GEDH_ASPTN
ID GEDH_ASPTN Reviewed; 150 AA.
AC P0DOB2; Q0CCX7;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 07-SEP-2016, sequence version 1.
DT 03-AUG-2022, entry version 13.
DE RecName: Full=Anthrone oxygenase gedH {ECO:0000303|PubMed:1810248};
DE EC=1.10.3.- {ECO:0000269|PubMed:1810248};
DE AltName: Full=Geodin synthesis protein H {ECO:0000303|PubMed:24009710};
GN Name=gedH {ECO:0000303|PubMed:24009710};
GN ORFNames=ATEG_08457-2 {ECO:0000303|PubMed:24009710};
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, AND CATALYTIC ACTIVITY.
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 GENE MODEL REVISION, AND 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: Anthrone oxygenase; 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 emodin
CC anthrone (PubMed:24009710). The next step is performed by the emodin
CC anthrone oxygenase gedH that catalyzes the oxidation of emodinanthrone
CC to emodin (PubMed:1810248). Emodin O-methyltransferase encoded probably
CC by gedA then catalyzes methylation of the 8-hydroxy group of emodin to
CC form questin (PubMed:1444712). Ring cleavage of questin by questin
CC oxidase gedK leads to desmethylsulochrin via several intermediates
CC including questin epoxide (PubMed:3182756). Another methylation step
CC probably catalyzed by methyltransferase gedG leads to the formation of
CC sulochrin which is further converted to dihydrogeodin by the sulochrin
CC halogenase gedL (PubMed:24009710). Finally, the dihydrogeodin oxidase
CC gedJ 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 -!- CATALYTIC ACTIVITY:
CC Reaction=emodin anthrone + O2 = emodin + H(+) + H2O;
CC Xref=Rhea:RHEA:64268, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:77659, ChEBI:CHEBI:150013;
CC Evidence={ECO:0000269|PubMed:1810248};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64269;
CC Evidence={ECO:0000269|PubMed:1810248};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:24009710}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the anthrone oxygenase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAU31630.1; Type=Erroneous gene model prediction; Note=The predicted gene ATEG_08457 has been split into 2 genes: ATEG_08457-1 and ATEG_08457-2.; Evidence={ECO:0000269|PubMed:24009710};
CC Sequence=EAU31630.1; Type=Erroneous translation; Evidence={ECO:0000305};
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DR EMBL; CH476605; EAU31630.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; P0DOB2; -.
DR OrthoDB; 1621831at2759; -.
DR BioCyc; MetaCyc:MON-21291; -.
DR Proteomes; UP000007963; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Membrane; Monooxygenase; Oxidoreductase; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..150
FT /note="Anthrone oxygenase gedH"
FT /id="PRO_0000437096"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 73..93
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 128..148
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 150 AA; 16271 MW; 6036551E65A78341 CRC64;
MANPAVGAMM GLSLVAVPVF LDTNTQSEQL LAQFASLYDY GHKLMPTIAV ATCALHGWVA
ARKRAAHQPW GRPVLAAVTT ITMVPFTWVC MVSTNNALFQ LHKGADANME MVRALIARWQ
WLHVARSLFP LAGAIVACQT LLKELVGGSR
