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Sterigmatocystin 8-O-methyltransferase (EC 2.1.1.110) (Aflatoxin biosynthesis protein P)

 AFLP_ASPPU              Reviewed;         418 AA.
Q12120; A0A0F0HZ60;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 1.
20-DEC-2017, entry version 74.
RecName: Full=Sterigmatocystin 8-O-methyltransferase {ECO:0000303|PubMed:8434913};
EC=2.1.1.110 {ECO:0000269|PubMed:8434913};
AltName: Full=Aflatoxin biosynthesis protein P {ECO:0000303|PubMed:15006741};
Flags: Precursor;
Name=aflP {ECO:0000303|PubMed:15006741}; Synonyms=omt-1, omtA;
ORFNames=P875_00052999-1;
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 [MRNA].
STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1;
PubMed=8285664;
Yu J., Cary J.W., Bhatnager D., Cleveland T.E., Keller N.P., Chu F.S.;
"Cloning and characterization of a cDNA from Aspergillus parasiticus
encoding an O-methyltransferase involved in aflatoxin biosynthesis.";
Appl. Environ. Microbiol. 59:3564-3571(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=70;
Yu J.;
Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1;
PubMed=7557460; DOI=10.1016/0378-1119(95)00397-O;
Yu J., Chang P.-K., Payne G.A., Cary J.W., Bhatnagar D.,
Cleveland T.E.;
"Comparison of the omtA genes encoding O-methyltransferases involved
in aflatoxin biosynthesis from Aspergillus parasiticus and A.
flavus.";
Gene 163:121-125(1995).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1;
PubMed=15094053; DOI=10.1016/S0014-5793(04)00327-8;
Yu J., Bhatnagar D., Cleveland T.E.;
"Completed sequence of aflatoxin pathway gene cluster in Aspergillus
parasiticus.";
FEBS Lett. 564:126-130(2004).
[5]
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.
[6]
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).
[7]
PROTEIN SEQUENCE OF 42-63, FUNCTION, CATALYTIC ACTIVITY, AND
BIOPHYSICOCHEMICAL PROPERTIES.
STRAIN=ATCC 56774 / SRRC 163 / avn-1;
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).
[8]
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).
[9]
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).
[10]
FUNCTION.
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).
[11]
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).
[12]
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).
[13]
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).
[14]
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).
[15]
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).
[16]
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).
[17]
SUBCELLULAR LOCATION.
PubMed=14722624; DOI=10.1007/s00203-003-0643-3;
Lee L.W., Chiou C.H., Klomparens K.L., Cary J.W., Linz J.E.;
"Subcellular localization of aflatoxin biosynthetic enzymes Nor-1,
Ver-1, and OmtA in time-dependent fractionated colonies of Aspergillus
parasiticus.";
Arch. Microbiol. 181:204-214(2004).
[18]
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).
[19]
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).
[20]
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).
[21]
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).
[22]
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).
[23]
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).
[24]
INDUCTION.
PubMed=23113196;
Jahanshiri Z., Shams-Ghahfarokhi M., Allameh A., Razzaghi-Abyaneh M.;
"Effect of curcumin on Aspergillus parasiticus growth and expression
of major genes involved in the early and late stages of aflatoxin
biosynthesis.";
Iran. J. Public Health 41:72-79(2012).
[25]
INDUCTION.
PubMed=24294264; DOI=10.1590/S1517-83822013000200045;
Yahyaraeyat R., Khosravi A.R., Shahbazzadeh D., Khalaj V.;
"The potential effects of Zataria multiflora Boiss essential oil on
growth, aflatoxin production and transcription of aflatoxin
biosynthesis pathway genes of toxigenic Aspergillus parasiticus.";
Braz. J. Microbiol. 44:643-649(2013).
