ATNK_ARTSZ
ID ATNK_ARTSZ Reviewed; 756 AA.
AC A0A455LLW7;
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 atnK {ECO:0000303|PubMed:29797385};
DE EC=1.-.-.- {ECO:0000305|PubMed:29797385};
DE AltName: Full=Arthripenoid biosynthesis cluster protein K {ECO:0000303|PubMed:29797385};
GN Name=atnK {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], FUNCTION, 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}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC {ECO:0000305}.
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DR EMBL; MH183017; AYO60884.1; -; mRNA.
DR AlphaFoldDB; A0A455LLW7; -.
DR SMR; A0A455LLW7; -.
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 2: Evidence at transcript level;
KW FAD; Flavoprotein; Glycoprotein; Membrane; Monooxygenase; Oxidoreductase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..756
FT /note="FAD-dependent monooxygenase atnK"
FT /id="PRO_0000452551"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 522..542
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 567..587
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 595..615
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 634..654
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 691..711
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 721..741
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 42..43
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 136
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 313
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 323..327
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 246
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 756 AA; 84072 MW; 40503A1FF71934A6 CRC64;
MAVIEKRPDF KVVIVGGSIS GLVLAHSLHQ AGIDYIVLEG RNRIDPQIGA SIGLFSNGSR
ILDQLGVYKS ILDLTEPLVW YDMLTGQGDL VRRDDSLRLI EARTGYPVAF LERRQVLQVL
HKHTPDQSKI LTGKKVVSVR TLADGVEVQC KDGSKFTGDI VAGADGVYSR IRREMWRQAK
SDGGLKHLED DVKAMSADYR CLYGMSYPVP GLRKKSLYRT FNKDWSFLVV VGKDECCFWF
VFEKLNGTHK LSNMPTYTES DQAEFVKPFM KRYVSQGVAF EALWHRKTAA TLAALEEAQY
NHWTYGRFVC LGDSIHKMTP NIGQGGNWAI ESAAALTNKL HSLMKTTRQP TTEQISDTLI
EYEQSRQVRT KEVCTTAGFA TRLEAFEKFW HRPMALYVVP LAGDMLVDVH CQSVAEAPKL
DFLPPPELSL KQDTIFQAVQ FDQQGPHLVS RVLRATPLLA LCFAAFHCLE PTGSAVPANA
DTEAVRLAML SYLGDFFPIQ VIAMVESARR GNSMGIAGLW PLFGLTGYWG STGYAVPVYF
FLQYILSPPS RYAASDNRLV PTHYARSAVA ATGVGYLLLV AYGVLSQQNY LAGYAYWYLL
PACTAVVHPL FASFLTHTTF ADRVQNPRAD MKYLLLSYAI SGVFSGITHV YTWAPSPWGL
GNILLIAARL RQGALLLEEM GPEKLIQRHH ILMLGGGLFW ALLHLWDLKS TGRLKAGWFK
VLGALGGMLV MFGPGTALVL GWAWREVVLA RKTGPH
