ID   VDE_LACSA               Reviewed;         473 AA.
AC   Q40251;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 48.
DE   RecName: Full=Violaxanthin de-epoxidase, chloroplastic;
DE            EC=1.10.99.3;
DE   Flags: Precursor;
GN   Name=VDE1;
OS   Lactuca sativa (Garden lettuce).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   asterids; campanulids; Asterales; Asteraceae; Cichorioideae;
OC   Cichorieae; Lactuca.
OX   NCBI_TaxID=4236;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, AND FUNCTION.
RC   STRAIN=cv. Romaine;
RX   MEDLINE=96270536; PubMed=8692813; DOI=10.1073/pnas.93.13.6320;
RA   Bugos R.C., Yamamoto H.Y.;
RT   "Molecular cloning of violaxanthin de-epoxidase from romaine lettuce
RT   and expression in Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:6320-6325(1996).
RN   [2]
RP   PROTEIN SEQUENCE OF 126-138; 265-272; 275-289 AND 341-353, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=cv. Romaine;
RX   PubMed=8742341; DOI=10.1104/pp.110.2.697;
RA   Rockholm D.C., Yamamoto H.Y.;
RT   "Violaxanthin de-epoxidase.";
RL   Plant Physiol. 110:697-703(1996).
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   -!- ENZYME REGULATION: Inhibited by DTT.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.352 uM for violaxanthin;
CC         KM=4.4 mM for ascorbate;
CC         Note=reaction significantly slower in the absence of
CC         monogalactosyldiacylglyceride;
CC       pH dependence:
CC         Optimum pH is 5.0;
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane;
CC       Peripheral membrane protein; Lumenal side (By similarity).
CC   -!- DEVELOPMENTAL STAGE: Low constitutive expression in etiolated
CC       seedlings and immature yellow leaves. Higher expression in mature
CC       green leaves.
CC   -!- MISCELLANEOUS: Associates specificaly at acidic pH with
CC       monogalactosyldiacylglyceride (MGDG), the major lipid of
CC       thylakoids.
CC   -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
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DR   EMBL; U31462; AAC49373.1; -; mRNA.
DR   BioCyc; MetaCyc:MON-2561; -.
DR   BRENDA; 1.10.99.3; 1470.
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   1: Evidence at protein level;
KW   Chloroplast; Coiled coil; Direct protein sequencing; Membrane;
KW   Oxidoreductase; Plastid; Thylakoid; Transit peptide.
FT   TRANSIT       1      ?       Chloroplast (Potential).
FT   TRANSIT       ?    125       Thylakoid.
FT   CHAIN       126    473       Violaxanthin de-epoxidase, chloroplastic.
FT                                /FTId=PRO_5000144686.
FT   COILED      383    463       Potential.
FT   COMPBIAS    132    175       Cys-rich.
SQ   SEQUENCE   473 AA;  54448 MW;  1B22522DC2C62699 CRC64;
     MALSLHTVFL CKEEALNLYA RSPCNERFHR SGQPPTNIIM MKIRSNNGYF NSFRLFTSYK
     TSSFSDSSHC KDKSQICSID TSFEEIQRFD LKRGMTLILE KQWRQFIQLA IVLVCTFVIV
     PRVDAVDALK TCACLLKECR IELAKCIANP SCAANVACLQ TCNNRPDETE CQIKCGDLFE
     NSVVDQFNEC AVSRKKCVPR KSDVGEFPVP DRNAVVQNFN MKDFSGKWYI TSGLNPTFDA
     FDCQLHEFHM ENDKLVGNLT WRIKTLDGGF FTRSAVQTFV QDPDLPGALY NHDNEFLHYQ
     DDWYILSSQI ENKPDDYIFV YYRGRNDAWD GYGGSVIYTR SPTLPESIIP NLQKAAKSVG
     RDFNNFITTD NSCGPEPPLV ERLEKTAEEG EKLLIKEAVE IEEEVEKEVE KVRDTEMTLF
     QRLLEGFKEL QQDEENFVRE LSKEEKEILN ELQMEATEVE KLFGRALPIR KLR
//