ASQO_EMENI
ID ASQO_EMENI Reviewed; 365 AA.
AC P9WEP9; C8VJQ2; Q5AR52;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 25-MAY-2022, sequence version 1.
DT 03-AUG-2022, entry version 2.
DE RecName: Full=Quinolone epoxide rearrangement protein asqO {ECO:0000303|PubMed:28114276};
DE EC=1.-.-.- {ECO:0000269|PubMed:28114276};
DE AltName: Full=4'-methoxyviridicatin/aspoquinolone biosynthesis cluster protein asqO {ECO:0000303|PubMed:28114276};
DE AltName: Full=Aspoquinolone biosynthesis protein O {ECO:0000303|PubMed:28114276};
GN Name=asqO {ECO:0000303|PubMed:28114276}; ORFNames=AN9228, ANIA_11201;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [3]
RP FUNCTION.
RX PubMed=25251934; DOI=10.1002/anie.201407920;
RA Ishikawa N., Tanaka H., Koyama F., Noguchi H., Wang C.C., Hotta K.,
RA Watanabe K.;
RT "Non-heme dioxygenase catalyzes atypical oxidations of 6,7-bicyclic systems
RT to form the 6,6-quinolone core of viridicatin-type fungal alkaloids.";
RL Angew. Chem. Int. Ed. 53:12880-12884(2014).
RN [4]
RP FUNCTION.
RX PubMed=26553478; DOI=10.1002/anie.201507835;
RA Brauer A., Beck P., Hintermann L., Groll M.;
RT "Structure of the dioxygenase AsqJ: mechanistic insights into a one-pot
RT multistep quinolone antibiotic biosynthesis.";
RL Angew. Chem. Int. Ed. 55:422-426(2016).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=28114276; DOI=10.1038/nchembio.2283;
RA Zou Y., Garcia-Borras M., Tang M.C., Hirayama Y., Li D.H., Li L.,
RA Watanabe K., Houk K.N., Tang Y.;
RT "Enzyme-catalyzed cationic epoxide rearrangements in quinolone alkaloid
RT biosynthesis.";
RL Nat. Chem. Biol. 13:325-332(2017).
RN [6]
RP FUNCTION.
RX PubMed=30026518; DOI=10.1038/s41467-018-05221-5;
RA Kishimoto S., Hara K., Hashimoto H., Hirayama Y., Champagne P.A.,
RA Houk K.N., Tang Y., Watanabe K.;
RT "Enzymatic one-step ring contraction for quinolone biosynthesis.";
RL Nat. Commun. 9:2826-2826(2018).
CC -!- FUNCTION: Quinolone epoxide rearrangement protein; part of the gene
CC cluster that mediates the biosynthesis of the aspoquinolone mycotoxins
CC (PubMed:25251934, PubMed:28114276). The first stage is catalyzed by the
CC nonribosomal pepdide synthetase asqK that condenses anthranilic acid
CC and O-methyl-L-tyrosine to produce 4'-methoxycyclopeptin
CC (PubMed:25251934). AsqK is also able to use anthranilic acid and L-
CC phenylalanine as substrates to produce cyclopeptin, but at a tenfold
CC lower rate (PubMed:25251934). 4'-methoxycyclopeptin is then converted
CC to 4'-methoxydehydrocyclopeptin by the ketoglutarate-dependent
CC dioxygenase asqJ through dehydrogenation to form a double bond between
CC C-alpha and C-beta of the O-methyltyrosine side chain (PubMed:25251934,
CC PubMed:26553478). AsqJ also converts its first product 4'-
CC methoxydehydrocyclopeptin to 4'-methoxycyclopenin (PubMed:25251934).
