TAZO_ASPTN
ID TAZO_ASPTN Reviewed; 435 AA.
AC Q0CS95;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=O-methyltransferase tazO {ECO:0000303|PubMed:35398258};
DE EC=2.1.1.- {ECO:0000305|PubMed:35398258};
DE AltName: Full=Azaphilone biosynthesis cluster protein O {ECO:0000303|PubMed:35398258};
GN Name=tazO {ECO:0000303|PubMed:35398258}; ORFNames=ATEG_03439;
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, INDUCTION, AND PATHWAY.
RX PubMed=35398258; DOI=10.1016/j.fgb.2022.103694;
RA Sun W.W., Li C.Y., Chiang Y.M., Lin T.S., Warren S., Chang F.R.,
RA Wang C.C.C.;
RT "Characterization of a silent azaphilone biosynthesis gene cluster in
RT Aspergillus terreus NIH 2624.";
RL Fungal Genet. Biol. 160:103694-103694(2022).
CC -!- FUNCTION: O-methyltransferase; part of the gene cluster that mediates
CC the biosynthesis of azaterrilone A and other azaphilones, a class of
CC fungal metabolites characterized by a highly oxygenated pyrano-quinone
CC bicyclic core and exhibiting a broad range of bioactivities
CC (PubMed:35398258). The first step of the pathway begins with the non-
CC reducing polyketide synthase tazA that assembles one acetyl-CoA starter
CC unit, five malonyl-CoA units, and catalyzes a series of Claisen
CC condensations, methylation, PT-mediated cyclization, and finally
CC releases the first hexaketide precursor through the R-domain. The tazA
CC product then undergoes reduction on its terminal ketone and the
CC following pyran-ring formation by yet undetermined enzyme(s).
CC Dehydration and enoyl reduction, possibly involving the trans-enoyl
CC reductase tazE leads to the next intermediate. TazD is predicted as an
CC acetyltransferase and might catalyze the acetylation steps leading to
CC the synthesis of azaterrilone A. Azaterrilone A is not the final
CC product of the taz pathway and both the highly reducing polyketide
CC synthase tazB and the dual enzyme tazHJ catalyze late steps of the
CC pathway, leading to the production of the 2 final stereoisomers that
CC contain additional polyketide modification whose structures have still
CC to be determined (Probable). {ECO:0000269|PubMed:35398258,
CC ECO:0000305|PubMed:35398258}.
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000305|PubMed:35398258}.
CC -!- INDUCTION: Expression is positively regulated by the azaterrilone A
CC cluster-specific transcription factor tazR.
CC {ECO:0000269|PubMed:35398258}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Cation-independent O-methyltransferase family.
CC {ECO:0000305}.
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DR EMBL; CH476597; EAU36713.1; -; Genomic_DNA.
DR RefSeq; XP_001212617.1; XM_001212617.1.
DR STRING; 33178.CADATEAP00010354; -.
DR EnsemblFungi; EAU36713; EAU36713; ATEG_03439.
DR GeneID; 4317483; -.
DR VEuPathDB; FungiDB:ATEG_03439; -.
DR eggNOG; KOG3178; Eukaryota.
DR HOGENOM; CLU_005533_1_4_1; -.
DR OMA; IQQMGTA; -.
DR OrthoDB; 817726at2759; -.
DR Proteomes; UP000007963; Unassembled WGS sequence.
DR GO; GO:0008171; F:O-methyltransferase activity; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR016461; COMT-like.
DR InterPro; IPR001077; O_MeTrfase_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00891; Methyltransf_2; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51683; SAM_OMT_II; 1.
PE 2: Evidence at transcript level;
KW Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..435
FT /note="O-methyltransferase tazO"
FT /id="PRO_0000456071"
FT ACT_SITE 333
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 288
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
SQ SEQUENCE 435 AA; 47807 MW; BFC23A485AA449C0 CRC64;
MTKTITLEGL ADQVQAQAST LSTLLAEANL PSPSFGPDAP PAPPHGKEFE KIQAARMALI
ESANAIRDLA LGPEDCITAF SDGIKHDLAA LHVIVDFNIP ELVPLHGEVS YAEIAQKVGF
PEYRVHRILR HAMTSRIFRE PRPGYVAHTG PSAAFLRNPV LRDWVSFNLD EVWKADTKLV
ETLRTCGDSE EPADSAIGRA FGFAPGKTYW DFIANDGEGE NKGWRQRRFA QGMKCRAAGN
PQTHHHLHSA FDWAGLGKAT VIDVGGSAGH VSIELAKAFP DLEFVVQDFE GLKSFHDGVP
DELKSRISFE AQDILQPNAH PNADVYLLRS ILHDWSDKYA VLILKNLVPA LKDGARVLIA
DFIGPENTQS GPMWLERLST IRSMQMMTMV NAPERSEKDW INVVKRADSR YSVKAVVTPA
GTAMSVIEIV FNASA
