ASQJ_EMENI
ID ASQJ_EMENI Reviewed; 416 AA.
AC Q5AR53; C8VJQ4;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Iron/alpha-ketoglutarate-dependent dioxygenase asqJ {ECO:0000303|PubMed:25251934};
DE EC=1.14.-.- {ECO:0000269|PubMed:25251934, ECO:0000269|PubMed:26553478};
DE AltName: Full=4'-methoxyviridicatin/aspoquinolone biosynthesis cluster protein asqJ {ECO:0000305};
DE AltName: Full=Aspoquinolone biosynthesis protein J {ECO:0000303|PubMed:25251934};
GN Name=asqJ {ECO:0000303|PubMed:25251934}; ORFNames=AN9227;
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, AND CATALYTIC ACTIVITY.
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=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 [5]
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).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 110-416, FUNCTION, CATALYTIC
RP ACTIVITY, AND COFACTOR.
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).
CC -!- FUNCTION: Iron/alpha-ketoglutarate-dependent dioxygenase; part of the
CC gene cluster that mediates the biosynthesis of the aspoquinolone
CC mycotoxins (PubMed:25251934, PubMed:26553478). The first stage is
CC catalyzed by the nonribosomal pepdide synthetase asqK that condenses
CC 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 -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000269|PubMed:26553478};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:25251934, ECO:0000269|PubMed:26553478}.
CC -!- PATHWAY: Alkaloid biosynthesis. {ECO:0000269|PubMed:25251934,
CC ECO:0000269|PubMed:26553478}.
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:25251934,
CC ECO:0000269|PubMed:26553478}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q4WAW9}.
CC -!- SIMILARITY: Belongs to the PhyH family. {ECO:0000305}.
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DR EMBL; BN001306; CBF82281.1; -; Genomic_DNA.
DR EMBL; AACD01000170; EAA61518.1; -; Genomic_DNA.
DR RefSeq; XP_682496.1; XM_677404.1.
DR PDB; 5DAP; X-ray; 1.70 A; A=110-416.
DR PDB; 5DAQ; X-ray; 1.70 A; A=110-416.
DR PDB; 5DAV; X-ray; 1.80 A; A=110-416.
DR PDB; 5DAW; X-ray; 1.60 A; A=110-416.
DR PDB; 5DAX; X-ray; 1.70 A; A=110-416.
DR PDB; 5OA4; X-ray; 1.55 A; A=110-416.
DR PDB; 5OA7; X-ray; 1.65 A; A=110-416.
DR PDB; 5OA8; X-ray; 1.75 A; A=110-416.
DR PDB; 5Y7R; X-ray; 1.96 A; B=109-416.
DR PDB; 5Y7T; X-ray; 2.05 A; B=109-416.
DR PDB; 6EOZ; X-ray; 1.55 A; A=110-416.
DR PDB; 6JZM; X-ray; 1.88 A; B=109-416.
DR PDB; 6K0E; X-ray; 1.71 A; B=109-416.
DR PDB; 6K0F; X-ray; 1.63 A; B=109-416.
DR PDB; 6K30; X-ray; 2.68 A; B=109-416.
DR PDB; 6KD9; X-ray; 2.44 A; B/F=109-416.
DR PDBsum; 5DAP; -.
DR PDBsum; 5DAQ; -.
DR PDBsum; 5DAV; -.
DR PDBsum; 5DAW; -.
DR PDBsum; 5DAX; -.
DR PDBsum; 5OA4; -.
DR PDBsum; 5OA7; -.
DR PDBsum; 5OA8; -.
DR PDBsum; 5Y7R; -.
DR PDBsum; 5Y7T; -.
DR PDBsum; 6EOZ; -.
DR PDBsum; 6JZM; -.
DR PDBsum; 6K0E; -.
DR PDBsum; 6K0F; -.
DR PDBsum; 6K30; -.
DR PDBsum; 6KD9; -.
DR AlphaFoldDB; Q5AR53; -.
DR SMR; Q5AR53; -.
DR STRING; 227321.Q5AR53; -.
DR EnsemblFungi; CBF82281; CBF82281; ANIA_09227.
DR EnsemblFungi; EAA61518; EAA61518; AN9227.2.
