ID   KO1_GIBFU               Reviewed;         525 AA.
AC   O94142;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 93.
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 fujikuroi (Bakanae and foot rot disease fungus) (Fusarium
OS   fujikuroi).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium fujikuroi species complex.
OX   NCBI_TaxID=5127;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CHARACTERIZATION.
RC   STRAIN=m567;
RX   PubMed=11472927; DOI=10.1128/aem.67.8.3514-3522.2001;
RA   Tudzynski B., Hedden P., Carrera E., Gaskin P.;
RT   "The P450-4 gene of Gibberella fujikuroi encodes ent-kaurene oxidase in the
RT   gibberellin biosynthesis pathway.";
RL   Appl. Environ. Microbiol. 67:3514-3522(2001).
RN   [2]
RP   INDUCTION.
RX   PubMed=12581353; DOI=10.1046/j.1365-2958.2003.03326.x;
RA   Mihlan M., Homann V., Liu T.-W.D., Tudzynski B.;
RT   "AREA directly mediates nitrogen regulation of gibberellin biosynthesis in
RT   Gibberella fujikuroi, but its activity is not affected by NMR.";
RL   Mol. Microbiol. 47:975-991(2003).
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. {ECO:0000269|PubMed:11472927}.
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   -!- INDUCTION: By nitrogen starvation. {ECO:0000269|PubMed:12581353}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; Y17243; CAA76703.1; -; Genomic_DNA.
DR   AlphaFoldDB; O94142; -.
DR   KEGG; ag:CAA76703; -.
DR   eggNOG; KOG0156; Eukaryota.
DR   BioCyc; MetaCyc:MON-11667; -.
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   Stress response; Transmembrane; Transmembrane helix.
FT   CHAIN           1..525
FT                   /note="Ent-kaurene oxidase"
FT                   /id="PRO_0000052208"
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;  59951 MW;  CE6DEC6788AC61B7 CRC64;
     MSKSNSMNST SHETLFQQLV LGLDRMPLMD VHWLIYVAFG AWLCSYVIHV LSSSSTVKVP
     VVGYRSVFEP TWLLRLRFVW EGGSIIGQGY NKFKDSIFQV RKLGTDIVII PPNYIDEVRK
     LSQDKTRSVE PFINDFAGQY TRGMVFLQSD LQNRVIQQRL TPKLVSLTKV MKEELDYALT
     KEMPDMKNDE WVEVDISSIM VRLISRISAR VFLGPEHCRN QEWLTTTAEY SESLFITGFI
     LRVVPHILRP FIAPLLPSYR TLLRNVSSGR RVIGDIIRSQ QGDGNEDILS WMRDAATGEE
     KQIDNIAQRM LILSLASIHT TAMTMTHAMY DLCACPEYIE PLRDEVKSVV GASGWDKTAL
     NRFHKLDSFL KESQRFNPVF LLTFNRIYHQ SMTLSDGTNI PSGTRIAVPS HAMLQDSAHV
     PGPTPPTEFD GFRYSKIRSD SNYAQKYLFS MTDSSNMAFG YGKYACPGRF YASNEMKLTL
     AILLLQFEFK LPDGKGRPRN ITIDSDMIPD PRARLCVRKR SLRDE