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O-methyltransferase gedA (EC 2.1.1.-) (Geodin synthesis protein A)

 GEDA_ASPTN              Reviewed;         486 AA.
Q0CCY5;
07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 1.
20-JUN-2018, entry version 51.
RecName: Full=O-methyltransferase gedA {ECO:0000303|PubMed:24009710};
EC=2.1.1.- {ECO:0000269|PubMed:1444712};
AltName: Full=Geodin synthesis protein A {ECO:0000303|PubMed:24009710};
Name=gedA {ECO:0000303|PubMed:24009710}; ORFNames=ATEG_08449;
Aspergillus terreus (strain NIH 2624 / FGSC A1156).
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
NCBI_TaxID=341663;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=NIH 2624 / FGSC A1156;
Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K.,
LaButti K., Pushparaj V., DeCaprio D., Crawford M., Koehrsen M.,
Engels R., Montgomery P., Pearson M., Howarth C., Larson L., Luoma S.,
White J., Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C.,
Denning D.W., Nierman W.C., Milne T., Madden K.;
"Annotation of the Aspergillus terreus NIH2624 genome.";
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[2]
FUNCTION.
PubMed=3182756; DOI=10.1093/oxfordjournals.jbchem.a122365;
Fujii I., Ebizuka Y., Sankawa U.;
"A novel anthraquinone ring cleavage enzyme from Aspergillus
terreus.";
J. Biochem. 103:878-883(1988).
[3]
FUNCTION.
PubMed=1810248;
Fujii I., Chen Z.G., Ebizuka Y., Sankawa U.;
"Identification of emodinanthrone oxygenase in fungus Aspergillus
terreus.";
Biochem. Int. 25:1043-1049(1991).
[4]
FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=1444712; DOI=10.1007/BF00249062;
Chen Z.G., Fujii I., Ebizuka Y., Sankawa U.;
"Emodin O-methyltransferase from Aspergillus terreus.";
Arch. Microbiol. 158:29-34(1992).
[5]
FUNCTION.
PubMed=7665560; DOI=10.1074/jbc.270.37.21495;
Huang K.X., Fujii I., Ebizuka Y., Gomi K., Sankawa U.;
"Molecular cloning and heterologous expression of the gene encoding
dihydrogeodin oxidase, a multicopper blue enzyme from Aspergillus
terreus.";
J. Biol. Chem. 270:21495-21502(1995).
[6]
BIOTECHNOLOGY.
PubMed=10819297;
Shinohara C., Chikanishi T., Nakashima S., Hashimoto A., Hamanaka A.,
Endo A., Hasumi K.;
"Enhancement of fibrinolytic activity of vascular endothelial cells by
chaetoglobosin A, crinipellin B, geodin and triticone B.";
J. Antibiot. 53:262-268(2000).
[7]
FUNCTION.
PubMed=12536215; DOI=10.1038/nbt781;
Askenazi M., Driggers E.M., Holtzman D.A., Norman T.C., Iverson S.,
Zimmer D.P., Boers M.E., Blomquist P.R., Martinez E.J., Monreal A.W.,
Feibelman T.P., Mayorga M.E., Maxon M.E., Sykes K., Tobin J.V.,
Cordero E., Salama S.R., Trueheart J., Royer J.C., Madden K.T.;
"Integrating transcriptional and metabolite profiles to direct the
engineering of lovastatin-producing fungal strains.";
Nat. Biotechnol. 21:150-156(2003).
[8]
BIOTECHNOLOGY.
PubMed=16320762; DOI=10.1038/ja.2005.79;
Sato S., Okusa N., Ogawa A., Ikenoue T., Seki T., Tsuji T.;
"Identification and preliminary SAR studies of (+)-Geodin as a glucose
uptake stimulator for rat adipocytes.";
J. Antibiot. 58:583-589(2005).
[9]
FUNCTION.
PubMed=19549600; DOI=10.1016/j.chembiol.2009.04.004;
Awakawa T., Yokota K., Funa N., Doi F., Mori N., Watanabe H.,
Horinouchi S.;
"Physically discrete beta-lactamase-type thioesterase catalyzes
product release in atrochrysone synthesis by iterative type I
polyketide synthase.";
Chem. Biol. 16:613-623(2009).
[10]
FUNCTION.
PubMed=24009710; DOI=10.1371/journal.pone.0072871;
Nielsen M.T., Nielsen J.B., Anyaogu D.C., Holm D.K., Nielsen K.F.,
Larsen T.O., Mortensen U.H.;
"Heterologous reconstitution of the intact geodin gene cluster in
Aspergillus nidulans through a simple and versatile PCR based
approach.";
PLoS ONE 8:E72871-E72871(2013).
