GEDI_ASPTN
ID GEDI_ASPTN Reviewed; 313 AA.
AC P0DOB3; Q0CCX7;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 07-SEP-2016, sequence version 1.
DT 25-MAY-2022, entry version 17.
DE RecName: Full=Decarboxylase gedI {ECO:0000305};
DE EC=4.1.1.- {ECO:0000305|PubMed:24009710};
DE AltName: Full=Geodin synthesis protein I {ECO:0000303|PubMed:24009710};
GN Name=gedI {ECO:0000303|PubMed:24009710};
GN ORFNames=ATEG_08457-1 {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.
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: Decarboxylase; 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 emodin anthrone
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). Questin oxidase is then involved in the ring
CC cleavage of questin to form desmethylsulochrin via several
CC intermediates including questin epoxide (PubMed:3182756). Another
CC methylation step probably catalyzed by one of the methyltransferases
CC identified in the cluster leads to the formation of sulochrin which is
CC further converted to dihydrogeodin by the sulochrin halogenase gedL
CC (PubMed:24009710). Finally, the dihydrogeodin oxidase gedJ catalyzes
CC the stereospecific phenol oxidative coupling reaction converting
CC dihydrogeodin to geodin (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=atrochrysone carboxylate + H(+) = atrochrysone + CO2;
CC Xref=Rhea:RHEA:64264, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:149713, ChEBI:CHEBI:150016;
CC Evidence={ECO:0000305|PubMed:24009710};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64265;
CC Evidence={ECO:0000305|PubMed:24009710};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:24009710}.
CC -!- SIMILARITY: Belongs to the tpcK 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:0000305|PubMed:24009710};
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DR EMBL; CH476605; EAU31630.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001217596.1; XM_001217595.1.
DR AlphaFoldDB; P0DOB3; -.
DR SMR; P0DOB3; -.
DR EnsemblFungi; EAU31630; EAU31630; ATEG_08457.
DR GeneID; 4353107; -.
DR VEuPathDB; FungiDB:ATEG_08457; -.
DR eggNOG; ENOG502SJ0E; Eukaryota.
DR OrthoDB; 1621831at2759; -.
DR Proteomes; UP000007963; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR InterPro; IPR011008; Dimeric_a/b-barrel.
DR InterPro; IPR009799; EthD_dom.
DR Pfam; PF07110; EthD; 1.
DR SUPFAM; SSF54909; SSF54909; 1.
PE 3: Inferred from homology;
KW Lyase; Reference proteome.
FT CHAIN 1..313
FT /note="Decarboxylase gedI"
FT /id="PRO_0000437110"
FT DOMAIN 197..292
FT /note="EthD"
FT /evidence="ECO:0000255"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 313 AA; 35205 MW; 93826FFA7466DA4C CRC64;
MKLEQCIVGR DHTDPRKWHH GDGRDGREHR TAPGLVGGSL AGRDPPVERA RGDGDGGHEF
MSVVVEGGEL REQLLGLRIG IEEDRHRDER QAHHRPYRRS TRCTAGSLYI GDFIAGRTTV
VGAIGAGPPS QRRFAFPEVN DCGPSSNIFA KCCAPGTILF GNIFDLPNFP RMSDVRAGSN
DPPGKYLCLT ICGYRKPGMS EEDYRHHMTK ISAPMTKDLM VKYGIKRWTM IHSPAVTRTL
MDQLYDSQMV NLADFDCFSQ VVFKSVEDYK RMKEDPYYKE HLFKDHEHFA DTKKSLFVHF
MPLPPPLGPC PGS
