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UniProtKB/Swiss-Prot entry Q39249


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name VDE_ARATH
Primary accession number Q39249
Secondary accession number Q9SJD9
Integrated into Swiss-Prot on January 23, 2007
Sequence was last modified on November 1, 1996 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 58)
Name and origin of the protein
Protein name Violaxanthin de-epoxidase, chloroplastic [Precursor]
Synonyms AtVxDE
EC 1.10.99.3
Protein NON-PHOTOCHEMICAL QUENCHING 1
Gene name
Name: VDE1
Synonyms: AVDE1, NPQ1, VXDE
OrderedLocusNames: At1g08550
ORFNames: F22O13.3, T27G7.23
From
Arabidopsis thaliana (Mouse-ear cress) [TaxID: 3702] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia;
DOI=10.1074/jbc.273.25.15321; PubMed=9624110 [NCBI, ExPASy, EBI, Israel, Japan]
Bugos R.C., Hieber A.D., Yamamoto H.Y.;
"Xanthophyll cycle enzymes are members of the lipocalin family, the first identified from plants.";
J. Biol. Chem. 273:15321-15324(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/35048500; PubMed=11130712 [NCBI, ExPASy, EBI, Israel, Japan]
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
Nature 408:816-820(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
DOI=10.1126/science.1088305; PubMed=14593172 [NCBI, ExPASy, EBI, Israel, Japan]
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis genome.";
Science 302:842-846(2003).
[4]
MUTAGENESIS OF CYS-185, AND FUNCTION.
STRAIN=cv. Columbia;
DOI=10.1105/tpc.10.7.1121; PubMed=9668132 [NCBI, ExPASy, EBI, Israel, Japan]
Niyogi K.K., Grossman A.R., Bjorkman O.;
"Arabidopsis mutants define a central role for the xanthophyll cycle in the regulation of photosynthetic energy conversion.";
Plant Cell 10:1121-1134(1998).
[5]
FUNCTION.
DOI=10.1104/pp.124.1.273; PubMed=10982442 [NCBI, ExPASy, EBI, Israel, Japan]
Havaux M., Bonfils J.-P., Luetz C., Niyogi K.K.;
"Photodamage of the photosynthetic apparatus and its dependence on the leaf developmental stage in the npq1 Arabidopsis mutant deficient in the xanthophyll cycle enzyme violaxanthin de-epoxidase.";
Plant Physiol. 124:273-284(2000).
[6]
DOMAIN, AND FUNCTION.
DOI=10.1007/s00425-001-0704-2; PubMed=11855651 [NCBI, ExPASy, EBI, Israel, Japan]
Hieber A.D., Bugos R.C., Verhoeven A.S., Yamamoto H.Y.;
"Overexpression of violaxanthin de-epoxidase: properties of C-terminal deletions on activity and pH-dependent lipid binding.";
Planta 214:476-483(2002).
[7]
ENZYME REGULATION.
DOI=10.1104/pp.010924; PubMed=11891252 [NCBI, ExPASy, EBI, Israel, Japan]
Mueller-Moule P., Conklin P.L., Niyogi K.K.;
"Ascorbate deficiency can limit violaxanthin de-epoxidase activity in vivo.";
Plant Physiol. 128:970-977(2002).
[8]
ENZYME REGULATION.
DOI=10.1093/pcp/pch010; PubMed=14749490 [NCBI, ExPASy, EBI, Israel, Japan]
Hieber A.D., Kawabata O., Yamamoto H.Y.;
"Significance of the lipid phase in the dynamics and functions of the xanthophyll cycle as revealed by PsbS overexpression in tobacco and in-vitro de-epoxidation in monogalactosyldiacylglycerol micelles.";
Plant Cell Physiol. 45:92-102(2004).
[9]
ENZYME REGULATION.
DOI=10.1007/s00425-006-0257-5; PubMed=16532316 [NCBI, ExPASy, EBI, Israel, Japan]
Yamamoto H.Y.;
"Functional roles of the major chloroplast lipids in the violaxanthin cycle.";
Planta 224:719-724(2006).
Comments
  • FUNCTION: Part of the xanthophyll (or violaxanthin) cycle for controlling the concentration of zeaxanthin in chloroplasts. Catalyzes the two-step mono de-epoxidation reaction. Stereospecific for all-trans xanthophylls. Zeaxanthin induces the dissipation of excitation energy in the chlorophyll of the light-harvesting protein complex of photosystem II.
  • CATALYTIC ACTIVITY: Violaxanthin + ascorbate = antheraxanthin + dehydroascorbate + H2O.
  • CATALYTIC ACTIVITY: Antheraxanthin + ascorbate = zeaxanthin + dehydroascorbate + H2O.
