ID   ORYH_ASPOR              Reviewed;         469 AA.
AC   Q2TXF4;
DT   12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=Lactonohydrolase oryH {ECO:0000303|PubMed:30104550};
DE            EC=3.1.1.- {ECO:0000305|PubMed:30104550};
DE   AltName: Full=Oryzines biosynthesis cluster protein H {ECO:0000303|PubMed:30104550};
DE   Flags: Precursor;
GN   Name=oryH {ECO:0000303|PubMed:30104550}; ORFNames=AO090010000167;
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}.
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DR   EMBL; AP007175; BAE66069.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2TXF4; -.
DR   STRING; 510516.Q2TXF4; -.
DR   EnsemblFungi; BAE66069; BAE66069; AO090010000167.
DR   HOGENOM; CLU_036110_1_1_1; -.
DR   OMA; WLLNNYY; -.
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..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..469
FT                   /note="Lactonohydrolase oryH"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5004216808"
SQ   SEQUENCE   469 AA;  50947 MW;  F96E2A6E26388284 CRC64;
     MYLSLRLVSL ALCIAPLASA GNNSTPLVQA CTGYSFPRVA CMYRYASKMP LDFYRKASVD
     ISNVDTYSST EVANDDSFQQ VGKATFLVWD QQRGSEILGS DPAYDIVFTI STGGHEAPVY
     VPDTNELWFS ELGKGELHQQ VISLDGDSPT ISEVLTDPPL YAPSGARYRN GKIYFSAGGG
     NSTLEGGPYH PGIYSVDPKT RKSTIEVNNY FGWYFNQVSM PTAHTRGGSP LSHFCTLVDP
     RLVAHGLTFQ HRPTTWILTN TVASGLVILV SSWTRDLTLV HTDAAIVLAR NHGTSTVAPQ
     VQASVYRYDP ETGAVNIVDD TLHCPNGVAF SPDYKTLYLT DTDAGVPMID PRVPLSEVPS
     LQYNSTNRRT VYAFDVSEDG SYLKNRRPIY TAKDFVPDGL KVASNGYVIT GAGKGVDILD
     TTGTPLLSIQ TNFTAVNMVF GGKNLDELWI VGHGAVARAR LNLTGPALE