ID   AT329_ASPTN             Reviewed;         162 AA.
AC   Q0D155;
DT   15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 39.
DE   RecName: Full=Putative oxygenase ATEG_00329 {ECO:0000305};
DE            EC=1.-.-.- {ECO:0000305};
DE   AltName: Full=Isoflavipucine biosynthesis cluster protein ATEG_00329 {ECO:0000303|PubMed:21236704};
GN   ORFNames=ATEG_00329;
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   IDENTIFICATION IN THE ISOFLAVIPUCINE CLUSTER, FUNCTION, AND INDUCTION.
RX   PubMed=21236704; DOI=10.1016/j.chembiol.2010.12.011;
RA   Gressler M., Zaehle C., Scherlach K., Hertweck C., Brock M.;
RT   "Multifactorial induction of an orphan PKS-NRPS gene cluster in Aspergillus
RT   terreus.";
RL   Chem. Biol. 18:198-209(2011).
CC   -!- FUNCTION: Putative oxygenase; part of the gene cluster that mediates
CC       the biosynthesis of isoflavipucine (PubMed:21236704). The PKS part of
CC       the PKS-NRPS ATEG_00325 probably assembles a triketide from an acetyl
CC       starter and two malonyl-CoA extender units (PubMed:21236704). The poly-
CC       beta-keto intermediate would then be fused to the leucine unit by the
CC       NRPS part (PubMed:21236704). The resulting amide would be liberated
CC       from the PKS-NRPS through reductive release of the linear PKS-NRPS
CC       product from the enzyme complex (PubMed:21236704). Further steps in
CC       isoflapucine synthesis include a cyclization step, an oxidation step, a
CC       hydrolysis step involving a trans-amidation, and an additional
CC       oxidation step, leading to flavipucine (PubMed:21236704). Formation of
CC       isoflavipucine from flavipucine requires an unusual rearrangement
CC       (PubMed:21236704). Alternative rearrangement reactions could build up
CC       rubrobramide, representing a branching of flavipucine biosynthesis
CC       (PubMed:21236704). The enzymes involved in the post-PKS-NRPS steps have
CC       not been identified yet, but the putative oxygenases ATEG_003329 and
CC       ATEG_00330 encoded by the cluster could play a role (PubMed:21236704).
CC       {ECO:0000269|PubMed:21236704}.
CC   -!- INDUCTION: Expression is positively controled by the cluster-specific
CC       regulator ATEG_00326 (PubMed:21236704). {ECO:0000269|PubMed:21236704}.
CC   -!- SIMILARITY: Belongs to the tpcK family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CH476594; EAU38975.1; -; Genomic_DNA.
DR   RefSeq; XP_001210415.1; XM_001210415.1.
DR   AlphaFoldDB; Q0D155; -.
DR   EnsemblFungi; EAU38975; EAU38975; ATEG_00329.
DR   GeneID; 4355081; -.
DR   VEuPathDB; FungiDB:ATEG_00329; -.
DR   eggNOG; ENOG502SNGW; Eukaryota.
DR   HOGENOM; CLU_115019_0_1_1; -.
DR   OMA; LGWVETY; -.
DR   OrthoDB; 1621831at2759; -.
DR   Proteomes; UP000007963; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR011008; Dimeric_a/b-barrel.
DR   InterPro; IPR009799; EthD_dom.
DR   Pfam; PF07110; EthD; 1.
DR   SUPFAM; SSF54909; SSF54909; 1.
PE   2: Evidence at transcript level;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN           1..162
FT                   /note="Putative oxygenase ATEG_00329"
FT                   /id="PRO_0000438999"
FT   DOMAIN          19..113
FT                   /note="EthD"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   162 AA;  18447 MW;  AB330943A3EFE3D1 CRC64;
     MSPVKQRLLR IAVSHNRHPS LSEEQFHQWA TKEHCARAAR IHSRHGIEAY GMLFSPETAR
     TTVQNLNRQL GGRWKIDEHD VTVEFYLHSL DELTSVLEDP EFKALQQEEE PYVSGEDIVA
     TLGWVETYVQ DGRVVNVDSE GVPTYPGFGV LADFSSEQVN QK