Chang P.K., Ehrlich K.C., Cary J.W., Bhatnagar D.,
Cleveland T.E., Payne G.A., Linz J.E., Woloshuk C.P., Bennett J.W.;
"Clustered pathway genes in aflatoxin biosynthesis.";
Appl. Environ. Microbiol. 70:1253-1262(2004).
[14]
FUNCTION.
PubMed=15528514; DOI=10.1128/AEM.70.11.6518-6524.2004;
Ehrlich K.C., Chang P.K., Yu J., Cotty P.J.;
"Aflatoxin biosynthesis cluster gene cypA is required for G aflatoxin
formation.";
Appl. Environ. Microbiol. 70:6518-6524(2004).
[15]
FUNCTION.
PubMed=15932995; DOI=10.1128/AEM.71.6.2999-3006.2005;
Sakuno E., Wen Y., Hatabayashi H., Arai H., Aoki C., Yabe K.,
Nakajima H.;
"Aspergillus parasiticus cyclase catalyzes two dehydration steps in
aflatoxin biosynthesis.";
Appl. Environ. Microbiol. 71:2999-3006(2005).
[16]
FUNCTION.
PubMed=16332900; DOI=10.1128/AEM.71.12.8963-8965.2005;
Ehrlich K.C., Montalbano B., Boue S.M., Bhatnagar D.;
"An aflatoxin biosynthesis cluster gene encodes a novel oxidase
required for conversion of versicolorin a to sterigmatocystin.";
Appl. Environ. Microbiol. 71:8963-8965(2005).
[17]
FUNCTION.
PubMed=15771506; DOI=10.1021/ja0455188;
Henry K.M., Townsend C.A.;
"Ordering the reductive and cytochrome P450 oxidative steps in
demethylsterigmatocystin formation yields general insights into the
biosynthesis of aflatoxin and related fungal metabolites.";
J. Am. Chem. Soc. 127:3724-3733(2005).
[18]
FUNCTION.
PubMed=16461654; DOI=10.1128/AEM.72.2.1096-1101.2006;
Cary J.W., Ehrlich K.C., Bland J.M., Montalbano B.G.;
"The aflatoxin biosynthesis cluster gene, aflX, encodes an
oxidoreductase involved in conversion of versicolorin A to
demethylsterigmatocystin.";
Appl. Environ. Microbiol. 72:1096-1101(2006).
[19]
FUNCTION.
PubMed=18486503; DOI=10.1016/j.fgb.2008.03.003;
Cai J., Zeng H., Shima Y., Hatabayashi H., Nakagawa H., Ito Y.,
Adachi Y., Nakajima H., Yabe K.;
"Involvement of the nadA gene in formation of G-group aflatoxins in
Aspergillus parasiticus.";
Fungal Genet. Biol. 45:1081-1093(2008).
[20]
FUNCTION.
PubMed=18403714; DOI=10.1126/science.1154711;
Crawford J.M., Thomas P.M., Scheerer J.R., Vagstad A.L.,
Kelleher N.L., Townsend C.A.;
"Deconstruction of iterative multidomain polyketide synthase
function.";
Science 320:243-246(2008).
-!- FUNCTION: Demethylsterigmatocystin 6-O-methyltransferase; part of
the gene cluster that mediates the biosynthesis of aflatoxins, a
group of polyketide-derived furanocoumarins, and part of the most
toxic and carcinogenic compounds among the known mycotoxins
(PubMed:15006741). The four major aflatoxins produced by
A.parasiticus are aflatoxin B1 (AFB1), aflatoxin B2 (AFB2),
aflatoxin G1 (AFG1) and aflatoxin G2 (AFG2) (PubMed:15006741). The
first step of the pathway is the conversion of acetate to
norsolorinic acid (NOR) and requires the fatty acid synthase
subunits aflA and aflB, as well as the PKS aflC (PubMed:15006741).
