GEDL_ASPTN
ID GEDL_ASPTN Reviewed; 548 AA.
AC Q0CCX4;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 07-SEP-2016, sequence version 2.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Sulochrin halogenase {ECO:0000303|PubMed:24009710};
DE EC=1.14.19.- {ECO:0000269|PubMed:24009710};
DE AltName: Full=Geodin synthesis protein L {ECO:0000303|PubMed:24009710};
GN Name=gedL {ECO:0000303|PubMed:24009710}; ORFNames=ATEG_08460;
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 GENE MODEL REVISION, FUNCTION, AND CATALYTIC ACTIVITY.
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: Sulochrin halogenase; 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 chloride + 2 FADH2 + 2 O2 + sulochrin = dihydrogeodin + 2
CC FAD + H(+) + 4 H2O; Xref=Rhea:RHEA:64312, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17996,
CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:77639,
CC ChEBI:CHEBI:150012; Evidence={ECO:0000269|PubMed:24009710};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64313;
CC Evidence={ECO:0000269|PubMed:24009710};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:24009710}.
CC -!- SIMILARITY: Belongs to the flavin-dependent halogenase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAU31633.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305|PubMed:24009710};
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DR EMBL; CH476605; EAU31633.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001217599.1; XM_001217598.1.
DR AlphaFoldDB; Q0CCX4; -.
DR SMR; Q0CCX4; -.
DR STRING; 341663.Q0CCX4; -.
DR PRIDE; Q0CCX4; -.
DR EnsemblFungi; EAU31633; EAU31633; ATEG_08460.
DR GeneID; 4353198; -.
DR eggNOG; ENOG502QW6Y; Eukaryota.
DR HOGENOM; CLU_024648_4_2_1; -.
DR OrthoDB; 462247at2759; -.
DR BioCyc; MetaCyc:MON-21294; -.
DR Proteomes; UP000007963; Unassembled WGS sequence.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR006905; Flavin_halogenase.
DR Pfam; PF04820; Trp_halogenase; 2.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW FAD; Flavoprotein; Monooxygenase; Oxidoreductase; Reference proteome.
FT CHAIN 1..548
FT /note="Sulochrin halogenase"
FT /id="PRO_0000437102"
FT BINDING 14..17
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P95480"
FT BINDING 37..48
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P95480"
FT BINDING 333..334
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250|UniProtKB:P95480"
SQ SEQUENCE 548 AA; 59940 MW; FFDC5F1BA95AF1B4 CRC64;
MSVPNKTTVL VIGGGPAGSY AAAVLARENV DTVLLEAEKF PRYHIGESML ASMRFFLRFI
DLEEQFDAYG FQKKYGATFK INSKREAYTD FSASLGPGGY AWNVIRSEAD DLIFRYAGEQ
GAHIFDGTKV DDIEFLSYDG ADGANFTPAA FLVNPGRPVA ATWSRKDGTR GRIKFDYLID
ASGRAGIIST KYLKNRTVNE GLRNIANWSY WKGAKVYGEG SDQQGSPFFE ALTDGSGWCW
AIPLHNGTLS VGVVMRQDLF FGKKKAAGSP GSLEMYKLCL QSVPGISGLL EDAEIVSDVK
MASDWSYSAS AYAGPHFRVA GDAGCFIDPY FSSGVHLALV GGLSAATTIQ AVRRGETSEF
SAAKWHSSKV TEGYTRFLLV VMAVLRQLRK QNAAVITDDK EEGFDTAFGL IQPVIQGQAD
TGESEQQRMV AGVQFSLERF GQATPEAQRA LLDKVQFAGQ NAEELEKLTA DELAVLHNII
GRQLKMTKVE KNLDNFTRDV IDGWAPRVER GKLGLQRADT SIMTAEMKDL FQLNRSLDST
KAGIQLPA