-!- FUNCTION: O-methyltransferase; part of the gene cluster that
mediates the biosynthesis of geodin, an intermediate in the
biosynthesis of other natural products (PubMed:7665560,
PubMed:19549600, PubMed:24009710). The pathway begins with the
synthesis of atrochrysone thioester by the polyketide synthase
(PKS) gedC (PubMed:12536215, PubMed:19549600). The atrochrysone
carboxyl ACP thioesterase gedB then breaks the thioester bond and
releases the atrochrysone carboxylic acid from gedC
(PubMed:19549600). The atrochrysone carboxylic acid is then
converted to atrochrysone which is further transformed into
emodinanthrone (PubMed:24009710). The next step is performed by
the emodinanthrone oxygenase gedH that catalyzes the oxidation of
emodinanthrone to emodin (PubMed:1810248). Emodin O-
methyltransferase encoded probably by gedA then catalyzes
methylation of the 8-hydroxy group of emodin to form questin
(PubMed:1444712). Ring cleavage of questin by questin oxidase gedK
leads to desmethylsulochrin via several intermediates including
questin epoxide (PubMed:3182756). Another methylation step
probably catalyzed by methyltransferase gedG leads to the
formation of sulochrin which is further converted to dihydrogeodin
by the sulochrin halogenase gedL (PubMed:24009710). Finally, the
dihydrogeodin oxidase gedJ catalyzes the stereospecific phenol
oxidative coupling reaction converting dihydrogeodin to geodin
(PubMed:7665560). {ECO:0000269|PubMed:12536215,
ECO:0000269|PubMed:1444712, ECO:0000269|PubMed:1810248,
ECO:0000269|PubMed:19549600, ECO:0000269|PubMed:24009710,
ECO:0000269|PubMed:3182756, ECO:0000269|PubMed:7665560}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.34 uM for emodin {ECO:0000269|PubMed:1444712};
KM=4.1 uM for S-adenosyl-l-methionine (SAM)
{ECO:0000269|PubMed:1444712};
pH dependence:
Optimum pH is 7.0-8.0. {ECO:0000269|PubMed:1444712};
-!- PATHWAY: Secondary metabolite biosynthesis.
{ECO:0000269|PubMed:24009710}.
-!- BIOTECHNOLOGY: Geodin shows the glucose uptake stimulator activity
towards rat adipocytes (PubMed:16320762). Geodin also enhances the
fibrinolytic activity of vascular endothelial cells
(PubMed:10819297). {ECO:0000269|PubMed:10819297,
ECO:0000269|PubMed:16320762}.
-!- SIMILARITY: Belongs to the class I-like SAM-binding
methyltransferase superfamily. Cation-independent O-
methyltransferase family.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; CH476605; EAU31622.1; -; Genomic_DNA.
RefSeq; XP_001217070.1; XM_001217070.1.
ProteinModelPortal; Q0CCY5; -.
EnsemblFungi; EAU31622; EAU31622; ATEG_08449.
GeneID; 4353099; -.
EuPathDB; FungiDB:ATEG_08449; -.
HOGENOM; HOG000216825; -.
OMA; HELRNIT; -.
OrthoDB; EOG092C3M7V; -.
SABIO-RK; Q0CCY5; -.
Proteomes; UP000007963; Unassembled WGS sequence.
GO; GO:0008171; F:O-methyltransferase activity; IEA:InterPro.
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; Methyltransferase; Reference proteome;
S-adenosyl-L-methionine; Transferase.
CHAIN 1 486 O-methyltransferase gedA.
/FTId=PRO_0000437065.
REGION 298 299 S-adenosyl-L-methionine binding.
{ECO:0000250|UniProtKB:O04385}.
REGION 353 354 S-adenosyl-L-methionine binding.
{ECO:0000250|UniProtKB:O04385}.
ACT_SITE 373 373 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU01020}.
BINDING 321 321 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU01020}.
BINDING 369 369 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000250|UniProtKB:O04385}.
SEQUENCE 486 AA; 53916 MW; 9F6B4B1F2FDB3961 CRC64;
MERQPKSLSD AVQLLQTTEI ISKCTQTIIA EWSNEAETFK KRASSGRAGA ELVLPSHELF
NAQRTITAAI GKLIELVSEP SVRILEIAGQ YQESRALYIA VERRIPDILA SQDNEGGMPV
KELSSRTGIE YRKLSRILRY LCSMGTFRQV GPDVFANNTI SACLVANEPL RAYVRLTGSE
AFTASDRLPK TLLDPSTGPS YDVTRTAWQD AIGTTKPRWE WIEERVEPDK LLDSGYHYPG
IPSLILEPQP PGEDGLVARP ELEIMGLAMV GGGRVFGAAH VFDFPWASLD NALVVDVGGG
VGGFALQLSK VYPDLRFVIQ DRGPVIQQAL ESVWPNENPA ALKDQRVQFM EHSFFDKNPV
EGADVYYLRY VLHDWSDDYC VNILSHIRES MAPHSRLLIC EQVMNTTIGD PDLTSAPAPL
PANYGFHARF SHSRDLTMMA AINGIERTPE EFKTILKSAG LALKQIWECR SQVSLLEAVR
ADARTA


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