NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
STRAIN=cv. Viviani;
TISSUE=Seedling;
PubMed=8665840 [NCBI, ExPASy, EBI, Israel, Japan]
Marin E., Nussaume L., Quesada A., Gonneau M., Sotta B., Hugueney P., Frey A., Marion-Poll A.;
"Molecular identification of zeaxanthin epoxidase of Nicotiana plumbaginifolia, a gene involved in abscisic acid biosynthesis and corresponding to the ABA locus of Arabidopsis thaliana.";
EMBO J. 15:2331-2342(1996).

[2]

CHARACTERIZATION.
STRAIN=cv. Viviani;
DOI=10.1104/pp.118.3.1021; PubMed=9808747 [NCBI, ExPASy, EBI, Israel, Japan]
Audran C., Borel C., Frey A., Sotta B., Meyer C., Simonneau T., Marion-Poll A.;
"Expression studies of the zeaxanthin epoxidase gene in Nicotiana plumbaginifolia.";
Plant Physiol. 118:1021-1028(1998).

Comments

FUNCTION: Converts zeaxanthin into antheraxanthin and subsequently violaxanthin. Involved in the epoxidation of zeaxanthin. Plays an important role in resistance to stresses, seed development and dormancy.
CATALYTIC ACTIVITY: Zeaxanthin + NAD(P)H + O₂ = antheraxanthin + NAD(P)⁺ + H₂O.
CATALYTIC ACTIVITY: Antheraxanthin + NAD(P)H + O₂ = violaxanthin + NAD(P)⁺ + H₂O.
COFACTOR: FAD (Potential).
PATHWAY: Plant hormone biosynthesis; abscisic acid biosynthesis .
PATHWAY: Lipid metabolism; steroid biosynthesis .
SUBCELLULAR LOCATION: Plastid, chloroplast membrane; Peripheral membrane protein. Plastid, chloroplast thylakoid membrane; Peripheral membrane protein.
TISSUE SPECIFICITY: Higher expression in leaves than in roots.
INDUCTION: By drought stress; in roots.
SIMILARITY: Contains 1 FHA domain.

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

X95732; CAA65048.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S69548; S69548.

3D structure databases

ModBase

Q40412.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-2602; -.

Ontologies

GO:0009540;	Molecular function: zeaxanthin epoxidase activity (inferred from electronic annotation from EC).
QuickGo view.

Family and domain databases

InterPro

IPR006076; FAD-dep_OxRdtase.
IPR000253; FHA.
IPR003042; Rng_hydrolase.
IPR017079; Zeaxanthin_epoxidase.
Graphical view of domain structure.

Gene3D

G3DSA:2.60.200.20; FHA; 1.

Pfam

PF01266; DAO; 1.
PF00498; FHA; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF036989; Zeaxanthin_epoxidase; 1.

PRINTS

PR00420; RNGMNOXGNASE.

SMART

SM00240; FHA; 1.
SMART graphical view of domain structure.

PROSITE

PS50006; FHA_DOMAIN; 1.
PROSITE graphical view of domain structure (profiles).

Other

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

Keywords

Abscisic acid biosynthesis; Chloroplast; FAD; Flavoprotein; Membrane; NAD; NADP; Oxidoreductase; Plastid; Stress response; Transit peptide.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 50`	`50`	`Chloroplast (Potential).`
`CHAIN`	`51 663`	`613`	`Zeaxanthin epoxidase, chloroplastic.`	`PRO_0000020611`
`DOMAIN`	`547 611`	`65`	`FHA.`
`NP_BIND`	`81 109`	`29`	`FAD (Potential).`
`NP_BIND`	`359 372`	`14`	`FAD (Potential).`

Sequence information

Length: 663 AA [This is the length of the unprocessed precursor]

Molecular weight: 72524 Da [This is the MW of the unprocessed precursor]

CRC64: D8D8BB4E73A661BA [This is a checksum on the sequence]

        10         20         30         40         50         60 
MYSTVFYTSV HPSTSAFSRK QLPLLISKDF PTELYHSLPC SRSLENGQIK KVKGVVKATI 

        70         80         90        100        110        120 
AEAPATIPPT DLKKVPQKKL KVLVAGGGIG GLVFALAAKK RGFDVLVFER DLSAIRGEGQ 

       130        140        150        160        170        180 
YRGPIQIQSN ALAALEAIDM DVAEDIMNAG CITGQRINGL VDGVSGNWYC KFDTFTPAVE 

       190        200        210        220        230        240 
RGLPVTRVIS RMTLQQNLAR AVGEDIIMNE SNVVNFEDDG EKVTVTLEDG QQYTGDLLVG 

       250        260        270        280        290        300 
ADGIRSKVRT NLFGPSDVTY SGYTCYTGIA DFVPADIETV GYRVFLGHKQ YFVSSDVGGG 

       310        320        330        340        350        360 
KMQWYAFHNE PAGGVDDPNG KKARLLKIFE GWCDNVIDLL VATDEDAILR RDIYDRPPTF 

       370        380        390        400        410        420 
SWGKGRVTLL GDSVHAMQPN LGQGGCMAIE DSYQLALELD KALSRSAESG TPVDIISSLR 

       430        440        450        460        470        480 
SYESSRKLRV GVIHGLARMA AIMASTYKAY LGVGLGPLSF LTKFRIPHPG RVGGRFFIDL 

       490        500        510        520        530        540 
GMPLMLSWVL GGNGEKLEGR IQHCRLSEKA NDQLRNWFED DDALERATDA EWLLLPAGNS 

       550        560        570        580        590        600 
NAALETLVLS RDENMPCNIG SVSHANIPGK SVVIPLPQVS EMHARISYKG GAFFVTDLRS 

       610        620        630        640        650        660 
EHGTWITDNE GRRYRASPNF PTRFHPSDII EFGSDKKAAF RVKVMKFPPK TAAKEERQAV 


GAA

Q40412 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