ID   KO1_GIBIN               Reviewed;         525 AA.
AC   Q701P2;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Ent-kaurene oxidase;
DE            EC=1.14.14.86 {ECO:0000250|UniProtKB:Q93ZB2};
DE   AltName: Full=Cytochrome P450 503A1;
DE   AltName: Full=Cytochrome P450-4;
GN   Name=CYP503A1;
OS   Gibberella intermedia (Bulb rot disease fungus) (Fusarium proliferatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium fujikuroi species complex.
OX   NCBI_TaxID=948311;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=D02945;
RX   PubMed=15746349; DOI=10.1128/aem.71.3.1462-1472.2005;
RA   Malonek S., Rojas M.C., Hedden P., Gaskin P., Hopkins P., Tudzynski B.;
RT   "Functional characterization of two cytochrome P450 monooxygenase genes,
RT   P450-1 and P450-4, of the gibberellic acid gene cluster in Fusarium
RT   proliferatum (Gibberella fujikuroi MP-D).";
RL   Appl. Environ. Microbiol. 71:1462-1472(2005).
RN   [2]
RP   CHARACTERIZATION.
RX   PubMed=16204516; DOI=10.1128/aem.71.10.6014-6025.2005;
RA   Malonek S., Rojas M.C., Hedden P., Hopkins P., Tudzynski B.;
RT   "Restoration of gibberellin production in Fusarium proliferatum by
RT   functional complementation of enzymatic blocks.";
RL   Appl. Environ. Microbiol. 71:6014-6025(2005).
CC   -!- FUNCTION: Catalyzes three successive oxidations of the 4-methyl group
CC       of ent-kaurene giving kaurenoic acid, a key step in gibberellin (GA)
CC       biosynthesis.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ent-kaur-16-ene + 3 O2 + 3 reduced [NADPH--hemoprotein
CC         reductase] = ent-kaur-16-en-19-oate + 4 H(+) + 4 H2O + 3 oxidized
CC         [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:32323, Rhea:RHEA-
CC         COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15415,
CC         ChEBI:CHEBI:57297, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210;
CC         EC=1.14.14.86; Evidence={ECO:0000250|UniProtKB:Q93ZB2};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- PATHWAY: Plant hormone biosynthesis; gibberellin biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- MISCELLANEOUS: This protein is poorly expressed and has no detectable
CC       ent-kaurene oxidase activity in this species. Consequently, this
CC       species does not produce gibberellins.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AJ628021; CAF31352.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q701P2; -.
DR   SMR; Q701P2; -.
DR   BRENDA; 1.14.14.86; 7521.
DR   UniPathway; UPA00390; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0052617; F:ent-kaur-16-en-19-al oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0052616; F:ent-kaur-16-en-19-ol oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0052615; F:ent-kaurene oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0009686; P:gibberellin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR002401; Cyt_P450_E_grp-I.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; SSF48264; 1.
PE   1: Evidence at protein level;
KW   Heme; Iron; Membrane; Metal-binding; Monooxygenase; NADP; Oxidoreductase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..525
FT                   /note="Ent-kaurene oxidase"
FT                   /id="PRO_0000052209"
FT   TRANSMEM        31..51
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         466
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"
SQ   SEQUENCE   525 AA;  59974 MW;  4E05AE3CEC4D3451 CRC64;
     MNKSNSMNNT SLERLFQQLV LGLDGIPLMD VHWLIYVAFG AWLCSYVIHV LSSSSTVKVP
     VVGYRSVFEP TWLLRLRFVW EGGSIIGQGY NKFKDSIFQV RKLGTDIVII PPNFIDEVRK
     LSQDKTRSVE PFINDFAGQY TRGMVFLQSD LQNRVIQQRL TPKLVSLTKV MKEELDYALT
     KEIPDMKDDE WVEVDISSIM VRLISRISAR VFLGPEHCRN QEWLTNTAEY SESLFITGFI
     LRVVPHILRP FIAPLLPSYR TLLRNVSSGR RVIGDIIRSQ QGDGNEDILS WMRDAATGEE
     KQIDNIAQRM LILSLASIHT TAMTMTHAMY DLCARPEYIE PLRDEVKGVV DASGWDKTAL
     NRLHRLDSFL KESQRFNPVF LLTFNRIYHQ SMTLSDGTNL PSGTRIAVPS HAMLQDSAHV
     PGPTPPTEFD GFRYSKIRSD SNYAQKYLFS MTDSSNMAFG YGKYACPGRF YASNEMKLTL
     AILLLQFEFK LPDGKGRPRN ITIDSDMIPD PRARLCVRKR SLRDE