ID   VDE_TOBAC               Reviewed;         478 AA.
AC   Q40593;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 49.
DE   RecName: Full=Violaxanthin de-epoxidase, chloroplastic;
DE            EC=1.10.99.3;
DE   Flags: Precursor;
GN   Name=VDE1; Synonyms=TVDE1;
OS   Nicotiana tabacum (Common tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Xanthi; TISSUE=Leaf;
RX   MEDLINE=98288256; PubMed=9624110; DOI=10.1074/jbc.273.25.15321;
RA   Bugos R.C., Hieber A.D., Yamamoto H.Y.;
RT   "Xanthophyll cycle enzymes are members of the lipocalin family, the
RT   first identified from plants.";
RL   J. Biol. Chem. 273:15321-15324(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Emanuelsson A.K., Eskling M., Aakerlund H.-E.;
RT   "Chemical and mutational modification of histidines in violaxanthinde-
RT   epoxidase from Spinacia oleracea.";
RL   Physiol. Plantarum 119:97-104(2003).
RN   [3]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=10482676; DOI=10.1104/pp.121.1.207;
RA   Bugos R.C., Chang S.-H., Yamamoto H.Y.;
RT   "Developmental expression of violaxanthin de-epoxidase in leaves of
RT   tobacco growing under high and low light.";
RL   Plant Physiol. 121:207-214(1999).
CC   -!- FUNCTION: Part of the xanthophyll (or violaxanthin) cycle for
CC       controlling the concentration of zeaxanthin in chloroplasts.
CC       Catalyzes the two-step mono de-epoxidation reaction.
CC       Stereospecific for all-trans xanthophylls. Zeaxanthin induces the
CC       dissipation of excitation energy in the chlorophyll of the light-
CC       harvesting protein complex of photosystem II.
CC   -!- CATALYTIC ACTIVITY: Violaxanthin + ascorbate = antheraxanthin +
CC       dehydroascorbate + H(2)O.
CC   -!- CATALYTIC ACTIVITY: Antheraxanthin + ascorbate = zeaxanthin +
CC       dehydroascorbate + H(2)O.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane;
CC       Peripheral membrane protein; Lumenal side (By similarity).
CC   -!- DEVELOPMENTAL STAGE: Low expression in young leaves, but high
CC       expression in older leaves.
CC   -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
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DR   EMBL; U34817; AAC50031.1; -; mRNA.
DR   PIR; T03750; T03750.
DR   BRENDA; 1.10.99.3; 298.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0005215; F:transporter activity; IEA:InterPro.
DR   GO; GO:0046422; F:violaxanthin de-epoxidase activity; IEA:EC.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:InterPro.
DR   InterPro; IPR012674; Calycin.
DR   InterPro; IPR002345; Lipocalin.
DR   InterPro; IPR010788; VDE.
DR   Gene3D; G3DSA:2.40.128.20; Calycin; 1.
DR   Pfam; PF07137; VDE; 1.
DR   PROSITE; PS00213; LIPOCALIN; 1.
PE   2: Evidence at transcript level;
KW   Chloroplast; Coiled coil; Membrane; Oxidoreductase; Plastid;
KW   Thylakoid; Transit peptide.
FT   TRANSIT       1      ?       Chloroplast (Potential).
FT   TRANSIT       ?    134       Thylakoid.
FT   CHAIN       135    478       Violaxanthin de-epoxidase, chloroplastic.
FT                                /FTId=PRO_5000144729.
FT   COILED      388    453       Potential.
FT   COMPBIAS    141    184       Cys-rich.
FT   CONFLICT    307    307       L -> H (in Ref. 2).
SQ   SEQUENCE   478 AA;  54561 MW;  0967DF4547D7809D CRC64;
     MALAPHSNFL ANHETIKYYV GSKLPGHKRF SWGWEDYFGS IVVAKICSSR RIPRYFRKSP
     RICCGLDSRG LQLFSHGKHN LSPAHSINQN VPKGNSGCKF PKDVALMVWE KWGQFAKTAI
     VAIFILSVAS KADAVDALKT CTCLLKECRL ELAKCISNPA CAANVACLQT CNNRPDETEC
     QIKCGDLFEN SVVDEFNECA VSRKKCVPRK SDVGDFPVPD PSVLVQKFDM KDFSGKWFIT
     RGLNPTFDAF DCQLHEFHTE ENKLVGNLSW RIRTPDGGFF TRSAVQKFVQ DPKYPGILYN
     HDNEYLLYQD DWYILSSKVE NSPEDYIFVY YKGRNDAWDG YGGSVLYTRS AVLPESIIPE
     LQTAAQKVGR DFNTFIKTDN TCGPEPPLVE RLEKKVEEGE RTIIKEVEEI EEEVEKVRDK
     EVTLFSKLFE GFKELQRDEE NFLRELSKEE MDVLDGLKME ATEVEKLFGR ALPIRKLR
//