ID   FSDH_FUSHE              Reviewed;         564 AA.
AC   S0ARX1;
DT   30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT   18-SEP-2013, sequence version 1.
DT   03-AUG-2022, entry version 24.
DE   RecName: Full=Cytochrome P450 monooxygenase fsdH {ECO:0000303|PubMed:23614392};
DE            EC=1.-.-.- {ECO:0000305|PubMed:23614392};
DE   AltName: Full=Fusaridione A biosynthesis protein H {ECO:0000303|PubMed:23614392};
GN   Name=fsdH {ECO:0000303|PubMed:23614392};
GN   Synonyms=eqi5 {ECO:0000303|PubMed:15724180};
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].
RC   STRAIN=ATCC 74349 / MF6069;
RX   PubMed=15724180; DOI=10.1039/b413523g;
RA   Sims J.W., Fillmore J.P., Warner D.D., Schmidt E.W.;
RT   "Equisetin biosynthesis in Fusarium heterosporum.";
RL   Chem. Commun. (Camb.) 2:186-188(2005).
RN   [2]
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).
CC   -!- FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that
CC       mediates the biosynthesis of fusaridione A, a bright yellow trans-fused
CC       decalin-containing tetramic acid with antimicrobial activity
CC       (PubMed:23614392). The PKS module of fsdS catalyzes the formation of
CC       the polyketide unit which is then conjugated to L-tyrosine by the
CC       condensation domain of the fsdS NRPS module. Activity of the Dieckmann
CC       cyclase domain (RED) results in release of the intermediate fusaridione
CC       A (PubMed:23614392). The unstable pyrrolidinedione ring of fusaridione
CC       A is opened through a reverse-Dieckmann reaction to afford its ring-
CC       opened form (PubMed:23614392). {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; AY700570; AGO65988.1; -; Genomic_DNA.
DR   AlphaFoldDB; S0ARX1; -.
DR   SMR; S0ARX1; -.
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:0016712; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen; IEA:InterPro.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002974; Cyt_P450_E_CYP52.
DR   InterPro; IPR002402; Cyt_P450_E_grp-II.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00464; EP450II.
DR   PRINTS; PR01239; EP450IICYP52.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   3: Inferred from homology;
KW   Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..564
FT                   /note="Cytochrome P450 monooxygenase fsdH"
FT                   /id="PRO_0000441315"
FT   TRANSMEM        18..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         472
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"
SQ   SEQUENCE   564 AA;  63743 MW;  56DAAA4AFC241826 CRC64;
     MALTVFEHAS ALWYRLQGSV SLAVLSTLAV VIAGWYILSS ISLYFSRRQF IALHGCKPIA
     NRYPSKWFGI NFILEAGRTY KERRYLDALT WNFRNIGYTH EVRALGGTSV WTVEPENIKA
     VLTSKFKDYS LGNRPAVMGP LLGRGVFVTD GEEWSHSRAL LRPNFAKDQV ADLSMIERHL
     QQLLKMIPDD GKAIDLNDLI LSFTMDSSTE FLFGESTETL TSGINRQFSD AFAYSLHDIS
     SGLRLGPWYK FRRTDPKAVQ SHRICREYAD KYVEKALEYR RNYIKSVEDG ATDKPSIDGG
     DSRRTFLREL ALATDDREKL RDELLSLLLA GRDTTASLIG SLLFSLAKKP ECWEKVRSEI
     EETLHGDLPS YEQLRNFKYA KYCVNEALRL YPPVPNNAKI AIRDTVLPRG GGPEGRDPII
     VPKDAPVIYT VYALHRRYDL FGDDADDFRP ERWENQRYTW EFLPFNGGPR ICLGQQYALV
     ETLYVLVRFA QHFSKIESMD PEPWTESLAL TVSSGNGVKV KLERGSSDVH GLSTQGVLID
     YGGLFAPTQK VPGTGVTQIS KGKA