ID DBAF_EMENI Reviewed; 467 AA. AC Q5AUY0; A0A1U8QSV1; C8V4K0; DT 13-FEB-2019, integrated into UniProtKB/Swiss-Prot. DT 26-APR-2005, sequence version 1. DT 13-FEB-2019, entry version 102. DE RecName: Full=FAD-dependent oxidoreductase dbaF {ECO:0000303|PubMed:23001671}; DE EC=1.21.-.- {ECO:0000305|PubMed:23001671}; DE AltName: Full=Derivative of benzaldehyde biosynthesis cluster protein F {ECO:0000303|PubMed:23001671}; DE Flags: Precursor; GN Name=dbaF {ECO:0000303|PubMed:23001671}; ORFNames=ANIA_07900; 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 IDENTIFICATION, INDUCTION, FUNCTION, DISRUPTION PHENOTYPE, AND RP PATHWAY. RX PubMed=23001671; DOI=10.1128/AEM.01808-12; RA Gerke J., Bayram O., Feussner K., Landesfeind M., Shelest E., RA Feussner I., Braus G.H.; RT "Breaking the silence: protein stabilization uncovers silenced RT biosynthetic gene clusters in the fungus Aspergillus nidulans."; RL Appl. Environ. Microbiol. 78:8234-8244(2012). RN [4] RP FUNCTION. RX PubMed=22510154; DOI=10.1021/ja3016395; RA Ahuja M., Chiang Y.M., Chang S.L., Praseuth M.B., Entwistle R., RA Sanchez J.F., Lo H.C., Yeh H.H., Oakley B.R., Wang C.C.; RT "Illuminating the diversity of aromatic polyketide synthases in RT Aspergillus nidulans."; RL J. Am. Chem. Soc. 134:8212-8221(2012). RN [5] RP INDUCTION. RX PubMed=25701285; DOI=10.1534/genetics.115.174342; RA Oiartzabal-Arano E., Garzia A., Gorostidi A., Ugalde U., Espeso E.A., RA Etxebeste O.; RT "Beyond asexual development: modifications in the gene expression RT profile caused by the absence of the Aspergillus nidulans RT transcription factor FlbB."; RL Genetics 199:1127-1142(2015). CC -!- FUNCTION: FAD-dependent oxidoreductase; part of the gene cluster CC that mediates the biosynthesis of the antibiotic 2,4-dihydroxy-3- CC methyl-6-(2-oxopropyl)benzaldehyde (DHMBA) and its derivatives CC (PubMed:22510154, PubMed:23001671). The direct non-reducing CC polyketide synthase dbaI product is 2,4-dihydroxy-3-methyl-6-(2- CC oxopropyl)benzaldehyde (DHMBA), produced by condensation of one CC acetyl-CoA starter unit with 4 malonyl-CoA units and one CC methylation step (PubMed:22510154). The FAD-dependent CC monooxygenase dbaH is responsible for the synthesis of yellow CC pigments derived from the oxidation of DHMBA (PubMed:23001671). CC The roles of dbaB, C, E and F have still to be determined CC (Probable). {ECO:0000269|PubMed:22510154, CC ECO:0000269|PubMed:23001671, ECO:0000305|PubMed:23001671}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000250|UniProtKB:B8NI10}; CC -!- PATHWAY: Secondary metabolite biosynthesis. CC {ECO:0000305|PubMed:23001671}. CC -!- INDUCTION: Deletion of the conserved eukaryotic csnE deneddylase CC subunit of the COP9 signalosome leading to defect in protein CC degradation results in the activation of the silenced dba gene CC cluster (PubMed:23001671). Expression is positively regulated by CC the dba cluster specific transcription factors dbaA and dbaG CC (PubMed:23001671). Expression is also controlled by the CC transcription factor flbB (PubMed:25701285). CC {ECO:0000269|PubMed:23001671, ECO:0000269|PubMed:25701285}. CC -!- DISRUPTION PHENOTYPE: Reduces the amounts of DHMDA produced. CC {ECO:0000269|PubMed:23001671}. CC -!- SIMILARITY: Belongs to the beta-cyclopiazonate dehydrogenase 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; AACD01000135; EAA59554.1; -; Genomic_DNA. DR EMBL; BN001302; CBF73488.1; -; Genomic_DNA. DR RefSeq; XP_681169.1; XM_676077.1. DR EnsemblFungi; CBF73488; CBF73488; ANIA_07900. DR EnsemblFungi; EAA59554; EAA59554; AN7900.2. DR GeneID; 2869100; -. DR KEGG; ani:AN7900.2; -. DR HOGENOM; HOG000161810; -. DR OMA; RNTWYTG; -. DR OrthoDB; EOG092C281O; -. DR Proteomes; UP000000560; Chromosome II. DR Proteomes; UP000005890; Unassembled WGS sequence. DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central. DR Gene3D; 3.50.50.60; -; 1. DR InterPro; IPR036188; FAD/NAD-bd_sf. DR SUPFAM; SSF51905; SSF51905; 1. PE 2: Evidence at transcript level; KW Complete proteome; FAD; Flavoprotein; Glycoprotein; Oxidoreductase; KW Reference proteome; Signal. FT SIGNAL 1 20 {ECO:0000255}. FT CHAIN 21 467 FAD-dependent oxidoreductase dbaF. FT {ECO:0000255}. FT /FTId=PRO_5010288538. FT CARBOHYD 96 96 N-linked (GlcNAc...) asparagine. FT {ECO:0000255|PROSITE-ProRule:PRU00498}. FT CARBOHYD 134 134 N-linked (GlcNAc...) asparagine. FT {ECO:0000255|PROSITE-ProRule:PRU00498}. FT CARBOHYD 337 337 N-linked (GlcNAc...) asparagine. FT {ECO:0000255|PROSITE-ProRule:PRU00498}. FT CARBOHYD 391 391 N-linked (GlcNAc...) asparagine. FT {ECO:0000255|PROSITE-ProRule:PRU00498}. FT CARBOHYD 451 451 N-linked (GlcNAc...) asparagine. FT {ECO:0000255|PROSITE-ProRule:PRU00498}. SQ SEQUENCE 467 AA; 51478 MW; 33086CC663EDE630 CRC64; MKSVLASGAL TLAFSLAALA ADAFQASSWD STHIIRRDVV IVGGGAAGTY AAIRLKDHGK SVVLVERRDR LGGHAVTYKD PNTGGSVDYG VQVYDNNTVV RDFFSRLNTP LADLSFASFG KPVYADFEEG MLLNLTAGTL GQDYINELNK YPYLDNGFEL PDPVPEDLLL PWVEYIGKYN IDLSTAIATL ARPAVTGNLL NILAIYVFNN LNHLLLHEMS GAVVVNANRD NSQLYRNAVS ELQPDLLLRS RVVAGQRRTR KRDGVRLVVD TPTGRKLIIA KQLIVGMPPI LDNMRTFGLD SHEHSVLSHI YGLPYYGGVV SDTGLAPGFS FKNYAANTSY NLAEIPSVVA FNPSSVDGLF YYWYNAPQPV SQRRIETEAR DAIKTLQRLT NSTTQPEPKF LAFSDFAPYQ LRVSAEAIRN GFYDDMYGLQ GHRNTWYTGT LFVTGSSQVW NNTEVMLPEI LAAVNSS //