DBAE_EMENI
ID DBAE_EMENI Reviewed; 278 AA.
AC Q5AUY1; A0A1U8QKJ2; C8V4J9;
DT 13-FEB-2019, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Esterase dbaE {ECO:0000303|PubMed:23001671};
DE EC=3.1.2.- {ECO:0000305|PubMed:23001671};
DE AltName: Full=Derivative of benzaldehyde biosynthesis cluster protein E {ECO:0000303|PubMed:23001671};
GN Name=dbaE {ECO:0000303|PubMed:23001671}; ORFNames=ANIA_07899;
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: Esterase; part of the gene cluster that mediates the
CC biosynthesis of the antibiotic 2,4-dihydroxy-3-methyl-6-(2-
CC 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 -!- 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: Reduces the amounts of DHMDA produced.
CC {ECO:0000269|PubMed:23001671}.
CC -!- SIMILARITY: Belongs to the LovG family. {ECO:0000305}.
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DR EMBL; AACD01000135; EAA59553.1; -; Genomic_DNA.
DR EMBL; BN001302; CBF73486.1; -; Genomic_DNA.
DR RefSeq; XP_681168.1; XM_676076.1.
DR AlphaFoldDB; Q5AUY1; -.
DR SMR; Q5AUY1; -.
DR STRING; 162425.CADANIAP00003918; -.
DR EnsemblFungi; CBF73486; CBF73486; ANIA_07899.
DR EnsemblFungi; EAA59553; EAA59553; AN7899.2.
DR GeneID; 2869190; -.
DR KEGG; ani:AN7899.2; -.
DR VEuPathDB; FungiDB:AN7899; -.
DR eggNOG; KOG2551; Eukaryota.
DR HOGENOM; CLU_051938_0_2_1; -.
DR InParanoid; Q5AUY1; -.
DR OMA; HDYCEPS; -.
DR OrthoDB; 1190789at2759; -.
DR Proteomes; UP000000560; Chromosome II.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016787; F:hydrolase activity; IBA:GO_Central.
DR GO; GO:0019748; P:secondary metabolic process; IBA:GO_Central.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEP:AspGD.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR005645; FSH_dom.
DR Pfam; PF03959; FSH1; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Reference proteome.
FT CHAIN 1..278
FT /note="Esterase dbaE"
FT /id="PRO_0000446359"
FT ACT_SITE 124
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P38777"
FT ACT_SITE 220
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P38777"
FT ACT_SITE 248
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P38777"
SQ SEQUENCE 278 AA; 30793 MW; 2417367FDF3EAAA5 CRC64;
MTIRIPSGEE ADYTLHLPRI LCLHGGGTNA RIFRMQCRVL ERFLRSTFRF VYAEAPFAAQ
PGSDVTSVYK DHGPFKAWLR CTAADPDRSA QEVVKKINLS IATAMYDDDM RGATGEWIAL
LGFSQGAKVA ASILYAQQTI QQRLGERAAT RPRFRFAVLM AGRGPLVWLL PETSSGPGSI
PMGLVDAASP SMLDSEPELP TDSTEHMLRL PTLHVHGLRD PGLSLHRRLL RSYCQSDSVS
LVEWEGEHRV PLKTKDVTAV VDQIYALARD TGVLDSWC
