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AUSK_EMENI
ID   AUSK_EMENI              Reviewed;         398 AA.
AC   C8VQ93;
DT   08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT   03-NOV-2009, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Aldo-keto reductase ausK {ECO:0000305};
DE            EC=1.1.1.- {ECO:0000305};
DE   AltName: Full=Austinoid biosynthesis clusters protein K {ECO:0000303|PubMed:22329759};
GN   Name=ausK {ECO:0000303|PubMed:22329759}; ORFNames=ANIA_11205;
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   FUNCTION.
RX   PubMed=22234162; DOI=10.1021/cb200455u;
RA   Rodriguez-Urra A.B., Jimenez C., Nieto M.I., Rodriguez J., Hayashi H.,
RA   Ugalde U.;
RT   "Signaling the induction of sporulation involves the interaction of two
RT   secondary metabolites in Aspergillus nidulans.";
RL   ACS Chem. Biol. 7:599-606(2012).
RN   [4]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=22329759; DOI=10.1021/ja209809t;
RA   Lo H.C., Entwistle R., Guo C.J., Ahuja M., Szewczyk E., Hung J.H.,
RA   Chiang Y.M., Oakley B.R., Wang C.C.;
RT   "Two separate gene clusters encode the biosynthetic pathway for the
RT   meroterpenoids austinol and dehydroaustinol in Aspergillus nidulans.";
RL   J. Am. Chem. Soc. 134:4709-4720(2012).
RN   [5]
RP   FUNCTION.
RX   PubMed=23865690; DOI=10.1021/ja405518u;
RA   Matsuda Y., Awakawa T., Wakimoto T., Abe I.;
RT   "Spiro-ring formation is catalyzed by a multifunctional dioxygenase in
RT   austinol biosynthesis.";
RL   J. Am. Chem. Soc. 135:10962-10965(2013).
RN   [6]
RP   FUNCTION.
RX   PubMed=29076725; DOI=10.1021/acschembio.7b00814;
RA   Mattern D.J., Valiante V., Horn F., Petzke L., Brakhage A.A.;
RT   "Rewiring of the austinoid biosynthetic pathway in filamentous fungi.";
RL   ACS Chem. Biol. 12:2927-2933(2017).
CC   -!- FUNCTION: Aldo-keto reductase; part of the gene cluster B that mediates
CC       the biosynthesis of austinol and dehydroaustinol, two fungal
CC       meroterpenoids (PubMed:22329759). The first step of the pathway is the
CC       synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase
CC       ausA (PubMed:22329759). 3,5-dimethylorsellinic acid is then prenylated
CC       by the polyprenyl transferase ausN (PubMed:22329759). Further
CC       epoxidation by the FAD-dependent monooxygenase ausM and cyclization by
CC       the probable terpene cyclase ausL lead to the formation of
CC       protoaustinoid A (PubMed:22329759). Protoaustinoid A is then oxidized
CC       to spiro-lactone preaustinoid A3 by the combined action of the FAD-
CC       binding monooxygenases ausB and ausC, and the dioxygenase ausE
CC       (PubMed:22329759, PubMed:23865690). Acid-catalyzed keto-rearrangement
CC       and ring contraction of the tetraketide portion of preaustinoid A3 by
CC       ausJ lead to the formation of preaustinoid A4 (PubMed:22329759). The
CC       aldo-keto reductase ausK, with the help of ausH, is involved in the
CC       next step by transforming preaustinoid A4 into isoaustinone which is in
CC       turn hydroxylated by the P450 monooxygenase ausI to form austinolide
CC       (PubMed:22329759). Finally, the cytochrome P450 monooxygenase ausG
CC       modifies austinolide to austinol (PubMed:22329759). Austinol can be
CC       further modified to dehydroaustinol which forms a diffusible complex
CC       with diorcinol that initiates conidiation (PubMed:22234162,
CC       PubMed:22329759). Due to genetic rearrangements of the clusters and the
CC       subsequent loss of some enzymes, the end products of the Emericella
CC       nidulans austinoid biosynthesis clusters are austinol and
CC       dehydroaustinol, even if additional enzymes, such as the O-
CC       acetyltransferase ausQ and the cytochrome P450 monooxygenase ausR are
CC       still functional (PubMed:29076725). {ECO:0000269|PubMed:22234162,
CC       ECO:0000269|PubMed:22329759, ECO:0000269|PubMed:23865690,
CC       ECO:0000269|PubMed:29076725}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC       {ECO:0000269|PubMed:22329759}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q8CG76}.