AflC combines a hexanoyl starter unit and 7 malonyl-CoA extender
units to synthesize the precursor NOR (PubMed:18403714). The
hexanoyl starter unit is provided to the acyl-carrier protein
(ACP) domain by the fungal fatty acid synthase aflA/aflB
(PubMed:16256699). The second step is the conversion of NOR to
averantin (AVN) and requires the norsolorinic acid ketoreductase
aflD, which catalyzes the dehydration of norsolorinic acid to form
(1'S)-averantin (PubMed:10584035). The norsolorinic acid
reductases aflE and aflF may also play a role in the conversion of
NOR to AVN (PubMed:15006741). The cytochrome P450 monooxygenase
aflG then catalyzes the hydroxylation of AVN to 5'hydroxyaverantin
(HAVN) (PubMed:8368836). The next step is performed by the 5'-
hydroxyaverantin dehydrogenase aflH that transforms HAVN to 5'-
oxoaverantin (OAVN) which is further converted to averufin (AVF)
by aflK that plays a dual role in the pathway, as a 5'-
oxoaverantin cyclase that mediates conversion of 5'-oxoaverantin,
as well as a versicolorin B synthase in a later step in the
pathway (PubMed:15006741, PubMed:11055914, PubMed:15932995). The
averufin oxidase aflI catalyzes the conversion of AVF to
versiconal hemiacetal acetate (VHA) (PubMed:15006741). VHA is then
the substrate for the versiconal hemiacetal acetate esterase aflJ
to yield versiconal (VAL) (PubMed:15006741). Versicolorin B
synthase aflK then converts VAL to versicolorin B (VERB) by
closing the bisfuran ring of aflatoxin which is required for DNA-
binding, thus giving to aflatoxin its activity as a mutagen
(PubMed:15006741, PubMed:8368837, PubMed:15932995). Then, the
activity of the versicolorin B desaturase aflL leads to
versicolorin A (VERA) (PubMed:15006741, PubMed:8368837). A branch
point starts from VERB since it can also be converted to
dihydrodemethylsterigmatocystin (DMDHST), probably also by aflL,
VERA being a precursor for aflatoxins B1 and G1, and DMDHST for
aflatoxins B2 and G2 (PubMed:15006741). Next, the versicolorin
reductase aflM and the cytochrome P450 monooxygenase aflN are
involved in conversion of VERA to demethylsterigmatocystin (DMST)
(PubMed:15006741, PubMed:1339261, PubMed:15771506). AflX and aflY
seem also involved in this step, through probable aflX-mediated
epoxide ring-opening step following versicolorin A oxidation and
aflY-mediated Baeyer-Villiger oxidation required for the formation
of the xanthone ring (PubMed:16332900, PubMed:16461654). The
methyltransferase aflO then leads to the modification of DMST to
sterigmatocystin (ST), and of DMDHST to dihydrosterigmatocystin
(DHST) (PubMed:10543813, PubMed:10806361, PubMed:16349476). Both
ST and DHST are then substrates of the O-methyltransferase aflP to
yield O-methylsterigmatocystin (OMST) and dihydro-O-
methylsterigmatocystin (DHOMST), respectively (PubMed:8434913).
Finally OMST is converted to aflatoxins B1 and G1, and DHOMST to
aflatoxins B2 and G2, via the action of several enzymes including
O-methylsterigmatocystin oxidoreductase aflQ, the cytodhrome P450
monooxygenase aflU, but also the NADH-dependent flavin
oxidoreductase nadA which is specifically required for the
synthesis of AFG1 (PubMed:15006741, PubMed:11996570,
PubMed:15528514, PubMed:18486503). {ECO:0000269|PubMed:10543813,
ECO:0000269|PubMed:10584035, ECO:0000269|PubMed:10806361,
ECO:0000269|PubMed:11055914, ECO:0000269|PubMed:11996570,
ECO:0000269|PubMed:1339261, ECO:0000269|PubMed:15528514,
ECO:0000269|PubMed:15771506, ECO:0000269|PubMed:15932995,
ECO:0000269|PubMed:16256699, ECO:0000269|PubMed:16332900,
ECO:0000269|PubMed:16349476, ECO:0000269|PubMed:16461654,
ECO:0000269|PubMed:18403714, ECO:0000269|PubMed:18486503,
ECO:0000269|PubMed:8368836, ECO:0000269|PubMed:8368837,
ECO:0000269|PubMed:8434913, ECO:0000305|PubMed:15006741}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + 6-
demethylsterigmatocystin = S-adenosyl-L-homocysteine +
sterigmatocystin. {ECO:0000269|PubMed:10543813}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.94 M for demethylsterigmatocystin
{ECO:0000269|PubMed:16349476};
KM=2.5 uM for dihydrodemethylsterigmatocystin
{ECO:0000269|PubMed:16349476};
pH dependence:
Optimum pH is 6.5-9.0. {ECO:0000269|PubMed:16349476};
-!- PATHWAY: Mycotoxin biosynthesis; aflatoxin biosynthesis.