CC AsqJ is a very unique dioxygenase which is capable of catalyzing
CC radical-mediated dehydrogenation and epoxidation reactions sequentially
CC on a 6,7-benzo-diazepinedione substrate in the 4'-methoxyviridicatin
CC biosynthetic pathway (PubMed:25251934). AsqJ is also capable of
CC converting cyclopeptin into dehydrocyclopeptin (PubMed:25251934). The
CC following conversion of 4'-methoxycyclopenin into 4'-methoxyviridicatin
CC is catalyzed by the cyclopenase asqI (PubMed:30026518). Cyclopenin can
CC also be converted into viridicatin by asqI (PubMed:30026518). 4'-
CC methoxyviridicatin is the precursor of quinolone natural products, and
CC is further converted to quinolinone B (Probable). The prenyltransferase
CC asqH1 then catalyzes the canonical Friedel-Crafts alkylation of
CC quinolinone B with dimethylallyl cation to yield dimethylallyl
CC quinolone, which is subjected to FAD-dependent dehydrogenation by the
CC FAD-linked oxidoreductase asqF to yield conjugated aryl diene (By
CC similarity). The delta(3') double bond then serves as the site of the
CC second alkylation with DMAPP catalyzed by the prenyltransferase asqH2
CC to yield a carbenium ion intermediate, which can be attacked by H(2)O
CC to yield a styrenyl quinolone containing a C3'-hydroxyprenyl chain (By
CC similarity). The FAD-dependent monooxygenase asqG performs epoxidation
CC of the terminal C7'-C8' olefin (PubMed:30026518). Finally, after
CC dehydratation of the epoxide at C3 by asqC, the quinolone epoxide
CC rearrangement protein asqO catalyzes an enzymatic 3-exo-tet cyclization
CC to yield the cyclopropyl-THF ring system in aspoquinolone
CC (PubMed:30026518). {ECO:0000250|UniProtKB:A0A1B2CTB2,
CC ECO:0000250|UniProtKB:A0A1B2CTB7, ECO:0000269|PubMed:25251934,
CC ECO:0000269|PubMed:26553478, ECO:0000269|PubMed:28114276,
CC ECO:0000269|PubMed:30026518, ECO:0000305|PubMed:30026518}.
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:30026518}.
CC -!- PATHWAY: Alkaloid biosynthesis. {ECO:0000269|PubMed:30026518}.
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:30026518}.
CC -!- SIMILARITY: Belongs to the quinolone epoxide rearrangement protein penF
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CBF82277.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EAA61519.1; Type=Erroneous gene model prediction; Note=The predicted gene AN9228 has been split into 2 genes: asqI and asqO.; Evidence={ECO:0000269|PubMed:28114276};
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DR EMBL; AACD01000170; EAA61519.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BN001306; CBF82277.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_682497.1; XM_677405.1.
DR EnsemblFungi; CBF82277; CBF82277; ANIA_11201.
DR GeneID; 2868027; -.
DR VEuPathDB; FungiDB:AN11201; -.
DR eggNOG; ENOG502SMYB; Eukaryota.
DR HOGENOM; CLU_051719_1_0_1; -.
DR InParanoid; P9WEP9; -.
DR OMA; PPHYPCS; -.
DR OrthoDB; 1068172at2759; -.
DR Proteomes; UP000000560; Chromosome VI.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Copper; Metal-binding; Monooxygenase; Oxidoreductase; Reference proteome.
FT CHAIN 1..365
FT /note="Quinolone epoxide rearrangement protein asqO"
FT /id="PRO_0000455385"
SQ SEQUENCE 365 AA; 39964 MW; C3C72E94B45D6E2A CRC64;
MQIVYLFSSV LLTAALAHEN GKVAYPFRLF NGTSSVEEIS QQDQMDAPKI MPHVNATTFE
WWYFDAVSTT SQNESLTVMF ENMGPEGLGA PYPGGPLAVQ ISGSFSNGTA FTIITAATKG
AVLEWGGGGV RGEWRGAGSS FAGKDHREYT VSIANPGIGV YGTMTLRSVS PPRYPCDVKE
RRASEQLIPN MYLANSQPDA IVEVDFNINE STLKFSGIGY HDLSWGSAPL ESSVHSWYWG
HGRLGRYSLV WFDVMGRDGK EYFSAWITEA GNVILCGCEP DSVLVRPWGE NSGFPPGRGT
PAPSGYSLRY DLGQNQIFIA NFTREVNIID NDFTKHIIGL FSGGFEGGEQ YEGRAMADQF
QFGDL
