ASQH2_EMENI
ID ASQH2_EMENI Reviewed; 421 AA.
AC C8VJQ0; Q5AR51;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Prenyltransferase asqH2 {ECO:0000305|PubMed:25251934};
DE EC=2.5.1.- {ECO:0000305|PubMed:25251934};
DE AltName: Full=4'-methoxyviridicatin/aspoquinolone biosynthesis cluster protein asqH2 {ECO:0000305|PubMed:25251934};
DE AltName: Full=Aspoquinolone biosynthesis protein H2 {ECO:0000305|PubMed:25251934};
GN Name=asqH2 {ECO:0000305|PubMed:25251934}; ORFNames=AN9229, ANIA_11202;
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=25251934; DOI=10.1002/anie.201407920;
RA Ishikawa N., Tanaka H., Koyama F., Noguchi H., Wang C.C., Hotta K.,
RA Watanabe K.;
RT "Non-heme dioxygenase catalyzes atypical oxidations of 6,7-bicyclic systems
RT to form the 6,6-quinolone core of viridicatin-type fungal alkaloids.";
RL Angew. Chem. Int. Ed. 53:12880-12884(2014).
RN [4]
RP FUNCTION.
RX PubMed=26553478; DOI=10.1002/anie.201507835;
RA Brauer A., Beck P., Hintermann L., Groll M.;
RT "Structure of the dioxygenase AsqJ: mechanistic insights into a one-pot
RT multistep quinolone antibiotic biosynthesis.";
RL Angew. Chem. Int. Ed. 55:422-426(2016).
RN [5]
RP FUNCTION.
RX PubMed=28114276; DOI=10.1038/nchembio.2283;
RA Zou Y., Garcia-Borras M., Tang M.C., Hirayama Y., Li D.H., Li L.,
RA Watanabe K., Houk K.N., Tang Y.;
RT "Enzyme-catalyzed cationic epoxide rearrangements in quinolone alkaloid
RT biosynthesis.";
RL Nat. Chem. Biol. 13:325-332(2017).
RN [6]
RP FUNCTION.
RX PubMed=30026518; DOI=10.1038/s41467-018-05221-5;
RA Kishimoto S., Hara K., Hashimoto H., Hirayama Y., Champagne P.A.,
RA Houk K.N., Tang Y., Watanabe K.;
RT "Enzymatic one-step ring contraction for quinolone biosynthesis.";
RL Nat. Commun. 9:2826-2826(2018).
CC -!- FUNCTION: Prenyltransferase; part of the gene cluster that mediates the
CC biosynthesis of the aspoquinolone mycotoxins (PubMed:25251934). The
CC first stage is catalyzed by the nonribosomal pepdide synthetase asqK
CC that condenses anthranilic acid and O-methyl-L-tyrosine to produce 4'-
CC methoxycyclopeptin (PubMed:25251934). AsqK is also able to use
CC anthranilic acid and L-phenylalanine as substrates to produce
CC cyclopeptin, but at a tenfold lower rate (PubMed:25251934). 4'-
CC methoxycyclopeptin is then converted to 4'-methoxydehydrocyclopeptin by
CC the ketoglutarate-dependent dioxygenase asqJ through dehydrogenation to
CC form a double bond between C-alpha and C-beta of the O-methyltyrosine
CC side chain (PubMed:25251934, PubMed:26553478). AsqJ also converts its
CC first product 4'-methoxydehydrocyclopeptin to 4'-methoxycyclopenin
CC (PubMed:25251934). AsqJ is a very unique dioxygenase which is capable
CC of catalyzing radical-mediated dehydrogenation and epoxidation
CC reactions sequentially on a 6,7-benzo-diazepinedione substrate in the
CC 4'-methoxyviridicatin biosynthetic pathway (PubMed:25251934). AsqJ is
CC also capable of converting cyclopeptin into dehydrocyclopeptin
CC (PubMed:25251934). The following conversion of 4'-methoxycyclopenin
CC into 4'-methoxyviridicatin is catalyzed by the cyclopenase asqI
CC (PubMed:30026518). Cyclopenin can also be converted into viridicatin by
CC asqI (PubMed:30026518). 4'-methoxyviridicatin is the precursor of
CC quinolone natural products, and is further converted to quinolinone B
CC (Probable). The prenyltransferase asqH1 then catalyzes the canonical
CC Friedel-Crafts alkylation of quinolinone B with dimethylallyl cation to
CC yield dimethylallyl quinolone, which is subjected to FAD-dependent
CC dehydrogenation by the FAD-linked oxidoreductase asqF to yield
CC conjugated aryl diene (By similarity). The delta(3') double bond then
CC serves as the site of the second alkylation with DMAPP catalyzed by the
CC prenyltransferase asqH2 to yield a carbenium ion intermediate, which
CC can be attacked by H(2)O to yield a styrenyl quinolone containing a
CC C3'-hydroxyprenyl chain (By similarity). The FAD-dependent
CC monooxygenase asqG performs epoxidation of the terminal C7'-C8' olefin
CC (PubMed:30026518). Finally, after dehydratation of the epoxide at C3 by
CC asqC, the quinolone epoxide rearrangement protein asqO catalyzes an
CC enzymatic 3-exo-tet cyclization to yield the cyclopropyl-THF ring
CC system in aspoquinolone (PubMed:30026518).
