ID   ORYM_ASPOR              Reviewed;         482 AA.
AC   Q2TXG0;
DT   12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 65.
DE   RecName: Full=Cis-aconitate decarboxylase-like protein oryM {ECO:0000303|PubMed:30104550};
DE            EC=4.1.1.- {ECO:0000305|PubMed:30104550};
DE   AltName: Full=Oryzines biosynthesis cluster protein M {ECO:0000303|PubMed:30104550};
GN   Name=oryM {ECO:0000303|PubMed:30104550}; ORFNames=AO090010000161;
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: Cis-aconitate decarboxylase-like protein; part of the gene
CC       cluster that mediates the biosynthesis of oryzines, natural products
CC       with an unusual maleidride backbone (PubMed:30104550). The two subunits
CC       of the fungal fatty acid synthase oryfasA and oryfasB probably form
CC       octenoic acid (Probable). This fatty acid is most likely activated by
CC       the acyl-CoA ligase oryP to give octenyl-CoA before the citrate
CC       synthase-like protein oryE catalyzes condensation with oxaloacetate to
CC       form tricarboxylic acid (Probable). The next steps of the pathways are
CC       conjectural, but a favorite possible route has been proposed, beginning
CC       with decarboxylation and concomitant dehydration by the decarboxylase
CC       oryM, followed by tautomerization, which may lead to the production of
CC       a 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 PrpD 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; AP007175; BAE66063.1; -; Genomic_DNA.
DR   RefSeq; XP_001827196.1; XM_001827144.1.
DR   AlphaFoldDB; Q2TXG0; -.
DR   SMR; Q2TXG0; -.
DR   STRING; 510516.Q2TXG0; -.
DR   EnsemblFungi; BAE66063; BAE66063; AO090010000161.
DR   GeneID; 5999330; -.
DR   KEGG; aor:AO090010000161; -.
DR   VEuPathDB; FungiDB:AO090010000161; -.
DR   HOGENOM; CLU_026574_1_1_1; -.
DR   OMA; ESELHYR; -.
DR   Proteomes; UP000006564; Chromosome 8.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.4100.10; -; 1.
DR   InterPro; IPR036148; MmgE/PrpD_sf.
DR   InterPro; IPR042183; MmgE/PrpD_sf_1.
DR   InterPro; IPR005656; MmgE_PrpD.
DR   InterPro; IPR045337; MmgE_PrpD_C.
DR   InterPro; IPR045336; MmgE_PrpD_N.
DR   PANTHER; PTHR16943; PTHR16943; 1.
DR   Pfam; PF03972; MmgE_PrpD; 1.
DR   Pfam; PF19305; MmgE_PrpD_C; 1.
DR   SUPFAM; SSF103378; SSF103378; 1.
PE   3: Inferred from homology;
KW   Lyase; Reference proteome.
FT   CHAIN           1..482
FT                   /note="Cis-aconitate decarboxylase-like protein oryM"
FT                   /id="PRO_0000450492"
SQ   SEQUENCE   482 AA;  51851 MW;  0C2FB1183D2F8D35 CRC64;
     MTVTDSTPEG NVTAELCNWV TELKPSDIPA DVLQRAKHLL LDGIACGLVG SHVPWSEQAA
     KAIDDYEPEG YCSVIGYNRR YGPQAAAILN GSFIQAVELD DYHSAAPLHS ASVLLPALFA
     AAEVQSKGHR KSVVSGLDFL VALVVGFETG PRVGSAMYGA DLLSRGWHSG PVFGSPAAAA
     ASSKLLGLSP DDTESAVGIA CTQAGGLMAA QYEGMVKRVQ HAFAARNGLF GALLARDGYV
     GIKKVFDRSY GGFLTMFTQG NGRTPQYKPE EVTTALGKEW QTTNIRVKLH ACVGGCHGQI
     EALEKLQRNY PDRFAVDQLH NIRRITVSLS EPVFAHDGWA PEERPLTATG GQMNAAYIGA
     AQLVYGQVLL DQFEPHALDS DAVWSLIDKT TCVHSSEFDK PGHLCGARIV VEFNDGETVE
     DVVAMPKGFD PPITDDEIRE KWRKLASSVI DSERLQRIEN SVLSLETSAD VSELLALISG
     EL