GEDE_ASPTN
ID GEDE_ASPTN Reviewed; 226 AA.
AC Q0CCY0;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 67.
DE RecName: Full=Glutathione S-transferase-like protein gedE {ECO:0000303|PubMed:24009710};
DE EC=2.5.1.- {ECO:0000305|PubMed:24009710};
DE AltName: Full=Geodin synthesis protein E {ECO:0000303|PubMed:24009710};
GN Name=gedE {ECO:0000303|PubMed:24009710}; ORFNames=ATEG_08454;
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, AND CATALYTIC ACTIVITY.
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: Glutathione S-transferase-like protein; part of the gene
CC cluster that mediates the biosynthesis of geodin, an intermediate in
CC the biosynthesis of other natural products (PubMed:7665560,
CC PubMed:19549600, PubMed:24009710). The pathway begins with the
CC synthesis of atrochrysone thioester by the polyketide synthase (PKS)
CC gedC (PubMed:12536215, PubMed:19549600). The atrochrysone carboxyl ACP
CC thioesterase gedB then breaks the thioester bond and releases the
CC atrochrysone carboxylic acid from gedC (PubMed:19549600). The
CC atrochrysone carboxylic acid is then converted to atrochrysone which is
CC further transformed into emodinanthrone (PubMed:24009710). The next
CC step is performed by the emodinanthrone oxygenase gedH that catalyzes
CC the oxidation of emodinanthrone to emodin (PubMed:1810248). Emodin O-
CC methyltransferase encoded probably by gedA then catalyzes methylation
CC of the 8-hydroxy group of emodin to form questin (PubMed:1444712). Ring
CC cleavage of questin by questin oxidase gedK leads to desmethylsulochrin
CC via several intermediates including questin epoxide (PubMed:3182756).
CC Another methylation step probably catalyzed by methyltransferase gedG
CC leads to the formation of sulochrin which is further converted to
CC dihydrogeodin by the sulochrin halogenase gedL (PubMed:24009710).
CC Finally, the dihydrogeodin oxidase gedJ catalyzes the stereospecific
CC phenol oxidative coupling reaction converting dihydrogeodin to geodin
CC (PubMed:7665560). {ECO:0000269|PubMed:12536215,
CC ECO:0000269|PubMed:1444712, ECO:0000269|PubMed:1810248,
CC ECO:0000269|PubMed:19549600, ECO:0000269|PubMed:24009710,
CC ECO:0000269|PubMed:3182756, ECO:0000269|PubMed:7665560}.
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:24009710}.
CC -!- SIMILARITY: Belongs to the GST superfamily. {ECO:0000305}.
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DR EMBL; CH476605; EAU31627.1; -; Genomic_DNA.
DR RefSeq; XP_001217593.1; XM_001217592.1.
DR AlphaFoldDB; Q0CCY0; -.
DR SMR; Q0CCY0; -.
DR STRING; 341663.Q0CCY0; -.
DR EnsemblFungi; EAU31627; EAU31627; ATEG_08454.
DR GeneID; 4353104; -.
DR VEuPathDB; FungiDB:ATEG_08454; -.
DR eggNOG; KOG0867; Eukaryota.
DR HOGENOM; CLU_011226_14_2_1; -.
DR OMA; NEKEWFE; -.
DR OrthoDB; 1231780at2759; -.
DR Proteomes; UP000007963; Unassembled WGS sequence.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR040079; Glutathione_S-Trfase.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR004046; GST_C.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF00043; GST_C; 1.
DR Pfam; PF13417; GST_N_3; 1.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
PE 1: Evidence at protein level;
KW Reference proteome; Transferase.
FT CHAIN 1..226
FT /note="Glutathione S-transferase-like protein gedE"
FT /id="PRO_0000437067"
FT DOMAIN 4..85
FT /note="GST N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00684"
FT DOMAIN 92..226
FT /note="GST C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00685"
SQ SEQUENCE 226 AA; 25639 MW; F3D56A0515CD9397 CRC64;
MSKLLPIKVW GQGGPNPPRV AIILEELGLP YEFMPIQLSQ VKEPEYLAIN PNGRLPAIYD
PNTDLTLWES GAIVEYLVER YDTAHDISFP RDTNDAQHAR QWLFFQASGQ GPYYGQACWF
KKYHPEPVPS ALERYIKEMN RVSGVVDGYL AKQPVPPGGD GPWLVGNKCS FADLAWVSWQ
MTLKKIIQTE DGYDVENFPH LKNWLDRMVA REPVKKVLSA VMPPPS