  • ENZYME REGULATION: Activity limitted by low ascorbate availability. Feedback inhibition by zeaxanthin. Requires the presence of micelle-forming lipids such as monogalactosyldiacylglyceride (MGDG). Low concentration of bilayer forming lipids, such as digalactosyldiacylglyceride (DGDG) or phosphatidylcholine, supports a slower but nearly complete activity.
  • SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Peripheral membrane protein; Lumenal side (By similarity).
  • DOMAIN: The cysteine rich N-terminal region is required for activity.
  • MISCELLANEOUS: The amount of VDE in vivo is estimated to be 1 molecule per 20-100 electron transport chains.
  • SIMILARITY: Belongs to the calycin superfamily. Lipocalin 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
U44133; AAC50032.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE005172; AAF99753.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC006932; AAF22898.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY063067; AAL34241.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF370251; AAK44066.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T00708; T00708.
RefSeq NP_001031000.1; -.
NP_172331.1; -.
UniGene At.20930
3D structure databases
ModBase Q39249.
Organism-specific databases
TAIR At1g08550; -.
Gene expression databases
ArrayExpress Q39249; -.
Ontologies
GO
GO:0009507; Cellular component: chloroplast (inferred from direct assay from TAIR).
GO:0031977; Cellular component: thylakoid lumen (inferred from direct assay from TAIR).
QuickGo view.
Family and domain databases
InterPro IPR012674; Calycin.
IPR002345; Lipocalin.
IPR010788; VDE.
Graphical view of domain structure.
Gene3D G3DSA:2.40.128.20; Calycin; 1.
Pfam PF07137; VDE; 1.
Pfam graphical view of domain structure.
PROSITE PS00213; LIPOCALIN; 1.
BLOCKS Q39249.
ProtoNet Q39249.
Genome annotation databases
GeneID 837377; -.
GenomeReviews CT485782_GR; AT1G08550.
KEGG ath:AT1G08550; -.
NMPDR fig|3702.1.peg.1063; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Chloroplast; Coiled coil; Complete proteome; Membrane; Oxidoreductase; Plastid; Thylakoid; Transit peptide.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
TRANSIT   1     ?        Chloroplast (Potential). 
TRANSIT   ?   113        Thylakoid. 
CHAIN   114   462  349     Violaxanthin de-epoxidase, chloroplastic. PRO_5000144817
REGION   380   391  12     Involved in the binding to the thylakoid membrane. 
COILED   372   437  66     Potential. 
COMPBIAS   120   163  44     Cys-rich. 
MUTAGEN   185   185        C->Y: In npq1-1; loss of activity. 
Sequence information
Length: 462 AA [This is the length of the unprocessed precursor] Molecular weight: 52017 Da [This is the MW of the unprocessed precursor] CRC64: 58E37B2C12D4426B [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAVATHCFTS PCHDRIRFFS SDDGIGRLGI TRKRINGTFL LKILPPIQSA DLRTTGGRSS 

        70         80         90        100        110        120 
RPLSAFRSGF SKGIFDIVPL PSKNELKELT APLLLKLVGV LACAFLIVPS ADAVDALKTC 

       130        140        150        160        170        180 
ACLLKGCRIE LAKCIANPAC AANVACLQTC NNRPDETECQ IKCGDLFENS VVDEFNECAV 

       190        200        210        220        230        240 
SRKKCVPRKS DLGEFPAPDP SVLVQNFNIS DFNGKWYITS GLNPTFDAFD CQLHEFHTEG 

       250        260        270        280        290        300 
DNKLVGNISW RIKTLDSGFF TRSAVQKFVQ DPNQPGVLYN HDNEYLHYQD DWYILSSKIE 

       310        320        330        340        350        360 
NKPEDYIFVY YRGRNDAWDG YGGAVVYTRS SVLPNSIIPE LEKAAKSIGR DFSTFIRTDN 

       370        380        390        400        410        420 
TCGPEPALVE RIEKTVEEGE RIIVKEVEEI EEEVEKEVEK VGRTEMTLFQ RLAEGFNELK 

       430        440        450        460 
QDEENFVREL SKEEMEFLDE IKMEASEVEK LFGKALPIRK VR 

Q39249 in FASTA format

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