CC {ECO:0000250|UniProtKB:A0A1B2CTB2, ECO:0000250|UniProtKB:A0A1B2CTB7,
CC ECO:0000269|PubMed:25251934, ECO:0000269|PubMed:26553478,
CC ECO:0000269|PubMed:30026518, ECO:0000305|PubMed:30026518}.
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000305|PubMed:25251934}.
CC -!- PATHWAY: Alkaloid biosynthesis. {ECO:0000305|PubMed:25251934}.
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000305|PubMed:25251934}.
CC -!- SIMILARITY: Belongs to the tryptophan dimethylallyltransferase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAA61520.1; Type=Erroneous gene model prediction; Note=The predicted gene AN9229 has been split into 2 genes: ANIA_11194 and ANIA_1120.; Evidence={ECO:0000305};
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DR EMBL; AACD01000170; EAA61520.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BN001306; CBF82274.1; -; Genomic_DNA.
DR RefSeq; XP_682498.1; XM_677406.1.
DR AlphaFoldDB; C8VJQ0; -.
DR SMR; C8VJQ0; -.
DR EnsemblFungi; CBF82274; CBF82274; ANIA_11202.
DR EnsemblFungi; EAA61520; EAA61520; AN9229.2.
DR GeneID; 2868058; -.
DR KEGG; ani:AN9229.2; -.
DR VEuPathDB; FungiDB:AN11202; -.
DR eggNOG; ENOG502S2XP; Eukaryota.
DR HOGENOM; CLU_037431_0_0_1; -.
DR InParanoid; C8VJQ0; -.
DR OMA; LFARNHI; -.
DR OrthoDB; 1531660at2759; -.
DR Proteomes; UP000000560; Chromosome VI.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0004659; F:prenyltransferase activity; IEA:UniProt.
DR GO; GO:0009820; P:alkaloid metabolic process; IEA:InterPro.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR CDD; cd13929; PT-DMATS_CymD; 1.
DR InterPro; IPR033964; Aro_prenylTrfase.
DR InterPro; IPR017795; Aro_prenylTrfase_DMATS.
DR Pfam; PF11991; Trp_DMAT; 1.
DR SFLD; SFLDS00036; Aromatic_Prenyltransferase; 1.
DR TIGRFAMs; TIGR03429; arom_pren_DMATS; 1.
PE 3: Inferred from homology;
KW Reference proteome; Transferase.
FT CHAIN 1..421
FT /note="Prenyltransferase asqH2"
FT /id="PRO_0000437622"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 105
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 119
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 272
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 274
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 276
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 341
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
SQ SEQUENCE 421 AA; 48505 MW; C7C036970BCC0DBB CRC64;
MDRNSFTAYG PATGAITESG EQENDHTKPH TWKTFAKYAC FESEAERQWW NDSGALIARF
LSLTNGDIDQ QYQCLLFVRQ VLIPALGPYP PVRRCCINTT EIGMELSLNF QGPGEPVFRV
SIDPVSRMTG TPMDPLNINT VNNMITRLAS MGIKGFDRTL HHHFTREFCM SEQSMQSYQR
DSGEAIAWSQ TILAFDFKGG DVVTKQYIWT RHAARASGLH PHSLIRRAIS RVENQMHCSA
AVELVLEYME TFNADIPVPF FSWDLVDPTQ SRFKIYGISW QWSWAKAEEV CTLGGKLNHH
DIDLLKKLWH ILKLDEFTPT MGFTWNYEIR PGQPKPEVRL YLAICDRSDE EVAQAVVQWF
ELLGWHERAQ SYPETLRYLH KTKSAHTWLS VTVSEKGVYT SLYYHPLGNG SDDFKIRENW
F