ORYG_ASPOR
ID ORYG_ASPOR Reviewed; 341 AA.
AC Q2TXF3;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Alpha-ketoglutarate-dependent dioxygenase oryG {ECO:0000303|PubMed:30104550};
DE EC=1.14.11.- {ECO:0000305|PubMed:30104550};
DE AltName: Full=Oryzines biosynthesis cluster protein G {ECO:0000303|PubMed:30104550};
GN Name=oryG {ECO:0000303|PubMed:30104550}; ORFNames=AO090010000168;
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: Alpha-ketoglutarate-dependent dioxygenase; 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 -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:P37610};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250|UniProtKB:P37610};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000305|PubMed:30104550}.
CC -!- SIMILARITY: Belongs to the TfdA dioxygenase family. {ECO:0000305}.
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DR EMBL; AP007175; BAE66070.1; -; Genomic_DNA.
DR RefSeq; XP_001827203.1; XM_001827151.1.
DR AlphaFoldDB; Q2TXF3; -.
DR SMR; Q2TXF3; -.
DR EnsemblFungi; BAE66070; BAE66070; AO090010000168.
DR GeneID; 5999337; -.
DR KEGG; aor:AO090010000168; -.
DR VEuPathDB; FungiDB:AO090010000168; -.
DR HOGENOM; CLU_036005_1_0_1; -.
DR OMA; TAQHEVP; -.
DR Proteomes; UP000006564; Chromosome 8.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.60.130.10; -; 1.
DR InterPro; IPR042098; TauD-like_sf.
DR InterPro; IPR003819; TauD/TfdA-like.
DR Pfam; PF02668; TauD; 1.
PE 3: Inferred from homology;
KW Dioxygenase; Iron; Metal-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..341
FT /note="Alpha-ketoglutarate-dependent dioxygenase oryG"
FT /id="PRO_0000450494"
FT BINDING 100
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P37610"
FT BINDING 140
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P37610"
FT BINDING 142
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P37610"
FT BINDING 167
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:P37610"
FT BINDING 299
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P37610"
FT BINDING 311
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:P37610"
FT BINDING 315
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:P37610"
FT BINDING 315
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P37610"
SQ SEQUENCE 341 AA; 38365 MW; D13CA60DE87E55D8 CRC64;
MHSTKVTYPE PMQLSGILDQ YESFQVTPCI GTEFPKANLA EWLHSPNADA LLRDLAITIA
QRGVVFFRAQ TDLDGELQKE LTHRLGVQSG KPAGHRLSKH PLHLIRKDDP EMGVLDPGRQ
QKLHGVENTQ KRQRAVLEYH SDGSYEVCPP DFTMLRMTEI PPTGGDTLWA SGYELYDRLS
TPYQKFFESL TAQHEVPSLR KLAETEPGIY DGPRGAPANT DMQFKQSHPM VRTHPVTGWK
TLFAGGLHCR RVNDVTDFES EQLLSKIISL VGDNHDLQVR FRWNNPGDVA IWDNRCVLHC
PTQDHYGLGG RMGYRTMGIA EKPYLDPNSP SRQEALAAAA K
