ID   G430_FUSSX              Reviewed;         571 AA.
AC   A0A6S6AA17;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   02-DEC-2020, sequence version 1.
DT   03-AUG-2022, entry version 5.
DE   RecName: Full=Cytochrome P450 monooxygenase g430 {ECO:0000303|PubMed:32139880};
DE            EC=1.-.-.- {ECO:0000305|PubMed:32139880};
DE   AltName: Full=1233A biosynthesis cluster protein g430 {ECO:0000303|PubMed:32139880};
GN   Name=g430 {ECO:0000303|PubMed:32139880};
OS   Fusarium sp.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX   NCBI_TaxID=29916;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INDUCTION, DISRUPTION
RP   PHENOTYPE, AND PATHWAY.
RC   STRAIN=RK97-94;
RX   PubMed=32139880; DOI=10.1038/s41429-020-0295-4;
RA   Kato S., Motoyama T., Uramoto M., Nogawa T., Kamakura T., Osada H.;
RT   "Induction of secondary metabolite production by hygromycin B and
RT   identification of the 1233A biosynthetic gene cluster with a self-
RT   resistance gene.";
RL   J. Antibiot. 73:475-479(2020).
CC   -!- FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that
CC       mediates the biosynthesis of 1233A, a natural compound known as an
CC       inhibitor of HMG-CoA synthase in the mevalonate pathway and with
CC       antibacterial and antifungal activities (PubMed:32139880). The highly
CC       reducing polyketide synthase g433 is responsible for the 1233A backbone
CC       biosynthesis and the cytochrome P450 monoxygenase g430 catalyzes
CC       oxidation of the backbone (Probable). {ECO:0000269|PubMed:32139880,
CC       ECO:0000305|PubMed:32139880}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
CC   -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:32139880}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- INDUCTION: Expression is increased upon exposure to hygromycin B.
CC       {ECO:0000269|PubMed:32139880}.
CC   -!- DISRUPTION PHENOTYPE: Impairs the ability to produce 1233A and its
CC       hydrolysis product 1233B. {ECO:0000269|PubMed:32139880}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; LC516401; BBU37365.1; -; Genomic_DNA.
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   2: Evidence at transcript level;
KW   Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..571
FT                   /note="Cytochrome P450 monooxygenase g430"
FT                   /id="PRO_0000454629"
FT   TRANSMEM        8..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          552..571
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         471
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   571 AA;  64978 MW;  B1423E5558C12BBC CRC64;
     MQISSAFGAL IWVVTSYILY AIISNFIISR RHAAKARELK CEEPPFEKNR WPLGIDNLLR
     ALAADKAQQF PVDIIKRFED LGAHTYRYQI LGARNIRTAD PKNIQTILAN KFNDFDVGPS
     RRGNFLPMLG NGIFTADGDH WKHSRAIIRP QFTRDQVSDL NLEETHVQNL MKLIGPMIGS
     NGWIEQIDLL PYFFRLTIDS ATEFLFGEPV NSQLRFLPGY QSSKLGSKEE RFATAFDSGQ
     MALATRSRFM DSWWLYDSLA FRNSCKIVHD FVDHFVQLAL SRGLREKVSD TNSGGKEQYI
     FLEAIAAETQ NPTELRSELL HVLLAGRDTT ASHLGWVFHN LARDPVRYKK LRDIIIDEFG
     TYENPSEITF AKLKACKYLR YVNDESLRLY PVVPINARYA NKDTTLPRGG GKDGNSPIFI
     PKGSSTDFSV HVMHRRKDIW GPDADEFKPE RWEGRKVGWE YLPFNGGPRI CIGQQFALIE
     ASYVTVRLLQ RFDRMESLDK DAVVGHNLTL INCIANGVKT RSSIEFDGQT SQNDDQLRTI
     VEKPLVQKRS RCPLPAEAKL PKSRKPIGTA S