DBAB_EMENI
ID DBAB_EMENI Reviewed; 393 AA.
AC Q5AUY3; A0A1U8QLN1; C8V4J6;
DT 13-FEB-2019, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=FAD-dependent monooxygenase dbaB {ECO:0000303|PubMed:23001671};
DE EC=1.-.-.- {ECO:0000305|PubMed:23001671};
DE AltName: Full=Derivative of benzaldehyde biosynthesis cluster protein B {ECO:0000303|PubMed:23001671};
DE Flags: Precursor;
GN Name=dbaB {ECO:0000303|PubMed:23001671}; ORFNames=ANIA_07897;
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 monooxygenase; 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:A6T923};
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 factor dbaA (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: Does not lead to any phenotypic changes.
CC {ECO:0000269|PubMed:23001671}.
CC -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC {ECO:0000305}.
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DR EMBL; BN001302; CBF73480.1; -; Genomic_DNA.
DR EMBL; AACD01000135; EAA59551.1; -; Genomic_DNA.
DR RefSeq; XP_681166.1; XM_676074.1.
DR AlphaFoldDB; Q5AUY3; -.
DR SMR; Q5AUY3; -.
DR STRING; 162425.CADANIAP00003915; -.
DR EnsemblFungi; CBF73480; CBF73480; ANIA_07897.
DR EnsemblFungi; EAA59551; EAA59551; AN7897.2.
DR GeneID; 2869255; -.
DR KEGG; ani:AN7897.2; -.
DR VEuPathDB; FungiDB:AN7897; -.
DR eggNOG; KOG2614; Eukaryota.
DR HOGENOM; CLU_009665_3_2_1; -.
DR InParanoid; Q5AUY3; -.
DR OMA; ASHAMTM; -.
DR OrthoDB; 1248412at2759; -.
DR Proteomes; UP000000560; Chromosome II.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEP:AspGD.
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 2: Evidence at transcript level;
KW FAD; Flavoprotein; Glycoprotein; Monooxygenase; Oxidoreductase;
KW Reference proteome; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..393
FT /note="FAD-dependent monooxygenase dbaB"
FT /evidence="ECO:0000255"
FT /id="PRO_5010288540"
FT BINDING 37..38
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 230..232
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 316..320
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 320
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 233
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 393 AA; 43163 MW; A20ED128566A0B91 CRC64;
MTRTSPTLPV IILGAGMVGL TLAQALKKAG IPYEVYERDS AADTEKGRGW ALTVHWALNA
LEECLPAELF NRLEEIQVDP TLDDSRRFCF LDLSTAIPKY VIPPSKRLRV NRRLLGNLLG
EGLDINYNKT LSSFHVSPET PDSVTVTFTD GTSTTGCLLV GTDGRNSKTR RLLLGEEAGA
LNPLPVRSIG TTITMTPEQF APIREIDPLL FQGSHPETGV YMWFSLVSSP TINGSKDTPN
PFYEGQLIQS WLYKSEKDAV PETDADRLAL FKNNAQHFQR RLREAIETLP EDSKVLHIKL
VDWVPVDWDN RGGRVTLAGD AAHAMTSYRG EAFNHGVADA AMLSRNIIAA WTNPGMTGGI
ADAPDSPIVS KRAKIAREAR DARARAKLSE IAV