-!- FUNCTION: Sterigmatocystin 8-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). 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: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: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 + sterigmatocystin =
S-adenosyl-L-homocysteine + 8-O-methylsterigmatocystin.
{ECO:0000269|PubMed:8434913}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine +
dihydrosterigmatocystin = S-adenosyl-L-homocysteine + 8-O-
methyldihydrosterigmatocystin. {ECO:0000269|PubMed:8434913}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=2 uM for sterigmatocystin {ECO:0000269|PubMed:8434913};
KM=9.6 uM for S-adenosyl-L-methionine
{ECO:0000269|PubMed:8434913};
pH dependence:
Optimum pH is 7-9.4. {ECO:0000269|PubMed:8434913};
Temperature dependence:
Optimum temperature is 40-45 degrees Celsius.
{ECO:0000269|PubMed:8434913};
-!- PATHWAY: Mycotoxin biosynthesis; aflatoxin biosynthesis.
{ECO:0000305|PubMed:15006741}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14722624}.
Vacuole {ECO:0000269|PubMed:14722624}.
-!- INDUCTION: Zataria multiflora essential oil reduces gene
expression (PubMed:24294264). Expression is repressed by curcumin
(PubMed:23113196). {ECO:0000269|PubMed:23113196,
ECO:0000269|PubMed:24294264}.
-!- 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; L22091; AAA32697.1; -; mRNA.
EMBL; L25835; AAA32699.1; -; Genomic_DNA.
EMBL; AY371490; AAS66017.1; -; Genomic_DNA.
EMBL; JZEE01000729; KJK60770.1; ALT_SEQ; Genomic_DNA.
ProteinModelPortal; Q12120; -.
SMR; Q12120; -.
EnsemblFungi; KJK60770; KJK60770; P875_00052999.
KEGG; ag:AAA32697; -.
KO; K17650; -.
BioCyc; MetaCyc:MONOMER-14043; -.
UniPathway; UPA00287; -.
Proteomes; UP000033540; Unassembled WGS sequence.
GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
GO; GO:0047146; F:sterigmatocystin 7-O-methyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0045122; P:aflatoxin biosynthetic process; IEA:UniProtKB-UniPathway.
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.
SUPFAM; SSF46785; SSF46785; 1.
SUPFAM; SSF53335; SSF53335; 1.
PROSITE; PS51683; SAM_OMT_II; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Direct protein sequencing;
Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
Transferase; Vacuole; Zymogen.
PROPEP 1 41 {ECO:0000269|PubMed:8434913}.
/FTId=PRO_0000021898.
CHAIN 42 418 Sterigmatocystin 8-O-methyltransferase.
/FTId=PRO_0000021899.
REGION 170 176 Substrate binding. {ECO:0000250}.
REGION 206 225 Substrate binding. {ECO:0000250}.
REGION 254 255 S-adenosyl-L-methionine binding.
{ECO:0000250|UniProtKB:O04385}.
REGION 297 298 S-adenosyl-L-methionine binding.
{ECO:0000250|UniProtKB:O04385}.
ACT_SITE 317 317 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU01020}.
BINDING 277 277 S-adenosyl-L-methionine.
{ECO:0000250|UniProtKB:O04385}.
BINDING 313 313 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000250|UniProtKB:O04385}.
CONFLICT 48 48 S -> D (in Ref. 7; AA sequence).
{ECO:0000305}.
CONFLICT 61 61 C -> Q (in Ref. 7; AA sequence).
{ECO:0000305}.
CONFLICT 63 63 R -> P (in Ref. 7; AA sequence).
{ECO:0000305}.
SEQUENCE 418 AA; 46397 MW; 2CC5F93245F91262 CRC64;
MALPSKAALV GLANTLSEQV KRYLATAGET KSPEDHKLCI ESERTPSSNE HAQAWEIVRT
CDRIGSLVHG PVPWLLSNAL SHLDSACLAA ATHLNLQDII VDGPSPTSLD TIVAATGVSE
DLLRRILRGC AQRFIFEEVA PDQYAHTDAS KMLRVTGIHA LVGFSCDEVM RSGASFSDFL
QQTKGKPPSW NVPSPFSLAF DPTKGLFDYY STVDEVRGRR FDLGMGGTEA TKPLVEEMFD
FSSLPEGSTV VDVGGGRGHL SRRVSQKHPH LRFIVQDLPA VIHGVEDTDK VTMMEHDIRR
PNPVRGADVY LLRSILHDYP DAACVEILSN IVTAMDPSKS RILLDEMIMP DLLAQDSQRF
MNQIDMTVVL TLNGKERSTK EWNSLITTVD GRLETEKIWW RKGEEGSHWG VQQLRLRK


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CSB-EL014703HU Human Molybdenum cofactor biosynthesis protein 1 [Includes: Molybdenum cofactor biosynthesis protein A; Molybdenum cofactor biosynthesis protein C](MOCS1) ELISA kit 96T
E2223m ELISA kit Amine N-methyltransferase,Aromatic alkylamine N-methyltransferase,Arylamine N-methyltransferase,Indolamine N-methyltransferase,Indolethylamine N-methyltransferase,Inmt,Mouse,Mus musculus,Te 96T


 

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