ID   ORYR_ASPOR              Reviewed;         496 AA.
AC   Q2TXG4;
DT   12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 67.
DE   RecName: Full=2-methylcitrate dehydratase-like protein oryR {ECO:0000303|PubMed:30104550};
DE            EC=4.2.1.- {ECO:0000305|PubMed:30104550};
DE   AltName: Full=Oryzines biosynthesis cluster protein R {ECO:0000303|PubMed:30104550};
GN   Name=oryR {ECO:0000303|PubMed:30104550}; ORFNames=AO090010000155;
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: 2-methylcitrate dehydratase-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}.
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DR   EMBL; AP007175; BAE66059.1; -; Genomic_DNA.
DR   RefSeq; XP_001827192.1; XM_001827140.1.
DR   AlphaFoldDB; Q2TXG4; -.
DR   SMR; Q2TXG4; -.
DR   STRING; 510516.Q2TXG4; -.
DR   EnsemblFungi; BAE66059; BAE66059; AO090010000155.
DR   GeneID; 5999326; -.
DR   KEGG; aor:AO090010000155; -.
DR   HOGENOM; CLU_021803_1_0_1; -.
DR   OMA; RDHCLRY; -.
DR   Proteomes; UP000006564; Chromosome 8.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0047547; F:2-methylcitrate dehydratase activity; IEA:InterPro.
DR   GO; GO:0019679; P:propionate metabolic process, methylcitrate cycle; IEA:InterPro.
DR   Gene3D; 1.10.4100.10; -; 1.
DR   Gene3D; 3.30.1330.120; -; 1.
DR   InterPro; IPR012705; 2Me_IsoCit_deHydtase_PrpD.
DR   InterPro; IPR036148; MmgE/PrpD_sf.
DR   InterPro; IPR042183; MmgE/PrpD_sf_1.
DR   InterPro; IPR042188; MmgE/PrpD_sf_2.
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.
DR   TIGRFAMs; TIGR02330; prpD; 1.
PE   3: Inferred from homology;
KW   Lyase; Reference proteome.
FT   CHAIN           1..496
FT                   /note="2-methylcitrate dehydratase-like protein oryR"
FT                   /id="PRO_0000450493"
SQ   SEQUENCE   496 AA;  54434 MW;  4209EEAD3856C958 CRC64;
     MTIPAADDNN CPSYDKVIDL IVDYAYDYEI DSPAAWTRAK AALIDALGAA IESIHTSPEC
     AAMIGPVWPQ TATVPGGFRL PGTQFQVDAL KGAFDLGGMI RYLDHNDAFP GAEWGHPSDN
     LGAILSTADI LSREALARGS PEEVISMKQV LTALIKAYEI QGVFQIRNAF NKVGLDHVIL
     VKVASSAMVS WLMGLSRDQA RAVVSHAWAD GHPLRVYRQA PNAGPRKGWA AGDACMRAVH
     LANLVRCGQP GIRSAITTPR WGFYDVLYRG QTFELPRPFT SWVMETVLFK VSTAEGHGLT
     AVEAALTIAE KLAQRGLRPE EDIVNIRART QEAGMIIINK KGPLHNAADR DHCLRYMVAV
     VLLKGSQITT ADYQDSSPWA RDPRVETLRS ITTMEEDPSF TRDYHDPQCR SVANALEVTL
     RDGTKLEELV PFPLGHVRRP ETLQLVREKA QQNLGLKLSS ERVGQILDTV DQPKFEKMAA
     SDFVDLFIPQ PASSAA