GEDB_ASPTN
ID GEDB_ASPTN Reviewed; 320 AA.
AC Q0CCY4;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Atrochrysone carboxyl ACP thioesterase {ECO:0000303|PubMed:19549600};
DE Short=ACTE {ECO:0000303|PubMed:19549600};
DE EC=3.1.2.- {ECO:0000269|PubMed:19549600};
DE AltName: Full=Geodin synthesis protein B {ECO:0000303|PubMed:24009710};
GN Name=gedB {ECO:0000303|PubMed:24009710}; ORFNames=ATEG_08450;
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: Atrochrysone carboxyl ACP thioesterase; 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 -!- CATALYTIC ACTIVITY:
CC Reaction=atrochrysone carboxyl-[ACP] + H2O = atrochrysone carboxylate +
CC H(+) + holo-[ACP]; Xref=Rhea:RHEA:64236, Rhea:RHEA-COMP:9685,
CC Rhea:RHEA-COMP:16552, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:64479, ChEBI:CHEBI:149712, ChEBI:CHEBI:149713;
CC Evidence={ECO:0000269|PubMed:19549600};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64237;
CC Evidence={ECO:0000269|PubMed:19549600};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q988B9};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q988B9};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:24009710}.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
CC {ECO:0000305}.
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DR EMBL; CH476605; EAU31623.1; -; Genomic_DNA.
DR RefSeq; XP_001217071.1; XM_001217071.1.
DR AlphaFoldDB; Q0CCY4; -.
DR SMR; Q0CCY4; -.
DR STRING; 341663.Q0CCY4; -.
DR EnsemblFungi; EAU31623; EAU31623; ATEG_08450.
DR GeneID; 4353100; -.
DR VEuPathDB; FungiDB:ATEG_08450; -.
DR eggNOG; KOG0813; Eukaryota.
DR HOGENOM; CLU_048478_1_0_1; -.
DR OMA; EGGYRQI; -.
DR OrthoDB; 576967at2759; -.
DR BioCyc; MetaCyc:MON-21292; -.
DR Proteomes; UP000007963; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.60.15.10; -; 1.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR Pfam; PF00753; Lactamase_B; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..320
FT /note="Atrochrysone carboxyl ACP thioesterase"
FT /id="PRO_0000437054"
FT ACT_SITE 107
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q988B9"
FT BINDING 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q988B9"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q988B9"
FT BINDING 108
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q988B9"
SQ SEQUENCE 320 AA; 35324 MW; 08B5337279C36F57 CRC64;
MKRGGYRQIN KALNISAFEN YLDIQHDHLP KLNDVEQLSP RVLRVLGQNA GKFTLQGTNT
YIVGTGRERL IIDTGQGIPE WTDLISSTLR DSAITLSHVL LTHWHGDHTG GVPDLIRLYP
HLSNSIFKHS SSNGQQPIID GQVFHVEGAT VRAMHSPGHS HDHMCFILEE ENAMFTGDNV
LGHGTSAVEL LGIWMASLRL MQSSGCRVGY PAHGAVIADL LAKIAGELDQ KARREARVVR
TLARNKREEQ SKGRSKGSMT VQELVTAMHG KGLDDQVRTM ALEPFINEVL GKLAGDGCVA
FEVRRGEKRW FIVNDVTSSP
