ID ASQG_EMENI Reviewed; 566 AA. AC Q5AR50; C8VJP9; DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot. DT 26-APR-2005, sequence version 1. DT 23-FEB-2022, entry version 90. DE RecName: Full=FAD-dependent monooxygenase asqG {ECO:0000303|PubMed:25251934}; DE EC=1.-.-.- {ECO:0000305|PubMed:25251934}; DE AltName: Full=4'-methoxyviridicatin/aspoquinolone biosynthesis cluster protein asqG {ECO:0000305}; DE AltName: Full=Aspoquinolone biosynthesis protein G {ECO:0000303|PubMed:25251934}; DE Flags: Precursor; GN Name=asqG {ECO:0000303|PubMed:25251934}; ORFNames=AN9230; 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). CC -!- FUNCTION: FAD-dependent monooxygenase; part of the gene cluster that CC mediates the biosynthesis of the aspoquinolone mycotoxins CC (PubMed:25251934). The first stage is catalyzed by the nonribosomal CC pepdide synthetase asqK that condenses anthranilic acid and O-methyl-L- CC tyrosine to produce 4'-methoxycyclopeptin (PubMed:25251934). AsqK is CC also able to use anthranilic acid and L-phenylalanine as substrates to CC produce cyclopeptin, but at a tenfold lower rate (PubMed:25251934). 4'- CC methoxycyclopeptin is then converted to 4'-methoxydehydrocyclopeptin by CC the ketoglutarate-dependent dioxygenase asqJ through dehydrogenation to CC form a double bond between C-alpha and C-beta of the O-methyltyrosine CC side chain (PubMed:25251934). 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). The following conversion of 4'- CC methoxycyclopenin into 4'-methoxyviridicatin proceeds non-enzymatically CC (PubMed:25251934). AsqJ is also capable of converting cyclopeptin into CC dehydrocyclopeptin and cyclopenin in a sequential fashion CC (PubMed:25251934). Cyclopenin can be converted into viridicatin non- CC enzymatically (PubMed:25251934). 4'-methoxyviridicatin likely acts as a CC precursor of quinolone natural products, such as aspoquinolones, CC peniprequinolones, penigequinolones, and yaequinolones CC (PubMed:25251934). Further characterization of the remaining genes in CC the cluster has still to be done to determine the exact identity of CC quinolone products this cluster is responsible for biosynthesizing CC (PubMed:25251934). {ECO:0000269|PubMed:25251934}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305}; CC -!- PATHWAY: Secondary metabolite biosynthesis. CC {ECO:0000305|PubMed:25251934}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane CC protein {ECO:0000255}. CC -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BN001306; CBF82272.1; -; Genomic_DNA. DR EMBL; AACD01000170; EAA61521.1; -; Genomic_DNA. DR RefSeq; XP_682499.1; XM_677407.1. DR SMR; Q5AR50; -. DR STRING; 227321.Q5AR50; -. DR EnsemblFungi; CBF82272; CBF82272; ANIA_09230. DR EnsemblFungi; EAA61521; EAA61521; AN9230.2. DR GeneID; 2868012; -. DR KEGG; ani:AN9230.2; -. DR eggNOG; KOG2614; Eukaryota. DR HOGENOM; CLU_009665_12_2_1; -. DR InParanoid; Q5AR50; -. DR OMA; RELEWAG; -. DR OrthoDB; 462247at2759; -. DR Proteomes; UP000000560; Chromosome VI. DR Proteomes; UP000005890; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0071949; F:FAD binding; IEA:InterPro. DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW. DR Gene3D; 3.50.50.60; -; 1. DR InterPro; IPR002938; FAD-bd. DR InterPro; IPR036188; FAD/NAD-bd_sf. DR Pfam; PF01494; FAD_binding_3; 1. DR SUPFAM; SSF51905; SSF51905; 1. PE 3: Inferred from homology; KW FAD; Flavoprotein; Membrane; Monooxygenase; Oxidoreductase; KW Reference proteome; Signal; Transmembrane; Transmembrane helix. FT SIGNAL 1..19 FT /evidence="ECO:0000255" FT CHAIN 20..566 FT /note="FAD-dependent monooxygenase asqG" FT /id="PRO_0000437618" FT TRANSMEM 448..468 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 482..502 FT /note="Helical" FT /evidence="ECO:0000255" FT NP_BIND 34..35 FT /note="FAD" FT /evidence="ECO:0000250|UniProtKB:A6T923" FT NP_BIND 323..327 FT /note="FAD" FT /evidence="ECO:0000250|UniProtKB:A6T923" FT BINDING 313 FT /note="FAD" FT /evidence="ECO:0000250|UniProtKB:A6T923" SQ SEQUENCE 566 AA; 61875 MW; D2B220D263CC2D82 CRC64; MAAFTVIIIG GSISGLTLAN VLEKYGIKYI LLEKRPSIGP QLGATVVVHP SGLHLLSQLG LRERVEELAT PVELQKAIGP DGTFVLNIAA TNQCDRTIAD ALSTGYMPMF IARQDLIKVL YDNLQDKFRV HASLGLRELE WAGDKVKVTT TDGTSVVGDI VVGADGANSR TRAEIWKIAD VEDPSYGSQQ LAKSIACTYR CVFGMVDDGD SSLARTAYLA FQYNRAYTYL PTDSGRAYFL AFFKNPAKTV NDAIPRYSDQ DEDADVAAHA NDIIVPGLTF GDLYKRRTRC TLVPLQEYLL DKCFYKRVVL IGDAVHKLNP ITGRGANLAI EGAALLGDLI KHALEKSLQP TDEMLQTAFF TYQQCTKSRA PSQIDDAHRV QSLAALENPL LKFMSLKLLK RATADKLALG VAVDFSTGHS MRYLPQLPQR GMVPLNKDVV ANPEHRPASS TVLWIILMLG MASLGAVWQK HQRAEEDQPI HGYTLLTLST FYNLMILFAS AVHGSLGRRA VNLSFSDDSG MVPFYAVGHA PDKYRPTTPS RRVGLLVPGP SYLGSGGHFN GLLEVA //