ID   ORYL_ASPOR              Reviewed;         436 AA.
AC   Q2TXF9;
DT   12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT   12-AUG-2020, sequence version 2.
DT   25-MAY-2022, entry version 48.
DE   RecName: Full=Lactonohydrolase oryL {ECO:0000303|PubMed:30104550};
DE            EC=3.1.1.- {ECO:0000305|PubMed:30104550};
DE   AltName: Full=Oryzines biosynthesis cluster protein L {ECO:0000303|PubMed:30104550};
DE   Flags: Precursor;
GN   Name=oryL {ECO:0000303|PubMed:30104550}; ORFNames=AO090010000162;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
RN   [2]
RP   FUNCTION, AND PATHWAY.
RX   PubMed=30104550; DOI=10.3390/jof4030096;
RA   Wasil Z., Kuhnert E., Simpson T.J., Cox R.J.;
RT   "Oryzines A & B, maleidride congeners from Aspergillus oryzae and their
RT   putative biosynthesis.";
RL   J. Fungi 4:0-0(2018).
CC   -!- FUNCTION: Lactonohydrolase; part of the gene cluster that mediates the
CC       biosynthesis of oryzines, natural products with an unusual maleidride
CC       backbone (PubMed:30104550). The two subunits of the fungal fatty acid
CC       synthase oryfasA and oryfasB probably form octenoic acid (Probable).
CC       This fatty acid is most likely activated by the acyl-CoA ligase oryP to
CC       give octenyl-CoA before the citrate synthase-like protein oryE
CC       catalyzes condensation with oxaloacetate to form tricarboxylic acid
CC       (Probable). The next steps of the pathways are conjectural, but a
CC       favorite possible route has been proposed, beginning with
CC       decarboxylation and concomitant dehydration by the decarboxylase oryM,
CC       followed by tautomerization, which may lead to the production of a
CC       diene intermediate (Probable). Reduction of this diene intermediate
CC       could give the known metabolite piliformic acid (Probable). On the
CC       pathway to oryzine B and oryzine A, however, hydroxylation of the diene
CC       by the alpha-ketoglutarate-dependent dioxygenase oryG and lactonisation
CC       by the lactonohydrolases oryH or oryL could give oryzine B directly
CC       (Probable). Finally, enoyl reduction by the dehydrogenase oryD would
CC       then convert oryzine B into oryzine A (Probable).
CC       {ECO:0000269|PubMed:30104550, ECO:0000305|PubMed:30104550}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000305|PubMed:30104550}.
CC   -!- SIMILARITY: Belongs to the SMP-30/CGR1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE66064.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AP007175; BAE66064.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001827197.2; XM_001827145.2.
DR   AlphaFoldDB; Q2TXF9; -.
DR   SMR; Q2TXF9; -.
DR   STRING; 510516.Q2TXF9; -.
DR   EnsemblFungi; BAE66064; BAE66064; AO090010000162.
DR   VEuPathDB; FungiDB:AO090701000942; -.
DR   HOGENOM; CLU_946583_0_0_1; -.
DR   Proteomes; UP000006564; Chromosome 8.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   Gene3D; 2.120.10.30; -; 1.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR013658; SGL.
DR   Pfam; PF08450; SGL; 2.
PE   3: Inferred from homology;
KW   Hydrolase; Reference proteome; Signal.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..436
FT                   /note="Lactonohydrolase oryL"
FT                   /id="PRO_0000450498"
SQ   SEQUENCE   436 AA;  47903 MW;  CA15791922B51389 CRC64;
     MLSYTSHCLQ ALLGVASLPY RQYQAYSSPQ APLQVPQVPQ AGPPITTLVS SCAGFSYPEV
     ACIDRYGSLL QGEFERKVRN VLGDADTYIS TNAPSEPTFS DLQNADFLVW NQSAAKAILG
     PNPHVDFMFS IEDCSHEAPV YVPTTNELYF SRLQQGFLPQ LVINLNNDPP TLEEKLAQPP
     IYAATGARFR DGLLYLATIG GNESLAGYTF RPGLYTLDPI TGKTQALLNN YYGYYFNAVD
     DLDIDHEGQI WFTDNDYGRP CQVNTYAPQI NAATYRFNPK TGLVTMVDDT LLEPNGLTFS
     PDNKTVYLTD TGAGSAIIDP NIYPAPHIAY NSTRKGRTIY AYDVAPSRKA LLNKRPVYLS
     MEYAPDGIKT SREGYLVSAT GKGVVVLTDE GEPLVRVQTN FTVINIAFAG AERDELWAIG
     KGGVARIRWG LKGSYA