DR GeneID; 2868057; -.
DR KEGG; ani:AN9227.2; -.
DR eggNOG; ENOG502S7ZW; Eukaryota.
DR HOGENOM; CLU_047725_1_0_1; -.
DR InParanoid; Q5AR53; -.
DR OMA; SHPIVEY; -.
DR OrthoDB; 623398at2759; -.
DR Proteomes; UP000000560; Chromosome VI.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR008775; Phytyl_CoA_dOase.
DR Pfam; PF05721; PhyH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Dioxygenase; Iron; Metal-binding; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..416
FT /note="Iron/alpha-ketoglutarate-dependent dioxygenase asqJ"
FT /id="PRO_0000437624"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 242
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:26553478"
FT BINDING 244
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:26553478"
FT BINDING 319
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:26553478"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:5OA4"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:5OA4"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:5OA4"
FT HELIX 131..138
FT /evidence="ECO:0007829|PDB:5OA4"
FT STRAND 139..144
FT /evidence="ECO:0007829|PDB:5OA4"
FT HELIX 149..165
FT /evidence="ECO:0007829|PDB:5OA4"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:5OA4"
FT STRAND 185..188
FT /evidence="ECO:0007829|PDB:5OA4"
FT TURN 192..194
FT /evidence="ECO:0007829|PDB:5OA4"
FT HELIX 196..200
FT /evidence="ECO:0007829|PDB:5OA4"
FT TURN 201..204
FT /evidence="ECO:0007829|PDB:5OA4"
FT HELIX 206..216
FT /evidence="ECO:0007829|PDB:5OA4"
FT TURN 217..219
FT /evidence="ECO:0007829|PDB:5OA4"
FT STRAND 222..232
FT /evidence="ECO:0007829|PDB:5OA4"
FT TURN 244..248
FT /evidence="ECO:0007829|PDB:5OA4"
FT HELIX 250..254
FT /evidence="ECO:0007829|PDB:5OA4"
FT STRAND 262..271
FT /evidence="ECO:0007829|PDB:5OA4"
FT TURN 275..278
FT /evidence="ECO:0007829|PDB:5OA4"
FT HELIX 286..288
FT /evidence="ECO:0007829|PDB:5OA4"
FT HELIX 297..299
FT /evidence="ECO:0007829|PDB:5OA4"
FT STRAND 310..314
FT /evidence="ECO:0007829|PDB:5OA4"
FT STRAND 326..328
FT /evidence="ECO:0007829|PDB:5OA4"
FT STRAND 331..340
FT /evidence="ECO:0007829|PDB:5OA4"
FT HELIX 354..358
FT /evidence="ECO:0007829|PDB:5OA4"
FT HELIX 362..367
FT /evidence="ECO:0007829|PDB:5OA4"
FT STRAND 375..377
FT /evidence="ECO:0007829|PDB:5OA4"
FT STRAND 383..386
FT /evidence="ECO:0007829|PDB:6KD9"
FT HELIX 391..394
FT /evidence="ECO:0007829|PDB:5OA4"
SQ SEQUENCE 416 AA; 45509 MW; FB2D74A1A2A5D2FA CRC64;
MGYPKAFTSS DSEPEPDLSR DLGNPVMGNP GVVSRSSSTV AQHSVRNNPT GPDGRLAGLW
NARALLRFPA EVNGVRLDFK SVSSRRPTSR LSLLPYSLCS ICPSSQATMT SKDHVKSQIP
RLSAINDLHK IWPTVEEHGA AIIESFLSLD IVRRLNEEVD PFVKIEPIPA AKTKDHPNHV
LSTTTRLVNV LAPISKAYRE DVLNSKVLHR ICSDAFHVYG DYWVLMGAVM ELAPSNPAQP
LHRDMRFSHP IVEYLKPDAP ATSINFLVAL SPFTAENGAT HVILGSHKWQ NLSNVSMDAT
VRALMNPGDA LLITDSTIHC GGAETTGTET RRLLTITMGI SQLTPLESNL AVPRPVIESL
TPLAQRLLGW ASQRSAAPRD IGLLTIRGNS IEKTMNLKAE QPLHDDEAEP LCRETI
