NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME ACTIVITY, AND MUTANT M594.
STRAIN=cv. Himalaya;
DOI=10.1073/pnas.041588998; PubMed=11172076 [NCBI, ExPASy, EBI, Israel, Japan]
Helliwell C.A., Chandler P.M., Poole A., Dennis E.S., Peacock J.W.;
"The CYP88A cytochrome P450, ent-kaurenoic acid oxidase, catalyzes three steps of the gibberellin biosynthesis pathway.";
Proc. Natl. Acad. Sci. U.S.A. 98:2065-2070(2001).

Comments

FUNCTION: Catalyzes three successive oxidations of ent-kaurenoic acid giving gibberellin 12 (GA12), a key step in gibberellins (GAs) biosynthesis. GAs, which are involved many processes, including stem elongation, play a central role in plant development.
CATALYTIC ACTIVITY: Ent-kaur-16-en-19-oate + NADPH + O₂ = ent-7-alpha-hydroxykaur-16-en-19-oate + NADP⁺ + H₂O.
CATALYTIC ACTIVITY: Ent-7-alpha-hydroxykaur-16-en-19-oate + NADPH + O₂ = gibberellin A(12) aldehyde + NADP⁺ + 2 H₂O.
CATALYTIC ACTIVITY: Gibberellin A(12) aldehyde + NADPH + O₂ = gibberellin A(12) + NADP⁺ + H₂O.
COFACTOR: Heme group (By similarity).
PATHWAY: Plant hormone biosynthesis; gibberellin biosynthesis .
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein (By similarity).
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

AF326277; AAK11616.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P33006; 1CPT. [HSSP ENTRY / PDB]

ModBase

Q9AXH9.

Organism-specific databases

Gramene

Q9AXH9; -.

Ontologies

GO:0005789;	Cellular component: endoplasmic reticulum membrane (inferred from electronic annotation from UniProtKB-SubCell).
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.

PROSITE

PS00086; CYTOCHROME_P450; 1.

Other

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

Keywords

Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Monooxygenase; NADP; Oxidoreductase; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 499`	`499`	`Ent-kaurenoic acid oxidase 1.`	`PRO_0000052180`
`TRANSMEM`	`5 25`	`21`	`Potential.`
`METAL`	`443 443`		`Iron (heme axial ligand) (By similarity).`
`MUTAGEN`	`372 372`		`N->K: In M594; induces dwarfism, due to accumulation of kaurenoic acid.`

Sequence information

Length: 499 AA [This is the length of the unprocessed precursor]

Molecular weight: 55876 Da [This is the MW of the unprocessed precursor]

CRC64: 76CB0C5CC6C3641F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MGEGAWWAVA AVVAALAVVA LDAAVRAAHA WYWTASLGAG RRGRLPPGDM GWPLVGGMWA 

        70         80         90        100        110        120 
FLRAFKSGRP DSFIDSFARR FGRAGLYRAF MFSSPTIMAT TPEACKQVLM DDDAFVTGWP 

       130        140        150        160        170        180 
KATVALIGPK SFVNMGYDEH RRLRKLTAAP INGFDALTSY LGFIDDTVVT TLRGWSERGG 

       190        200        210        220        230        240 
DGHFEFLTEL RRMTFRIIVQ IFMGGADERT AAELERTYTE LNYGMRAMAI DLPGFAYHKA 

       250        260        270        280        290        300 
IRARRRLVAA LQRVLDERRA RGGKTAAGAA APVDMMDRLI AVEDEGGRRL QDDEIIDVLV 

       310        320        330        340        350        360 
MYLNAGHESS GHITMWATVF LQENPEILAK AKAEQEAIMR SIPPGQKGLT LRDFRKMAYL 

       370        380        390        400        410        420 
SQVVDETLRF VNISFVSFRQ ATRDVFVNGY LIPKGWKVQL WYRSVHMDPQ VYPDPKKFDP 

       430        440        450        460        470        480 
SRWEGPPPRA GTFLPFGLGT RLCPGNDLAK LEISVFLHHF LLGYKLTRKN PNCRVRYLPH 

       490 
PRPVDNCLAK ITRLSSSHG

Q9AXH9 in FASTA format

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View entry in raw text format (no links)
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	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