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 02-NOV-2016, entry version 71. 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 OS 194 / M139) (Aspergillus nidulans). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus. 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., RA Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., RA Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., RA Purcell S., Harris S., Braus G.H., Draht O., Busch S., D'Enfert C., RA Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., RA Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., RA Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., RA Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., RA 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., RA von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., RA Fekete E., Flipphi M., Estrada C.G., Geysens S., Goldman G., RA de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., RA Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., RA Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., RA Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., RA Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., RA Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., RA Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., RA Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., RA van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., RA Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., RA de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., RA Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.; RT "The 2008 update of the Aspergillus nidulans genome annotation: a RT community 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 RT systems to form the 6,6-quinolone core of viridicatin-type fungal RT alkaloids."; RL Angew. Chem. Int. Ed. 53:12880-12884(2014). CC -!- FUNCTION: FAD-dependent monooxygenase; part of the gene cluster CC that mediates the biosynthesis of the aspoquinolone mycotoxins CC (PubMed:25251934). The first stage is catalyzed by the CC nonribosomal pepdide synthetase asqK that condenses anthranilic CC acid and O-methyl-L-tyrosine to produce 4'-methoxycyclopeptin CC (PubMed:25251934). AsqK is also able to use anthranilic acid and CC L-phenylalanine as substrates to produce cyclopeptin, but at a CC tenfold lower rate (PubMed:25251934). 4'-methoxycyclopeptin is CC then converted to 4'-methoxydehydrocyclopeptin by the CC ketoglutarate-dependent dioxygenase asqJ through dehydrogenation CC to form a double bond between C-alpha and C-beta of the O- CC methyltyrosine side chain (PubMed:25251934). AsqJ also converts CC its first product 4'-methoxydehydrocyclopeptin to 4'- CC methoxycyclopenin (PubMed:25251934). AsqJ is a very unique CC dioxygenase which is capable of catalyzing radical-mediated CC dehydrogenation and epoxidation reactions sequentially on a 6,7- CC benzo-diazepinedione substrate in the 4'-methoxyviridicatin CC biosynthetic pathway (PubMed:25251934). The following conversion CC of 4'-methoxycyclopenin into 4'-methoxyviridicatin proceeds non- CC enzymatically (PubMed:25251934). AsqJ is also capable of CC converting cyclopeptin into dehydrocyclopeptin and cyclopenin in a CC sequential fashion (PubMed:25251934). Cyclopenin can be converted CC into viridicatin non-enzymatically (PubMed:25251934). 4'- CC methoxyviridicatin likely acts as a precursor of quinolone natural CC products, such as aspoquinolones, peniprequinolones, CC penigequinolones, and yaequinolones (PubMed:25251934). Further CC characterization of the remaining genes in the cluster has still CC to be done to determine the exact identity of quinolone products CC this cluster is responsible for biosynthesizing (PubMed:25251934). CC {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 CC family. {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 ProteinModelPortal; Q5AR50; -. DR EnsemblFungi; CADANIAT00009360; CADANIAP00009360; CADANIAG00009360. DR EnsemblFungi; EAA61521; EAA61521; AN9230.2. DR GeneID; 2868012; -. DR KEGG; ani:AN9230.2; -. DR HOGENOM; HOG000201495; -. DR OMA; RELEWAG; -. DR OrthoDB; EOG092C0LJ1; -. DR Proteomes; UP000000560; Chromosome VI. DR Proteomes; UP000005890; Partially assembled 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; IBA:GO_Central. DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IBA:GO_Central. DR Gene3D; 3.50.50.60; -; 3. DR InterPro; IPR002938; FAD-bd. DR InterPro; IPR023753; FAD/NAD-binding_dom. DR Pfam; PF01494; FAD_binding_3; 1. DR SUPFAM; SSF51905; SSF51905; 2. PE 3: Inferred from homology; KW Complete proteome; FAD; Flavoprotein; Membrane; Monooxygenase; KW Oxidoreductase; Reference proteome; Signal; Transmembrane; KW Transmembrane helix. FT SIGNAL 1 19 {ECO:0000255}. FT CHAIN 20 566 FAD-dependent monooxygenase asqG. FT /FTId=PRO_0000437618. FT TRANSMEM 448 468 Helical. {ECO:0000255}. FT TRANSMEM 482 502 Helical. {ECO:0000255}. FT REGION 5 344 FAD-binding. {ECO:0000255}. 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 //