TAZI_ASPTN
ID TAZI_ASPTN Reviewed; 489 AA.
AC Q0CS90;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 03-AUG-2022, sequence version 2.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Cytochrome P450 monooxygenase tazI {ECO:0000303|PubMed:35398258};
DE EC=1.-.-.- {ECO:0000305|PubMed:35398258};
DE AltName: Full=Azaphilone biosynthesis cluster protein I {ECO:0000303|PubMed:35398258};
GN Name=tazI {ECO:0000303|PubMed:35398258}; ORFNames=ATEG_03444;
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: Cytochrome P450 monooxygenase; part of the gene cluster that
CC mediates the biosynthesis of azaterrilone A and other azaphilones, a
CC class of fungal metabolites characterized by a highly oxygenated
CC pyrano-quinone bicyclic core and exhibiting a broad range of
CC bioactivities (PubMed:35398258). The first step of the pathway begins
CC with the non-reducing polyketide synthase tazA that assembles one
CC acetyl-CoA starter unit, five malonyl-CoA units, and catalyzes a series
CC of Claisen condensations, methylation, PT-mediated cyclization, and
CC finally releases the first hexaketide precursor through the R-domain.
CC The tazA product then undergoes reduction on its terminal ketone and
CC the 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 -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
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 cytochrome P450 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAU36718.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CH476597; EAU36718.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001212622.1; XM_001212622.1.
DR EnsemblFungi; EAU36718; EAU36718; ATEG_03444.
DR GeneID; 4317677; -.
DR VEuPathDB; FungiDB:ATEG_03444; -.
DR eggNOG; KOG0158; Eukaryota.
DR HOGENOM; CLU_001570_14_9_1; -.
DR OMA; ERRGCID; -.
DR OrthoDB; 467733at2759; -.
DR Proteomes; UP000007963; Unassembled WGS sequence.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:InterPro.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 2: Evidence at transcript level;
KW Heme; Iron; Metal-binding; Monooxygenase; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..489
FT /note="Cytochrome P450 monooxygenase tazI"
FT /id="PRO_0000456075"
FT BINDING 433
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P04798"
SQ SEQUENCE 489 AA; 55336 MW; 77929DA95BD29F3F CRC64;
MAYIQASSTQ AVVVLLLVLV LTKIYRVYTG PLAHLPGPAI SKWTGLVLQK HLFAGNRPRY
VQKLHQLYGP IVRISPDELD VSDSAAAKSI HRVASRFYKG RFYEHIGHRS PKTLFSSTDP
QFHAYRRRLL GGAMSETSIR QHEPTVAQKV KLCVDQMARE AERRGCIDVF KWWCFLATDT
IGELSFGESF RMLEKGEKSQ YSRDLELVST LMIIRTTFPF LSRVAEYVPL PYFKQAAQSG
KRMFGYASES IQRYKKHVEM KGXXXXXXXX XXXXXXXXXE GSLTEAEIRL EAGGYIVAGS
DTSAISLTYL VWAVCKNPLI RDSLVAEVAT LPEDFTDDDV RALPYTRRVI DETLRLYPAV
PGALPRAVPP EGATLVDHFI PGGVTVSTQV YSLHRDPKIF PDPDRRFDPD RWIDPTTEMR
DSFMPFGGGS RTCIGMHLAR MELRLATAHF FRRFTSPTVS TKEGFTDDDM YQHMYFLVSP
KGHRCLIDV