CC   -!- DISRUPTION PHENOTYPE: Impairs the synthesis of austinol and
CC       dehydroaustinol and accumulates the intermediate compounds preaustinoid
CC       A4, preaustinoid A5 and austinoneol A11 (PubMed:22329759).
CC       {ECO:0000269|PubMed:22329759}.
CC   -!- MISCELLANEOUS: In A.calidoustus, the austinoid gene cluster lies on a
CC       contiguous DNA region, while clusters from E.nidulans and P.brasilianum
CC       are split in their respective genomes. Genetic rearrangements provoked
CC       variability among the clusters and E.nidulans produces the least number
CC       of austionoid derivatives with the end products austinol and
CC       dehydroaustinol, while P.brasilianum can produce until
CC       acetoxydehydroaustin, and A.calidoustus produces the highest number of
CC       identified derivatives. {ECO:0000305|PubMed:29076725}.
CC   -!- SIMILARITY: Belongs to the aldo/keto reductase family. Aldo/keto
CC       reductase 2 subfamily. {ECO:0000305}.
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DR   EMBL; BN001308; CBF87258.1; -; Genomic_DNA.
DR   AlphaFoldDB; C8VQ93; -.
DR   SMR; C8VQ93; -.
DR   EnsemblFungi; CBF87258; CBF87258; ANIA_11205.
DR   VEuPathDB; FungiDB:AN11205; -.
DR   eggNOG; KOG1575; Eukaryota.
DR   HOGENOM; CLU_023205_2_2_1; -.
DR   InParanoid; C8VQ93; -.
DR   OMA; AWYFARA; -.
DR   OrthoDB; 706185at2759; -.
DR   UniPathway; UPA00213; -.
DR   Proteomes; UP000000560; Chromosome VIII.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:1900560; P:austinol biosynthetic process; IMP:AspGD.
DR   GO; GO:1900563; P:dehydroaustinol biosynthetic process; IMP:AspGD.
DR   GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.20.20.100; -; 1.
DR   InterPro; IPR023210; NADP_OxRdtase_dom.
DR   InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR   Pfam; PF00248; Aldo_ket_red; 1.
DR   SUPFAM; SSF51430; SSF51430; 1.
PE   3: Inferred from homology;
KW   NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..398
FT                   /note="Aldo-keto reductase ausK"
FT                   /id="PRO_0000436493"
FT   ACT_SITE        81
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q8CG76"
FT   BINDING         76
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:O43488"
FT   BINDING         156
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8CG76"
FT   BINDING         186..187
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:O43488"
FT   BINDING         212
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:O43488"
FT   BINDING         241..251
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:O43488"
FT   BINDING         317..325
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:O43488"
SQ   SEQUENCE   398 AA;  43714 MW;  C2A90F9A679C5CFB CRC64;
     MTGTRILELF GPAPEPPSEL GRYRILSPTA GIRVSPLQLG ALSIGDAWST DLGSMDKDSA
     MELLDAYAAA GGNFIDTANA YQNEQSEMWI GEWMASRGNR DKMVIATKFG TDYRAHELGK
     GLAVNYSGNH KRSLHMSVRD SLQKLRTSWI DILYLHTWDY TTSIPELMDS LHHLVQRGDV
     LYLGICNTPA WVVSAANTYA QQQGKTQFSV YQGRWNPLRR ELERDILPMA RHFGMAVTVY
     DALGSGKFQS RDMLARRKDQ GEGLRAIYGG QQTALEEAMS KALGVVAAQH GIESVTAVAL
     AYLLAKAPYV FPIIGGRKIQ HLHDNIEALS LRLSQEEIEY LESVGDFDPG FPYDMAGVDP
     ADTGIATPIV AQAAPMAFVQ RSKAIGYAES SKGSQMFG
 
 
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