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 27-MAR-2024, entry version 99.
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 SMR; O94142; -.
DR KEGG; ag:CAA76703; -.
DR eggNOG; KOG0156; Eukaryota.
DR OrthoDB; 1351063at2759; -.
DR BioCyc; MetaCyc:MONOMER-11667; -.
DR UniPathway; UPA00390; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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 CDD; cd11041; CYP503A1-like; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR PANTHER; PTHR46206; CYTOCHROME P450; 1.
DR PANTHER; PTHR46206:SF9; CYTOCHROME P450 MONOOXYGENASE AN1598-RELATED; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; Cytochrome P450; 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
//
