GEDG_ASPTN
ID GEDG_ASPTN Reviewed; 320 AA.
AC Q0CCX8;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Methyltransferase gedG {ECO:0000303|PubMed:24009710};
DE EC=2.1.1.- {ECO:0000305|PubMed:24009710};
DE AltName: Full=Geodin synthesis protein G {ECO:0000303|PubMed:24009710};
GN Name=gedG {ECO:0000303|PubMed:24009710}; ORFNames=ATEG_08456;
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION.
RX PubMed=3182756; DOI=10.1093/oxfordjournals.jbchem.a122365;
RA Fujii I., Ebizuka Y., Sankawa U.;
RT "A novel anthraquinone ring cleavage enzyme from Aspergillus terreus.";
RL J. Biochem. 103:878-883(1988).
RN [3]
RP FUNCTION.
RX PubMed=1810248;
RA Fujii I., Chen Z.G., Ebizuka Y., Sankawa U.;
RT "Identification of emodinanthrone oxygenase in fungus Aspergillus
RT terreus.";
RL Biochem. Int. 25:1043-1049(1991).
RN [4]
RP FUNCTION.
RX PubMed=1444712; DOI=10.1007/bf00249062;
RA Chen Z.G., Fujii I., Ebizuka Y., Sankawa U.;
RT "Emodin O-methyltransferase from Aspergillus terreus.";
RL Arch. Microbiol. 158:29-34(1992).
RN [5]
RP FUNCTION.
RX PubMed=7665560; DOI=10.1074/jbc.270.37.21495;
RA Huang K.X., Fujii I., Ebizuka Y., Gomi K., Sankawa U.;
RT "Molecular cloning and heterologous expression of the gene encoding
RT dihydrogeodin oxidase, a multicopper blue enzyme from Aspergillus
RT terreus.";
RL J. Biol. Chem. 270:21495-21502(1995).
RN [6]
RP FUNCTION.
RX PubMed=12536215; DOI=10.1038/nbt781;
RA Askenazi M., Driggers E.M., Holtzman D.A., Norman T.C., Iverson S.,
RA Zimmer D.P., Boers M.E., Blomquist P.R., Martinez E.J., Monreal A.W.,
RA Feibelman T.P., Mayorga M.E., Maxon M.E., Sykes K., Tobin J.V., Cordero E.,
RA Salama S.R., Trueheart J., Royer J.C., Madden K.T.;
RT "Integrating transcriptional and metabolite profiles to direct the
RT engineering of lovastatin-producing fungal strains.";
RL Nat. Biotechnol. 21:150-156(2003).
RN [7]
RP FUNCTION.
RX PubMed=19549600; DOI=10.1016/j.chembiol.2009.04.004;
RA Awakawa T., Yokota K., Funa N., Doi F., Mori N., Watanabe H.,
RA Horinouchi S.;
RT "Physically discrete beta-lactamase-type thioesterase catalyzes product
RT release in atrochrysone synthesis by iterative type I polyketide
RT synthase.";
RL Chem. Biol. 16:613-623(2009).
RN [8]
RP FUNCTION.
RX PubMed=24009710; DOI=10.1371/journal.pone.0072871;
RA Nielsen M.T., Nielsen J.B., Anyaogu D.C., Holm D.K., Nielsen K.F.,
RA Larsen T.O., Mortensen U.H.;
RT "Heterologous reconstitution of the intact geodin gene cluster in
RT Aspergillus nidulans through a simple and versatile PCR based approach.";
RL PLoS ONE 8:E72871-E72871(2013).
CC -!- FUNCTION: Methyltransferase; part of the gene cluster that mediates the
CC biosynthesis of geodin, an intermediate in the biosynthesis of other
CC natural products (PubMed:7665560, PubMed:19549600, PubMed:24009710).
CC The pathway begins with the synthesis of atrochrysone thioester by the
CC polyketide synthase (PKS) gedC (PubMed:12536215, PubMed:19549600). The
CC atrochrysone carboxyl ACP thioesterase gedB then breaks the thioester
CC bond and releases the atrochrysone carboxylic acid from gedC
CC (PubMed:19549600). The atrochrysone carboxylic acid is then converted
CC to atrochrysone which is further transformed into emodinanthrone
CC (PubMed:24009710). The next step is performed by the emodinanthrone
CC oxygenase gedH that catalyzes the oxidation of emodinanthrone to emodin
CC (PubMed:1810248). Emodin O-methyltransferase encoded probably by gedA
CC then catalyzes methylation of the 8-hydroxy group of emodin to form
CC questin (PubMed:1444712). Ring cleavage of questin by questin oxidase
CC gedK leads to desmethylsulochrin via several intermediates including
CC questin epoxide (PubMed:3182756). Another methylation step probably
CC catalyzed by methyltransferase gedG leads to the formation of sulochrin
CC which is further converted to dihydrogeodin by the sulochrin halogenase
CC gedL (PubMed:24009710). Finally, the dihydrogeodin oxidase gedJ
CC catalyzes the stereospecific phenol oxidative coupling reaction
CC converting dihydrogeodin to geodin (PubMed:7665560).
CC {ECO:0000269|PubMed:12536215, ECO:0000269|PubMed:1444712,
CC ECO:0000269|PubMed:1810248, ECO:0000269|PubMed:19549600,
CC ECO:0000269|PubMed:24009710, ECO:0000269|PubMed:3182756,
CC ECO:0000269|PubMed:7665560}.
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:24009710}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC {ECO:0000305}.
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DR EMBL; CH476605; EAU31629.1; -; Genomic_DNA.
DR RefSeq; XP_001217595.1; XM_001217594.1.
DR AlphaFoldDB; Q0CCX8; -.
DR SMR; Q0CCX8; -.
DR EnsemblFungi; EAU31629; EAU31629; ATEG_08456.
DR GeneID; 4353106; -.
DR VEuPathDB; FungiDB:ATEG_08456; -.
DR eggNOG; ENOG502SJ7Q; Eukaryota.
DR HOGENOM; CLU_049344_0_1_1; -.
DR OMA; SKFQHVI; -.
DR OrthoDB; 899118at2759; -.
DR Proteomes; UP000007963; Unassembled WGS sequence.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR013216; Methyltransf_11.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF08241; Methyltransf_11; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 3: Inferred from homology;
KW Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..320
FT /note="Methyltransferase gedG"
FT /id="PRO_0000437070"
FT REGION 61..154
FT /note="Methyltransferase domain"
FT /evidence="ECO:0000255"
FT REGION 231..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..252
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 320 AA; 36778 MW; 96FCDC623F03021F CRC64;
MSVDTANPTS PMMETHEQIF AQDPDFWKNY RRGRPQVPYS FFQRIYNYHQ GHSGRFETVH
DAGAGNGVYS KELRSKFHHV IVSDVVAENV RQAEERLGTE GYSFRVGKME ELDEIPAASV
DMVFVMNAMH WADDQTRAMR AIAAQLRPGG TFACAGFGPA RFRDARVQDV WERISQQGGR
LLLQTANQPV DTINVMVRSQ DHYNVAPLDE RLFRQRALRI YLNQETGGLT GLLPPERRGE
VTEPDHEGPH DQITFEHDDE WRFDMDLDGF KEHFRTFPHA FRDPEAFTSL WQEIEELVRQ
GSRLDGAWPV TLILATRTNA
