ALNB_EMENI
ID ALNB_EMENI Reviewed; 284 AA.
AC C8VJR6;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 1.
DT 03-AUG-2022, entry version 52.
DE RecName: Full=Esterase alnB {ECO:0000303|PubMed:30339758};
DE EC=3.1.2.- {ECO:0000305|PubMed:30339758};
DE AltName: Full=Asperlin biosynthesis cluster protein B {ECO:0000303|PubMed:30339758};
GN Name=alnB {ECO:0000303|PubMed:30339758}; ORFNames=ANIA_11199;
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 BIOTECHNOLOGY.
RX PubMed=21762468; DOI=10.1111/j.1755-148x.2011.00887.x;
RA Flori E., Mastrofrancesco A., Kovacs D., Ramot Y., Briganti S., Bellei B.,
RA Paus R., Picardo M.;
RT "2,4,6-Octatrienoic acid is a novel promoter of melanogenesis and
RT antioxidant defence in normal human melanocytes via PPAR-gamma
RT activation.";
RL Pigment Cell Melanoma Res. 24:618-630(2011).
RN [4]
RP IDENTIFICATION, DISRUPTION PHENOTYPE, FUNCTION, INDUCTION, AND PATHWAY.
RX PubMed=30339758; DOI=10.1021/acschembio.8b00679;
RA Grau M.F., Entwistle R., Chiang Y.M., Ahuja M., Oakley C.E., Akashi T.,
RA Wang C.C.C., Todd R.B., Oakley B.R.;
RT "Hybrid transcription factor engineering activates the silent secondary
RT metabolite gene cluster for (+)-asperlin in Aspergillus nidulans.";
RL ACS Chem. Biol. 13:3193-3205(2018).
CC -!- FUNCTION: Esterase; part of the gene cluster that mediates the
CC biosynthesis of asperlin, a polyketide showing anti-inflammatory,
CC antitumor and antibiotic activities (PubMed:30339758). The first step
CC of the asperlin biosynthesis is the production of the intermediate
CC 2,4,6-octatrienoic acid by the highly redusing polyketide synthase alnA
CC with cleavage of the PKS product by the esterase alnB
CC (PubMed:30339758). 2,4,6-octatrienoic acid is further converted to
CC asperlin via several steps involving the remaining enzymes from the
CC cluster (PubMed:30339758). {ECO:0000269|PubMed:30339758}.
CC -!- PATHWAY: Polyketide biosynthesis. {ECO:0000269|PubMed:30339758}.
CC -!- INDUCTION: Expression is controlled by the asperlin biosynthesis
CC cluster-specific transcription factor alnR.
CC {ECO:0000269|PubMed:30339758}.
CC -!- DISRUPTION PHENOTYPE: Fully eliminates the production of asperlin.
CC {ECO:0000269|PubMed:30339758}.
CC -!- BIOTECHNOLOGY: 2,4,6-octatrienoic acid is a particularly interesting
CC compound because of its potential as a natural tanning agent for human
CC skin. It is a promoter of melanogenesis and antioxidant defense in
CC melanocytes in vitro and in vivo, topically and systemically.
CC Pigmentation is a powerful protectant from UV damage and skin cancer,
CC and octatrienoic acid is an attractive natural photoprotectant.
CC {ECO:0000269|PubMed:21762468}.
CC -!- SIMILARITY: Belongs to the LovG family. {ECO:0000305}.
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DR EMBL; BN001306; CBF82302.1; -; Genomic_DNA.
DR AlphaFoldDB; C8VJR6; -.
DR EnsemblFungi; CBF82302; CBF82302; ANIA_11199.
DR VEuPathDB; FungiDB:AN11199; -.
DR eggNOG; KOG2551; Eukaryota.
DR HOGENOM; CLU_051938_4_1_1; -.
DR InParanoid; C8VJR6; -.
DR OMA; MLSAVEW; -.
DR OrthoDB; 1190789at2759; -.
DR Proteomes; UP000000560; Chromosome VI.
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 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 1: Evidence at protein level;
KW Hydrolase; Reference proteome.
FT CHAIN 1..284
FT /note="Esterase alnB"
FT /id="PRO_0000445940"
FT ACT_SITE 93
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P38777"
FT ACT_SITE 226
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P38777"
FT ACT_SITE 255
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P38777"
SQ SEQUENCE 284 AA; 31017 MW; 0C592649A4D1F203 CRC64;
MPKILCLHGY GTSASILQHQ LGPFMAAADP SYEFVFLEGE IECQKAQGLG PFVKGPFLCY
NESFAPADIQ ESCDLIDEMI QAAGPFDGII GFSQGGSVAL SYLLQRQIDG HPPPFRWAVF
FSTVIAFAPN DTFGSNILAN LTDHEIRLLD GYPATDLSSL HPLTRALCET TAQTFYSAKT
GGFISPNTPI AEFSKRDDPS QPRVFHPALL GDRIPIPTVH ITGRKDNSLM VGLSVLVQGL
CDQRLIRSLT HSGGHNVPRS ADDVRAAWAA VDWAIQHSQK QHIW
