ORYK_ASPOR
ID ORYK_ASPOR Reviewed; 625 AA.
AC Q2TXF6;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 12-AUG-2020, sequence version 2.
DT 25-MAY-2022, entry version 72.
DE RecName: Full=Ankyrin repeat domain-containing protein oryK {ECO:0000303|PubMed:30104550};
DE AltName: Full=Oryzines biosynthesis cluster protein K {ECO:0000303|PubMed:30104550};
GN Name=oryK {ECO:0000303|PubMed:30104550}; ORFNames=AO090010000165;
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: Ankyrin repeat domain-containing 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 -!- SEQUENCE CAUTION:
CC Sequence=BAE66067.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP007175; BAE66067.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001827200.2; XM_001827148.2.
DR AlphaFoldDB; Q2TXF6; -.
DR SMR; Q2TXF6; -.
DR EnsemblFungi; BAE66067; BAE66067; AO090010000165.
DR GeneID; 5999334; -.
DR KEGG; aor:AO090010000165; -.
DR HOGENOM; CLU_683294_0_0_1; -.
DR Proteomes; UP000006564; Chromosome 8.
DR Gene3D; 1.25.40.20; -; 3.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR Pfam; PF12796; Ank_2; 2.
DR SMART; SM00248; ANK; 6.
DR SUPFAM; SSF48403; SSF48403; 2.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
PE 4: Predicted;
KW ANK repeat; Reference proteome; Repeat.
FT CHAIN 1..625
FT /note="Ankyrin repeat domain-containing protein oryK"
FT /id="PRO_0000450495"
FT REPEAT 1..27
FT /note="ANK 1"
FT /evidence="ECO:0000255"
FT REPEAT 31..60
FT /note="ANK 2"
FT /evidence="ECO:0000255"
FT REPEAT 62..89
FT /note="ANK 3"
FT /evidence="ECO:0000255"
FT REPEAT 90..119
FT /note="ANK 4"
FT /evidence="ECO:0000255"
FT REPEAT 162..195
FT /note="ANK 5"
FT /evidence="ECO:0000255"
FT REPEAT 202..232
FT /note="ANK 6"
FT /evidence="ECO:0000255"
FT REPEAT 500..530
FT /note="ANK 7"
FT /evidence="ECO:0000255"
FT REPEAT 534..562
FT /note="ANK 8"
FT /evidence="ECO:0000255"
FT REPEAT 568..598
FT /note="ANK 9"
FT /evidence="ECO:0000255"
SQ SEQUENCE 625 AA; 69625 MW; 723E5EA52BA5F0C4 CRC64;
MDIYEAASQG RIDAIKFAVE QGCDVDGPNE DGKTPLWFAV QSGQPEACRF LMSLGAGRGP
QNPSLLEVAV GGGYADIVAL LWPHCNAERE HRSLKTAISL GFHEIADFLI ETGAFEYQDS
EVSGTESLIE DGSPERESTV FQQWERFLFV RRGQKLPLHR VFFDYALLLA TKAGRNAGLR
LVEFLLGESM PDVNCKIMIN GQFETPLTAA AEKGNLEILA TLIDHPNIDL TICGKYNWPA
FLHLLASPLS ISTERGRVIA RRLAYKAVYN RLFIDSREIR LQGAFQNVLR FGDDGLVKQV
IDLVRGAAGT LILPLLIRAN EVDGLTWVLN CDGVSSKKPP PAFWVLLCQY FKRYQDQDAL
GLFTSVTEFL VEKKIWNQAI LKCLHACNFS FIQQFFYPLS EAPPKEVTEE TLSPGFENLL
FSNADLNGSD PHPNGLGRLE LEIIPHAFFD DPSSAAQKIS LRSALPSASP NPSNPHLYSY
QMELIRLEQQ NKRRLFFAGD TRCPLSWAAK SHNAPLVNAL LRSPQVNVNF QDPSDRTPLL
YAIAVNDRPI VERLLNHRDI DLNLRDAEGR TAIFYAAQGG DLSIVQLLIG TQNVDFSIRN
KNGKNVKEFA KKAKLKQDIV AALSN
