GEDJ_ASPTN
ID GEDJ_ASPTN Reviewed; 605 AA.
AC Q0CCX6;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Dihydrogeodin oxidase {ECO:0000303|PubMed:7665560};
DE Short=DHGO {ECO:0000303|PubMed:7665560};
DE EC=1.10.3.- {ECO:0000269|PubMed:7665560};
DE AltName: Full=Geodin synthesis protein J {ECO:0000303|PubMed:24009710};
DE Flags: Precursor;
GN Name=gedJ {ECO:0000303|PubMed:24009710}; ORFNames=ATEG_08458;
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=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 [3]
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 [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
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 [5]
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 [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: Dihydrogeodin oxidase; part of the gene cluster that mediates
CC the biosynthesis of geodin, an intermediate in the biosynthesis of
CC other natural products (PubMed:7665560, PubMed:19549600,
CC PubMed:24009710). The pathway begins with the synthesis of atrochrysone
CC thioester by the polyketide synthase (PKS) gedC (PubMed:12536215,
CC PubMed:19549600). The atrochrysone carboxyl ACP thioesterase gedB then
CC breaks the thioester bond and releases the atrochrysone carboxylic acid
CC from gedC (PubMed:19549600). The atrochrysone carboxylic acid is then
CC converted to atrochrysone which is further transformed into
CC emodinanthrone (PubMed:24009710). The next step is performed by the
CC emodinanthrone oxygenase gedH that catalyzes the oxidation of
CC emodinanthrone to emodin (PubMed:1810248). Emodin O-methyltransferase
CC encoded probably by gedA then catalyzes methylation of the 8-hydroxy
CC group of emodin to form questin (PubMed:1444712). Ring cleavage of
CC questin by questin oxidase gedK leads to desmethylsulochrin via several
CC intermediates including questin epoxide (PubMed:3182756). Another
CC methylation step probably catalyzed by methyltransferase gedG leads to
CC the formation of sulochrin which is further converted to dihydrogeodin
CC by the sulochrin halogenase gedL (PubMed:24009710). Finally, the
CC dihydrogeodin oxidase gedJ catalyzes the stereospecific phenol
CC 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 -!- CATALYTIC ACTIVITY:
CC Reaction=2 dihydrogeodin + 2 H(+) + O2 = 2 (+)-geodin + 2 H2O;
CC Xref=Rhea:RHEA:64316, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:150012, ChEBI:CHEBI:150868;
CC Evidence={ECO:0000269|PubMed:7665560};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64317;
CC Evidence={ECO:0000269|PubMed:7665560};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000250|UniProtKB:Q70KY3};
CC Note=Binds 4 Cu cations per monomer. {ECO:0000250|UniProtKB:Q70KY3};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:24009710}.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
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DR EMBL; CH476605; EAU31631.1; -; Genomic_DNA.
DR RefSeq; XP_001217597.1; XM_001217596.1.
DR AlphaFoldDB; Q0CCX6; -.
DR SMR; Q0CCX6; -.
DR STRING; 341663.Q0CCX6; -.
DR EnsemblFungi; EAU31631; EAU31631; ATEG_08458.
DR GeneID; 4353196; -.
DR VEuPathDB; FungiDB:ATEG_08458; -.
DR eggNOG; KOG1263; Eukaryota.
DR HOGENOM; CLU_006504_3_2_1; -.
DR OMA; TFWIDGH; -.
DR OrthoDB; 454773at2759; -.
DR BioCyc; MetaCyc:MON-17515; -.
DR Proteomes; UP000007963; Unassembled WGS sequence.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.420; -; 3.
DR InterPro; IPR001117; Cu-oxidase.
DR InterPro; IPR011706; Cu-oxidase_C.
DR InterPro; IPR045087; Cu-oxidase_fam.
DR InterPro; IPR011707; Cu-oxidase_N.
DR InterPro; IPR033138; Cu_oxidase_CS.
DR InterPro; IPR002355; Cu_oxidase_Cu_BS.
DR InterPro; IPR008972; Cupredoxin.
DR PANTHER; PTHR11709; PTHR11709; 1.
DR Pfam; PF00394; Cu-oxidase; 1.
DR Pfam; PF07731; Cu-oxidase_2; 1.
DR Pfam; PF07732; Cu-oxidase_3; 1.
DR SUPFAM; SSF49503; SSF49503; 3.
DR PROSITE; PS00079; MULTICOPPER_OXIDASE1; 1.
DR PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
PE 1: Evidence at protein level;
KW Copper; Glycoprotein; Metal-binding; Oxidoreductase; Reference proteome;
KW Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..605
FT /note="Dihydrogeodin oxidase"
FT /id="PRO_0000437103"
FT DOMAIN 65..183
FT /note="Plastocyanin-like 1"
FT /evidence="ECO:0000255"
FT DOMAIN 189..347
FT /note="Plastocyanin-like 2"
FT /evidence="ECO:0000255"
FT DOMAIN 424..567
FT /note="Plastocyanin-like 3"
FT /evidence="ECO:0000255"
FT BINDING 117
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 119
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 161
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 163
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 484
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 487
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 489
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 543
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 544
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 545
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT BINDING 549
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q70KY3"
FT CARBOHYD 27
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 278
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 467
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 605 AA; 67579 MW; C98560B9CF3AC2DA CRC64;
MPSLKDWVVA GLVPMTIASS TSRLPSNCTN GPSSRRCWQD GFDIWSDYTD PKVAPPGKLV
EYDLTVTQVT ISPDGYERLG TVFNGQYPGP LIEADWGDTL RITVHNNLTN GNGTAVHWHG
IRLFETNWID GVPGVTQCPI PPGESQVYEF RATQYGTSWY HSHFSLQYSN GLYGPLVIHG
PSSSDWDVDL GPWTLTDWYH EDAFTLNWIS LAGQLAPIPV STLLNGKGTY DCDPGLDPAC
TGKQEYFETT FQQGTKYKMA IVNTATLLTY TFWIDGHNFT VIEADFVPVE PYSTNVLNVG
MGQRYEIVVE ANADRTQGSS FWIHAHYCDI PDVIPNNKVG IIRYDESDTS EPATPPLSEQ
HRDFGCSDPS LGDLVPVVKK TVGPRVNQIG PHDYLTIGEQ GKIPTPWEKD PRVHLWTIKN
TAMYVDWQTP SLEKLTADHD EEFPPETVPV TLDFDTGEWV YFLLTSNYSL EDVVTPRNLT
PSVHPIHLHG HDFAILAQGK GPFTPDIAPQ LDNPPRRDVV DVDIGGYAWI AFEVDNPGAW
LLHCHLQYHA SEGMALQYIE QPSKIKPLIE NAGVLNDFGN RCASWKRYYN AVDIPNDRPQ
DDSGI
