AUSN_EMENI
ID AUSN_EMENI Reviewed; 330 AA.
AC Q5AR21; C8VQ99;
DT 08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Polyprenyl transferase ausN {ECO:0000305|PubMed:22329759};
DE EC=2.5.1.- {ECO:0000305|PubMed:22329759};
DE AltName: Full=Austinoid biosynthesis clusters protein N {ECO:0000303|PubMed:22329759};
GN Name=ausN {ECO:0000303|PubMed:22329759}; ORFNames=AN9259;
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: Polyprenyl transferase; part of the gene cluster B that
CC mediates 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 -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate + 3,5-dimethylorsellinate = (3R)-
CC 3-farnesyl-6-hydroxy-2,3,5-trimethyl-4-oxocyclohexa-1,5-diene-1-
CC carboxylate + diphosphate + H(+); Xref=Rhea:RHEA:49632,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:131856,
CC ChEBI:CHEBI:131857, ChEBI:CHEBI:175763;
CC Evidence={ECO:0000305|PubMed:22329759};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49633;
CC Evidence={ECO:0000305|PubMed:22329759};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P32378};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000269|PubMed:22329759}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Impairs the synthesis of austinol and
CC dehydroaustinol and accumulates the intermediate compound 3,5-
CC dimethylorsellinic acid (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 UbiA prenyltransferase family.
CC {ECO:0000305}.
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DR EMBL; BN001308; CBF87269.1; -; Genomic_DNA.
DR EMBL; AACD01000172; EAA66326.1; -; Genomic_DNA.
DR RefSeq; XP_682528.1; XM_677436.1.
DR AlphaFoldDB; Q5AR21; -.
DR SMR; Q5AR21; -.
DR STRING; 162425.CADANIAP00001028; -.
DR EnsemblFungi; CBF87269; CBF87269; ANIA_09259.
DR EnsemblFungi; EAA66326; EAA66326; AN9259.2.
DR GeneID; 2867775; -.
DR KEGG; ani:AN9259.2; -.
DR VEuPathDB; FungiDB:AN9259; -.
DR eggNOG; KOG1381; Eukaryota.
DR HOGENOM; CLU_034879_2_0_1; -.
DR InParanoid; Q5AR21; -.
DR OMA; QVARCRV; -.
DR OrthoDB; 1343847at2759; -.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000000560; Chromosome VIII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0008412; F:4-hydroxybenzoate octaprenyltransferase activity; IBA:GO_Central.
DR GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IBA:GO_Central.
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 GO; GO:0006744; P:ubiquinone biosynthetic process; IBA:GO_Central.
DR CDD; cd13959; PT_UbiA_COQ2; 1.
DR Gene3D; 1.10.357.140; -; 1.
DR InterPro; IPR039653; Prenyltransferase.
DR InterPro; IPR000537; UbiA_prenyltransferase.
DR InterPro; IPR044878; UbiA_sf.
DR PANTHER; PTHR11048; PTHR11048; 1.
DR Pfam; PF01040; UbiA; 1.
PE 3: Inferred from homology;
KW Magnesium; Membrane; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..330
FT /note="Polyprenyl transferase ausN"
FT /id="PRO_0000436495"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 189..209
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 260..280
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 330 AA; 36545 MW; 54C9AD015766900B CRC64;
MAVISELKRH HPKTGLLRYL PTGVVPYGEL VRIHRALGYY LNTSPYVVGI AYTAATAETK
LPLDLLLDRL LLLTLWSLIL RSAGCAWNDL VDVDIDRQIS RTQSRPLPRG AISLSAATIF
TACLFVLGCS LLLFLPRECL FDAGIKVFFA LLYPFGKRFT DHPQLILINI AWAIPMAMHS
LGMEPSSQIL SMLCMCVFFS AVIVMIDLVY SRQDTEEDLK VGVKSMAVRY RNCVETMAYS
LFAISSLALL FGGVLGGLRV PFVLFSVGGH IVGFWRFLRA SLQAGPAGVE SRAKSSCLIA
SVFWVLGLGI EYAEMVKEKD NPTDKKKHPH
