[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION. STRAIN=m567; DOI=10.1128/AEM.67.8.3514-3522.2001; PubMed=11472927 [NCBI, ExPASy, EBI, Israel, Japan] Tudzynski B., Hedden P., Carrera E., Gaskin P.; "The P450-4 gene of Gibberella fujikuroi encodes ent-kaurene oxidase in the gibberellin biosynthesis pathway."; Appl. Environ. Microbiol. 67:3514-3522(2001).
[2]	INDUCTION. DOI=10.1046/j.1365-2958.2003.03326.x; PubMed=12581353 [NCBI, ExPASy, EBI, Israel, Japan] Mihlan M., Homann V., Liu T.-W.D., Tudzynski B.; "AREA directly mediates nitrogen regulation of gibberellin biosynthesis in Gibberella fujikuroi, but its activity is not affected by NMR."; Mol. Microbiol. 47:975-991(2003).

Comments

FUNCTION: Catalyzes three successive oxidations of the 4-methyl group of ent-kaurene giving kaurenoic acid, a key step in gibberellin (GA) biosynthesis.
CATALYTIC ACTIVITY: Ent-kaur-16-ene + NADPH + O₂ = ent-kaur-16-en-19-ol + NADP⁺ + H₂O.
CATALYTIC ACTIVITY: Ent-kaur-16-en-19-ol + NADPH + O₂ = ent-kaur-16-en-19-al + NADP⁺ + 2 H₂O.
CATALYTIC ACTIVITY: Ent-kaur-16-en-19-al + NADPH + O₂ = ent-kaur-16-en-19-oate + NADP⁺ + H₂O.
COFACTOR: Heme group (By similarity).
PATHWAY: Plant hormone biosynthesis; gibberellin biosynthesis .
SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein (Potential).
INDUCTION: By nitrogen starvation.
SIMILARITY: Belongs to the cytochrome P450 family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

Y17243; CAA76703.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

ModBase

O94142.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-11667; -.

Ontologies

GO:0016021;	Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0010241;	Molecular function: ent-kaurene oxidase activity (inferred from electronic annotation from EC).
GO:0020037;	Molecular function: heme binding (inferred from electronic annotation from InterPro).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006950;	Biological process: response to stress (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001128; Cyt_P450.
IPR002401; Cyt_P450_E_grp-I.
Graphical view of domain structure.

Gene3D

G3DSA:1.10.630.10; Cyt_P450; 1.

PANTHER

PTHR19383; Cyt_P450; 1.

Pfam

PF00067; p450; 1.
Pfam graphical view of domain structure.

PRINTS

PR00463; EP450I.
PR00385; P450.

Other

ProtoNet

O94142.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Heme; Iron; Membrane; Metal-binding; Monooxygenase; NADP; Oxidoreductase; Stress response; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 525`	`525`	`Ent-kaurene oxidase.`	`PRO_0000052208`
`TRANSMEM`	`31 51`	`21`	`Potential.`
`METAL`	`466 466`		`Iron (heme axial ligand) (By similarity).`

Sequence information

Length: 525 AA [This is the length of the unprocessed precursor]

Molecular weight: 59951 Da [This is the MW of the unprocessed precursor]

CRC64: CE6DEC6788AC61B7 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSKSNSMNST SHETLFQQLV LGLDRMPLMD VHWLIYVAFG AWLCSYVIHV LSSSSTVKVP 

        70         80         90        100        110        120 
VVGYRSVFEP TWLLRLRFVW EGGSIIGQGY NKFKDSIFQV RKLGTDIVII PPNYIDEVRK 

       130        140        150        160        170        180 
LSQDKTRSVE PFINDFAGQY TRGMVFLQSD LQNRVIQQRL TPKLVSLTKV MKEELDYALT 

       190        200        210        220        230        240 
KEMPDMKNDE WVEVDISSIM VRLISRISAR VFLGPEHCRN QEWLTTTAEY SESLFITGFI 

       250        260        270        280        290        300 
LRVVPHILRP FIAPLLPSYR TLLRNVSSGR RVIGDIIRSQ QGDGNEDILS WMRDAATGEE 

       310        320        330        340        350        360 
KQIDNIAQRM LILSLASIHT TAMTMTHAMY DLCACPEYIE PLRDEVKSVV GASGWDKTAL 

       370        380        390        400        410        420 
NRFHKLDSFL KESQRFNPVF LLTFNRIYHQ SMTLSDGTNI PSGTRIAVPS HAMLQDSAHV 

       430        440        450        460        470        480 
PGPTPPTEFD GFRYSKIRSD SNYAQKYLFS MTDSSNMAFG YGKYACPGRF YASNEMKLTL 

       490        500        510        520 
AILLLQFEFK LPDGKGRPRN ITIDSDMIPD PRARLCVRKR SLRDE

O94142 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools