DBAF_EMENI
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 25-MAY-2022, entry version 112.
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 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 IDENTIFICATION, INDUCTION, FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RX PubMed=23001671; DOI=10.1128/aem.01808-12;
RA Gerke J., Bayram O., Feussner K., Landesfeind M., Shelest E., Feussner I.,
RA Braus G.H.;
RT "Breaking the silence: protein stabilization uncovers silenced biosynthetic
RT 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 Aspergillus
RT 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 profile
RT caused by the absence of the Aspergillus nidulans transcription factor
RT FlbB.";
RL Genetics 199:1127-1142(2015).
CC -!- FUNCTION: FAD-dependent oxidoreductase; part of the gene cluster that
CC mediates the biosynthesis of the antibiotic 2,4-dihydroxy-3-methyl-6-
CC (2-oxopropyl)benzaldehyde (DHMBA) and its derivatives (PubMed:22510154,
CC PubMed:23001671). The direct non-reducing polyketide synthase dbaI
CC product is 2,4-dihydroxy-3-methyl-6-(2-oxopropyl)benzaldehyde (DHMBA),
CC produced by condensation of one acetyl-CoA starter unit with 4 malonyl-
CC CoA units and one methylation step (PubMed:22510154). The FAD-dependent
CC monooxygenase dbaH is responsible for the synthesis of yellow pigments
CC derived from the oxidation of DHMBA (PubMed:23001671). The roles of
CC dbaB, C, E and F have still to be determined (Probable).
CC {ECO:0000269|PubMed:22510154, ECO:0000269|PubMed:23001671,
CC 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 cluster
CC (PubMed:23001671). Expression is positively regulated by the dba
CC cluster specific transcription factors dbaA and dbaG (PubMed:23001671).
CC Expression is also controlled by the transcription factor flbB
CC (PubMed:25701285). {ECO:0000269|PubMed:23001671,
CC 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 family.
CC {ECO:0000305}.
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DR EMBL; AACD01000135; EAA59554.1; -; Genomic_DNA.
DR EMBL; BN001302; CBF73488.1; -; Genomic_DNA.
DR RefSeq; XP_681169.1; XM_676077.1.
DR AlphaFoldDB; Q5AUY0; -.
DR SMR; Q5AUY0; -.
DR EnsemblFungi; CBF73488; CBF73488; ANIA_07900.
DR EnsemblFungi; EAA59554; EAA59554; AN7900.2.
DR GeneID; 2869100; -.
DR KEGG; ani:AN7900.2; -.
DR eggNOG; ENOG502SMFE; Eukaryota.
DR HOGENOM; CLU_028280_0_0_1; -.
DR InParanoid; Q5AUY0; -.
DR OMA; GSSQVWN; -.
DR OrthoDB; 569857at2759; -.
DR Proteomes; UP000000560; Chromosome II.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0046592; F:polyamine oxidase 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 FAD; Flavoprotein; Glycoprotein; Oxidoreductase; Reference proteome;
KW Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..467
FT /note="FAD-dependent oxidoreductase dbaF"
FT /evidence="ECO:0000255"
FT /id="PRO_5010288538"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 337
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 391
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 451
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="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
