ATNJ_ARTSZ
ID ATNJ_ARTSZ Reviewed; 421 AA.
AC A0A455LLW0;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 05-JUN-2019, sequence version 1.
DT 03-AUG-2022, entry version 12.
DE RecName: Full=FAD-dependent monooxygenase atnJ {ECO:0000303|PubMed:29797385};
DE EC=1.-.-.- {ECO:0000269|PubMed:29797385};
DE AltName: Full=Arthripenoid biosynthesis cluster protein J {ECO:0000303|PubMed:29797385};
GN Name=atnJ {ECO:0000303|PubMed:29797385};
OS Arthrinium sp.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Apiosporaceae; Arthrinium;
OC unclassified Arthrinium.
OX NCBI_TaxID=1756131;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], DISRUPTION PHENOTYPE, FUNCTION, CATALYTIC
RP ACTIVITY, AND PATHWAY.
RC STRAIN=NF2194;
RX PubMed=29797385; DOI=10.1002/anie.201804317;
RA Zhang X., Wang T.T., Xu Q.L., Xiong Y., Zhang L., Han H., Xu K., Guo W.J.,
RA Xu Q., Tan R.X., Ge H.M.;
RT "Genome mining and comparative biosynthesis of meroterpenoids from two
RT phylogenetically distinct fungi.";
RL Angew. Chem. Int. Ed. 57:8184-8188(2018).
CC -!- FUNCTION: FAD-dependent monooxygenase; part of the gene cluster that
CC mediates the biosynthesis of the meroterpenoids arthripenoids
CC (PubMed:29797385). The pathway begins with the HR-PKS atnH that
CC catalyzes two chain-extension steps to form a reduced triketide, which
CC then primes the SAT domain in the NR-PKS atnG to initiate three more
CC cycles of extension to give a linear hexaketide corresponding to the
CC polyketide part of arthripenoids (PubMed:29797385). The FAD-dependent
CC monooxygenase atnJ then performs an oxidative decarboxylation at C11 of
CC the atnH/atnG product, via an electrophilic aromatic hydroxylation with
CC concomitant ipso-decarboxylation (PubMed:29797385). The membrane-bound
CC polyprenyl transferase atnF then introduces a farnesyl group before the
CC FAD-dependent monooxygenase atnK functions as the first epoxidase on
CC terminal C12'-C13' olefin, followed by a second epoxidation on C7'-C8'
CC catalyzed by atnA (PubMed:29797385). The terpene cyclase/mutase atnI
CC then initiates the sequential tricyclic ring formation through
CC protonation of the terminal epoxide and catalyzes the regioselective
CC and stereoselective 6/6/6-tricyclic ring formation (PubMed:29797385).
CC The cytochrome P450 monooxygenase atnM is responsible for hydroxylating
CC both C1' and C10' (Probable). The next steps may involve ketoreduction
CC and acetyl transfer by the ketoreductase atnB and the acetyltransferase
CC atnC, and lead to the production of arthripenoid B, the final
CC biosynthetic product of the atn cluster (PubMed:29797385). The
CC hydroquinone moiety in arthripenoid B is prone to undergo spontaneous
CC oxidation to afford a benzoquinone compound, a key intermediate for
CC generating structure diversity (Probable). For instance, addition of a
CC cysteine followed by ring contraction gives arthripenoid A,
CC tautomerization gives the main product arthripenoid C, addition of a
CC molecular of water or amine affords arthripenoid D or E, respectively,
CC and loss of one water forms arthripenoid F (Probable).
CC {ECO:0000269|PubMed:29797385, ECO:0000305|PubMed:29797385}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:A6T923};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000269|PubMed:29797385}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Abolishes the production of arthripenoids but
CC leads to the accumulation of new product which has no double bond in
CC the side chain. {ECO:0000269|PubMed:29797385}.
CC -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC {ECO:0000305}.
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DR EMBL; MH183016; AYO60883.1; -; mRNA.
DR AlphaFoldDB; A0A455LLW0; -.
DR SMR; A0A455LLW0; -.
DR UniPathway; UPA00213; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR Pfam; PF01494; FAD_binding_3; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW FAD; Flavoprotein; Membrane; Monooxygenase; Oxidoreductase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..421
FT /note="FAD-dependent monooxygenase atnJ"
FT /id="PRO_0000452552"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 371..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 22
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 41..42
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 232..234
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 303
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 313..317
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
SQ SEQUENCE 421 AA; 45429 MW; F162D96094665A27 CRC64;
MSTTKPICLV PLHVVIVGAG IGGLSAAVAL ANRGHSVLIL ESTSELSHVG AGVALPPTTR
KWYESEGVLQ VDDTACVPLE GIEITKWDTG ELVTRTAANP AGKQTAIHHG DMQLALLARA
RELTNVEIRL GARVVDVDLE ATVALLADGQ RVAGDLIIAA DGVKSTLKAK VCPPEAVVPL
PTGEAAYRFT LPRELLESDA ELRELVQRPW GVRWDGPSCH VVAYPLRNHR LLNVVLIHPD
NGDAKESWTS VTDKQNVLAD YQGWNPTLLK LIALAPPEVP NFRMFLYSPA PVWVKGSTIL
LGDSCHAMLP YLGQGVAQAV EDATAIATVL SLIETRKQLP LALRAYESSR KERVDQIQAA
TYRAREQLHL RDGDAQAARD SQRKATSGTG QNSDVVKMQQ SYWTWDAAGV AEKTLAALII
A
