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Reviewed, UniProtKB/Swiss-Prot P93236 (ABA2_SOLLC)

Last modified November 4, 2008. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Zeaxanthin epoxidase, chloroplastic
    EC=1.14.13.90
OrganismSolanum lycopersicum (Tomato) (Lycopersicon esculentum)
Taxonomic identifier4081 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanumLycopersicon

Protein attributes

Sequence length669 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

General annotation (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 + O(2) = antheraxanthin + NAD(P)(+) + H(2)O.

Antheraxanthin + NAD(P)H + O(2) = violaxanthin + NAD(P)(+) + H(2)O.

Cofactor

FAD Potential.

Pathway

Plant hormone biosynthesis; abscisic acid biosynthesis.

Lipid metabolism; steroid biosynthesis.

Subcellular location

PlastidchloroplastBy similarity.

Sequence similarities

Contains 1 FHA domain.

Ontologies

Keywords

   Biological processAbscisic acid biosynthesis
   Cellular componentChloroplast
Plastid
   DomainTransit peptide
   LigandFAD
Flavoprotein
NAD
NADP
   Molecular functionOxidoreductase

Gene Ontology (GO)

   Biological processabscisic acid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentchloroplast

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionzeaxanthin epoxidase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4949Chloroplast Potential
Chain50 – 669620Zeaxanthin epoxidase, chloroplastic
PRO_0000020610

Regions

Domain553 – 61765FHA
Nucleotide binding87 – 11529FAD Potential
Nucleotide binding365 – 37814FAD Potential

Sequences

Sequence LengthMass (Da)Tools
P93236-1 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: 1140C9F29C3499B7

FASTA66973,102
        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 

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References

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

Cross-references

Sequence databases

Z83835 mRNA. Translation: CAB06084.1.
PIRT07754.
UniGeneLes.112

3D structure databases

ModBaseSearch...

Family and domain databases

InterProIPR006076. FAD-dep_OxRdtase.
IPR000253. FHA.
IPR003042. Rng_hydrolase.
IPR017079. Zeaxanthin_epoxidase.
[Graphical view]
Gene3DG3DSA:2.60.200.20. FHA. 1 hit.
PfamPF01266. DAO. 1 hit.
PF00498. FHA. 1 hit.
[Graphical view]
PIRSFPIRSF036989. Zeaxanthin_epoxidase. 1 hit.
PRINTSPR00420. RNGMNOXGNASE.
SMARTSM00240. FHA. 1 hit.
[Graphical view]
PROSITEPS50006. FHA_DOMAIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameABA2_SOLLC
AccessionPrimary (citable) accession number: P93236
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: May 1, 1997
Last modified: November 4, 2008
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents