[1]	NUCLEOTIDE SEQUENCE [MRNA]. Burbidge A., Grieve T., Terry C., Corlett J., Thompson A., Taylor I.; "Structure and expression of a cDNA encoding zeaxanthine epoxidase, isolated from a wilt-related tomato (Lycopersicon esculentum Mill.) library."; J. Exp. Bot. 48:1749-1750(1997).

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 (By similarity).
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

Z83835; CAB06084.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

T07754; T07754.

UniGene

Les.112

3D structure databases

ModBase

P93236.

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; NAD; NADP; Oxidoreductase; Plastid; Transit peptide.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 49`	`49`	`Chloroplast (Potential).`
`CHAIN`	`50 669`	`620`	`Zeaxanthin epoxidase, chloroplastic.`	`PRO_0000020610`
`DOMAIN`	`553 617`	`65`	`FHA.`
`NP_BIND`	`87 115`	`29`	`FAD (Potential).`
`NP_BIND`	`365 378`	`14`	`FAD (Potential).`

Sequence information

Length: 669 AA [This is the length of the unprocessed precursor]

Molecular weight: 73102 Da [This is the MW of the unprocessed precursor]

CRC64: 1140C9F29C3499B7 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MYSTVFYTSV HPSTSVLSRK QLPLLISKDF SAELYHSLPC RSLENGHINK VKGVKVKATI 

        70         80         90        100        110        120 
AEAPVTPTEK TDSGANGDLK VPQKKLKVLV AGGGIGGLVF ALAAKKRGFD VLVFERDLSA 

       130        140        150        160        170        180 
IRGEGQYRGP IQIQSNALAA LEAIDLDVAE DIMNAGCITG QRINGLVDGI SGNWYCKFDT 

       190        200        210        220        230        240 
FTPAVERGLP VTRVISRMTL QQILARAVGE EIIMNESNVV DFEDDGEKVT VVLENGQRFT 

       250        260        270        280        290        300 
GDLLVGADGI RSKVRTNLFG PSEATYSGYT CYTGIADFVP ADIDTVGYRV FLGHKQYFVS 

       310        320        330        340        350        360 
SDVGGGKMQW YAFYNEPAGG ADAPNGKKER LLKIFGGWCD NVIDLLVATD EDAILRRDIY 

       370        380        390        400        410        420 
DRPPTFSWGR GRVTLLGDSV HAMQPNLGQG GCMAIEDSYQ LALELEKACS RSAEFGSPVD 

       430        440        450        460        470        480 
IISSLRSYES ARKLRVGVIH GLARMAAIMA STYKAYLGVG LGPLSFLTQY RIPHPGRVGG 

       490        500        510        520        530        540 
RVFIDLGMPL MLSWVLGGNG DKLEGRIKHC RLSEKANDQL RKWFEDDDAL ERATDAEWLL 

       550        560        570        580        590        600 
LPAGNGSSGL EAIVLSRDED VPCTVGSISH TNIPGKSIVL PLPQVSEMHA RISCKDGAFF 

       610        620        630        640        650        660 
VTDLRSEHGT WVTDNEGRRY RTSPNFPTRF HPSDVIEFGS DKAAFRVKAM KFPLKTSERK 


EEREAVEAA

P93236 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