ID   ORYE_ASPOR              Reviewed;         447 AA.
AC   Q2TXF1;
DT   12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Citrate synthase-like protein oryE {ECO:0000303|PubMed:30104550};
DE            EC=2.3.3.- {ECO:0000305|PubMed:30104550};
DE   AltName: Full=Oryzines biosynthesis cluster protein E {ECO:0000303|PubMed:30104550};
GN   Name=oryE {ECO:0000303|PubMed:30104550}; ORFNames=AO090010000170;
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: Citrate synthase-like protein; part of the gene cluster that
CC       mediates the biosynthesis of oryzines, natural products with an unusual
CC       maleidride backbone (PubMed:30104550). The two subunits of the fungal
CC       fatty acid synthase oryfasA and oryfasB probably form octenoic acid
CC       (Probable). This fatty acid is most likely activated by the acyl-CoA
CC       ligase oryP to give octenyl-CoA before the citrate synthase-like
CC       protein oryE catalyzes condensation with oxaloacetate to form
CC       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 citrate synthase family. {ECO:0000305}.
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DR   EMBL; AP007175; BAE66072.1; -; Genomic_DNA.
DR   RefSeq; XP_001827205.1; XM_001827153.1.
DR   AlphaFoldDB; Q2TXF1; -.
DR   SMR; Q2TXF1; -.
DR   STRING; 510516.Q2TXF1; -.
DR   EnsemblFungi; BAE66072; BAE66072; AO090010000170.
DR   GeneID; 5999339; -.
DR   KEGG; aor:AO090010000170; -.
DR   VEuPathDB; FungiDB:AO090010000170; -.
DR   HOGENOM; CLU_025068_0_1_1; -.
DR   OMA; QGFMAHW; -.
DR   Proteomes; UP000006564; Chromosome 8.
DR   GO; GO:0046912; F:acyltransferase activity, acyl groups converted into alkyl on transfer; IEA:InterPro.
DR   Gene3D; 1.10.230.10; -; 1.
DR   Gene3D; 1.10.580.10; -; 1.
DR   InterPro; IPR016142; Citrate_synth-like_lrg_a-sub.
DR   InterPro; IPR016143; Citrate_synth-like_sm_a-sub.
DR   InterPro; IPR002020; Citrate_synthase.
DR   InterPro; IPR019810; Citrate_synthase_AS.
DR   InterPro; IPR024176; Citrate_synthase_bac-typ.
DR   InterPro; IPR036969; Citrate_synthase_sf.
DR   PANTHER; PTHR11739; PTHR11739; 1.
DR   Pfam; PF00285; Citrate_synt; 1.
DR   PIRSF; PIRSF001369; Citrate_synth; 1.
DR   PRINTS; PR00143; CITRTSNTHASE.
DR   SUPFAM; SSF48256; SSF48256; 1.
DR   PROSITE; PS00480; CITRATE_SYNTHASE; 1.
PE   3: Inferred from homology;
KW   Reference proteome; Transferase.
FT   CHAIN           1..447
FT                   /note="Citrate synthase-like protein oryE"
FT                   /id="PRO_0000450491"
FT   ACT_SITE        331
FT                   /evidence="ECO:0000255|PIRSR:PIRSR001369-1"
FT   ACT_SITE        387
FT                   /evidence="ECO:0000255|PIRSR:PIRSR001369-1"
SQ   SEQUENCE   447 AA;  49674 MW;  DFD7ECF141735F80 CRC64;
     MTVTQEASPK RESLHIIDDR TGSYYSIPIV NNAINASDFK KVTAPEDKAY PANQTENGLR
     VYDPGYSNTA VSHSKITYID GLKGTIQYRG YSINDIVGRK TFIDTAHLLI WGHWPSTAEA
     ETLQQRLDQV PVPQDFVFNV IKSFPRDGSL MGMVIAGLSA LQSSDMNAIP AHVGKTIYLN
     NPELADQQII RVMANMSMLT AAAYCHHIGR DFTPPRAGLS YIENFLLMTG HVEAATGLPN
     PRYVNAIERL WVLIADHEMT CSTAALLQTA SALPDVISCM VSAISALYGP LHGGAIEVAY
     KNIESIGSIS NVPAKIARVK AGKERLYGYG HRVYRVTDPR FVFIREILNE LSEEVEKDPL
     LKVAFEVDRV ASEDEYFTSR NLRPNADLFA AFVYKALGFP PEFILPLSIL SRTQGFMAHW
     REAMGNPPRI WRPGQIYTGD LNKSMDE