EQXH_FUSHE
ID EQXH_FUSHE Reviewed; 513 AA.
AC S4W283;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2013, sequence version 1.
DT 03-AUG-2022, entry version 27.
DE RecName: Full=Cytochrome P450 monooxygenase eqxH {ECO:0000303|PubMed:23614392};
DE EC=1.-.-.- {ECO:0000305|PubMed:23614392};
DE AltName: Full=Equisetin biosynthesis protein H {ECO:0000303|PubMed:23614392};
GN Name=eqxH {ECO:0000303|PubMed:23614392};
OS Fusarium heterosporum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium heterosporum species complex.
OX NCBI_TaxID=42747;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PATHWAY.
RC STRAIN=ATCC 74349 / MF6069;
RX PubMed=23614392; DOI=10.1021/cb400159f;
RA Kakule T.B., Sardar D., Lin Z., Schmidt E.W.;
RT "Two related pyrrolidinedione synthetase loci in Fusarium heterosporum ATCC
RT 74349 produce divergent metabolites.";
RL ACS Chem. Biol. 8:1549-1557(2013).
RN [2]
RP FUNCTION.
RX PubMed=18652469; DOI=10.1021/ja803078z;
RA Sims J.W., Schmidt E.W.;
RT "Thioesterase-like role for fungal PKS-NRPS hybrid reductive domains.";
RL J. Am. Chem. Soc. 130:11149-11155(2008).
CC -!- FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that
CC mediates the biosynthesis of equisetin, a trans-fused decalin-
CC containing tetramic acid with antimicrobial activity (PubMed:23614392).
CC The PKS module of eqxS together with the enoylreductase eqxC catalyze
CC the formation of the polyketide unit which is then conjugated to L-
CC serine by the condensation domain of the eqxS NRPS module
CC (PubMed:23614392). Activity of the Dieckmann cyclase domain (RED)
CC results in release of the Dieckmann product intermediate
CC (PubMed:23614392, PubMed:18652469). Diels-Alderase eqx3 is involved in
CC endo-selective Diels-Alder cycloaddition to form the decalin ring,
CC leading to the production of N-desmethylequisetin also called
CC trichosetin (By similarity). Subsequent N-methylation is carried out by
CC eqxD to give equisetin (PubMed:23614392).
CC {ECO:0000250|UniProtKB:A0A0E4AZP0, ECO:0000269|PubMed:18652469,
CC ECO:0000269|PubMed:23614392}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000305|PubMed:23614392}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; KC439347; AGO86661.1; -; Genomic_DNA.
DR AlphaFoldDB; S4W283; -.
DR SMR; S4W283; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00465; EP450IV.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW Oxidoreductase; Transmembrane; Transmembrane helix.
FT CHAIN 1..513
FT /note="Cytochrome P450 monooxygenase eqxH"
FT /id="PRO_0000441314"
FT TRANSMEM 13..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 449
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P04798"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 513 AA; 58375 MW; 9AD67F3C89B7E675 CRC64;
MSTKLDTILE NPQYAILCGI TVFTLFIVQL SLFDRGRNYP LLNPKGSFEI STNRVVREFI
SDSRNLLEKG KSLFKGQPYR ANTDWGEVVV IPPQFLDALK SHKDLDFTIP AQDDSHCYIP
GFEPFDADPN LSKVVIKYLT KALNRVTGPL SEEASIAFRT VISDSPEWHE IQPQPAFVRI
ISRMSSRVFM GEELCRNEEW VKLAGDYTVQ SFKTGDELRM YPRWSRPFVH HFLPSCKEVR
RTLNAARNCL NPLLERRNAI KAEAKAKGEP CPYDNSFEWF EKEYSTHDPA VAQLNLSLVA
IHTTTDLLME TVFNIAQHPE LLAPLREEIV RVLSTEGLKK TALLNLKLMD SVLKESQRLR
PALLGSFRRL AMADVTLPNG DVIKKGTKIV CSTSHMWSAD SHESGEEFDG YRFLRMREKE
ETEQGKTSHP HLVSPSSDHL GFGFGNHACP GRFFAANELK IALCHMLLKY DWKLAKDAVP
RSASFGMILM PDLRTKLLIR RRSEELDIDS VES