{ECO:0000269|PubMed:10543813, ECO:0000305|PubMed:15006741}.
-!- SIMILARITY: Belongs to the class I-like SAM-binding
methyltransferase superfamily. Cation-independent O-
methyltransferase family. COMT subfamily. {ECO:0000255|PROSITE-
ProRule:PRU01020}.
-!- SEQUENCE CAUTION:
Sequence=KJK60770.1; Type=Erroneous gene model prediction; Note=The predicted gene P875_00052999 has been split into 2 genes: P875_00052999-1 (aflP) and P875_00052999-2 (aflO).; Evidence={ECO:0000305};
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EMBL; AB022905; BAA86103.1; -; Genomic_DNA.
EMBL; AB022906; BAA86104.1; -; mRNA.
EMBL; AY371490; AAS66016.1; -; Genomic_DNA.
EMBL; JZEE01000729; KJK60770.1; ALT_SEQ; Genomic_DNA.
ProteinModelPortal; Q9UQY0; -.
SMR; Q9UQY0; -.
BRENDA; 2.1.1.109; 523.
UniPathway; UPA00287; -.
Proteomes; UP000033540; Unassembled WGS sequence.
GO; GO:0047145; F:demethylsterigmatocystin 6-O-methyltransferase activity; IDA:UniProtKB.
GO; GO:0045122; P:aflatoxin biosynthetic process; IDA:UniProtKB.
Gene3D; 1.10.10.10; -; 1.
InterPro; IPR016461; O-MeTrfase_COMT.
InterPro; IPR001077; O_MeTrfase_2.
InterPro; IPR029063; SAM-dependent_MTases.
InterPro; IPR036388; WH-like_DNA-bd_sf.
InterPro; IPR036390; WH_DNA-bd_sf.
Pfam; PF00891; Methyltransf_2; 1.
PIRSF; PIRSF005739; O-mtase; 1.
SUPFAM; SSF46785; SSF46785; 1.
SUPFAM; SSF53335; SSF53335; 1.
PROSITE; PS51683; SAM_OMT_II; 1.
1: Evidence at protein level;
Complete proteome; Direct protein sequencing; Methyltransferase;
Reference proteome; S-adenosyl-L-methionine; Transferase.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:10543813}.
CHAIN 2 386 Demethylsterigmatocystin 6-O-
methyltransferase.
/FTId=PRO_5000049327.
REGION 137 150 Substrate binding. {ECO:0000250}.
REGION 177 197 Substrate binding. {ECO:0000250}.
REGION 228 229 S-adenosyl-L-methionine binding.
{ECO:0000250|UniProtKB:O04385}.
REGION 273 274 S-adenosyl-L-methionine binding.
{ECO:0000250|UniProtKB:O04385}.
ACT_SITE 293 293 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU01020}.
BINDING 253 253 S-adenosyl-L-methionine.
{ECO:0000250|UniProtKB:O04385}.
BINDING 289 289 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000250|UniProtKB:O04385}.
CONFLICT 8 8 I -> T (in Ref. 2; AAS66016 and 3;
KJK60770). {ECO:0000305}.
SEQUENCE 386 AA; 43155 MW; 1C25C2EE5F3F6114 CRC64;
MTGLDMEIIF AKIKEEYART DDVGKRQIQG HIRELQVGFY SDWDVVMRLS SGPLQVALTK
VGIDLGIFRS LKESDTPITL AEIVKKTGAS PRLLGRILRT QAAFGLIKET GPQEYTSSAF
TDVFANSDAA GAVVQLFDIS GPCTQILPDF LAERNYQDIT SNKDCVFQKA FGSDLTMFEW
MPQHPKHMES LGHLMALERP VSWVDHYPVL EELGGFPAPD KVLMVDIGGG FGQQSKALRA
KFPDLPGRLI VQDIPQTLAN AQPAAGIEFM EHNFFEPQPI QNAKFYYLRH VFHDWPDEQC
VLILKQIIPA MGPESQILID EMVIPSTGVP WQAAFTDLLM MNSLGGVERT RAEWDDLMEQ
VGLEIIQSKV YDSKEQAILV AVPKRT


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