VDE_SPIOL
ID VDE_SPIOL Reviewed; 472 AA.
AC Q9SM43;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 2.
DT 25-MAY-2022, entry version 77.
DE RecName: Full=Violaxanthin de-epoxidase, chloroplastic {ECO:0000303|Ref.2};
DE EC=1.23.5.1 {ECO:0000269|Ref.1, ECO:0000269|Ref.2};
DE Flags: Precursor;
GN Name=VDE1 {ECO:0000303|Ref.2}; Synonyms=SVDE1;
OS Spinacia oleracea (Spinach).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX NCBI_TaxID=3562;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF HIS-245; HIS-248; HIS-291 AND
RP HIS-297, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC TISSUE=Leaf;
RX DOI=10.1034/j.1399-3054.2003.00151.x;
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 [2]
RP PROTEIN SEQUENCE OF 125-144, AND CATALYTIC ACTIVITY.
RX DOI=10.1007/BF00117662;
RA Arvidsson P.-O., Bratt C.E., Carlsson M., Aakerlund H.-E.;
RT "Purification and identification of the violaxanthin deepoxidase as a 43
RT kDa protein.";
RL Photosyn. Res. 49:119-129(1996).
RN [3]
RP SUBCELLULAR LOCATION, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX DOI=10.1007/BF00203597;
RA Hager A., Holocher K.;
RT "Localization of the xanthophyll-cycle enzyme violaxanthin de-epoxidase
RT within the thylakoid lumen and abolition of its mobility by a (light-
RT dependent) pH decrease.";
RL Planta 192:581-589(1994).
RN [4]
RP SUBCELLULAR LOCATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX DOI=10.1007/BF00032588;
RA Bratt C.E., Arvidsson P.-O., Carlsson M., Aakerlund H.-E.;
RT "Regulation of violaxanthin de-epoxidase activity by pH and ascorbate
RT concentration.";
RL Photosyn. Res. 45:169-175(1995).
RN [5]
RP ACTIVITY REGULATION.
RX DOI=10.1023/A:1005868026374;
RA Arvidsson P.-O., Carlsson M., Stefansson H., Albertsson P.-A.,
RA Aakerlund H.-E.;
RT "Violaxanthin accessibility and temperature dependency for de-epoxidation
RT in spinach thylakoid membranes.";
RL Photosyn. Res. 52:39-48(1997).
RN [6]
RP ACTIVITY REGULATION.
RX PubMed=16228481; DOI=10.1023/a:1006496719927;
RA Pan R.-S., Dilley R.A.;
RT "Influence of Ca(2+) on the thylakoid lumen violaxanthin de-epoxidase
RT activity through Ca(2+) gating of H(+) flux at the CF(o) H(+) channel.";
RL Photosyn. Res. 65:141-154(2000).
RN [7]
RP ACTIVITY REGULATION.
RX PubMed=15078086; DOI=10.1021/bi049652g;
RA Latowski D., Aakerlund H.-E., Strzalka K.;
RT "Violaxanthin de-epoxidase, the xanthophyll cycle enzyme, requires lipid
RT inverted hexagonal structures for its activity.";
RL Biochemistry 43:4417-4420(2004).
RN [8]
RP ACTIVITY REGULATION.
RX PubMed=17618598; DOI=10.1016/j.bbamem.2007.06.001;
RA Szilagyi A., Sommarin M., Akerlund H.E.;
RT "Membrane curvature stress controls the maximal conversion of violaxanthin
RT to zeaxanthin in the violaxanthin cycle--influence of alpha-tocopherol,
RT cetylethers, linolenic acid, and temperature.";
RL Biochim. Biophys. Acta 1768:2310-2318(2007).
RN [9]
RP MUTAGENESIS OF CYS-131; CYS-133; CYS-138; CYS-145; CYS-151; CYS-157;
RP CYS-161; CYS-170; CYS-174; CYS-189; CYS-196; CYS-242 AND CYS-372, AND
RP DISULFIDE BOND.
RX PubMed=25764016; DOI=10.1007/s11120-015-0118-9;
RA Hallin E.I., Guo K., Aakerlund H.E.;
RT "Violaxanthin de-epoxidase disulphides and their role in activity and
RT thermal stability.";
RL Photosyn. Res. 124:191-198(2015).
CC -!- FUNCTION: Part of the xanthophyll (or violaxanthin) cycle for
CC controlling the concentration of zeaxanthin in chloroplasts. Catalyzes
CC the two-step mono de-epoxidation reaction. Stereospecific for all-trans
CC xanthophylls. Zeaxanthin induces the dissipation of excitation energy
CC in the chlorophyll of the light-harvesting protein complex of
CC photosystem II.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-violaxanthin + 2 L-ascorbate = all-trans-zeaxanthin
CC + 2 H2O + 2 L-dehydroascorbate; Xref=Rhea:RHEA:32371,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:27547, ChEBI:CHEBI:35288,
CC ChEBI:CHEBI:38290, ChEBI:CHEBI:58539; EC=1.23.5.1;
CC Evidence={ECO:0000269|Ref.1};
CC -!- ACTIVITY REGULATION: Irreversibly inhibited by DTT and iodoacetamide at
CC pH 5.7 or pH 5.2, but not at pH 7.2 (Ref.5, Ref.3). Regulated through
CC Ca(2+) gating of H(+) flux at the CFoH(+) channel (PubMed:16228481).
CC Requires the presence of lipids forming reverse hexagonal structures
CC such as monogalactosyldiacylglyceride (MGDG) or
CC phosphatidylethanolamine (PubMed:15078086). A negative curvature
CC elastic stress in the thylakoid lipid bilayer is required for VDE1
CC activity (PubMed:17618598). {ECO:0000269|PubMed:15078086,
CC ECO:0000269|PubMed:16228481, ECO:0000269|PubMed:17618598,
CC ECO:0000269|Ref.3, ECO:0000269|Ref.5}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=10 mM for ascorbate at pH 6.0 {ECO:0000269|Ref.4};
CC KM=2.5 mM for ascorbate at pH 5.5 {ECO:0000269|Ref.4};
CC KM=1 mM for ascorbate at pH 5.0 {ECO:0000269|Ref.4};
CC KM=0.3 mM for ascorbate at pH 4.5 {ECO:0000269|Ref.4};
CC Note=KM for ascorbate increased when H-245, H-248, H-291 or H-297 are
CC mutated. {ECO:0000269|Ref.1};
CC pH dependence:
CC Optimum pH is 5.0. {ECO:0000269|Ref.3};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000269|Ref.3, ECO:0000269|Ref.4}; Peripheral membrane protein
CC {ECO:0000269|Ref.3, ECO:0000269|Ref.4}; Lumenal side
CC {ECO:0000269|Ref.3, ECO:0000269|Ref.4}. Note=Binds to the thylakoid
CC membrane at pH 5.2 and is released in the lumen at pH 7.2.
CC {ECO:0000269|Ref.3}.
CC -!- PTM: Disulfide bonds. Reduction of the disulfides results in loss of a
CC rigid structure, a decrease in thermal stability of 15 degrees Celsius
CC and a loss of activity. {ECO:0000269|PubMed:25764016}.
CC -!- MISCELLANEOUS: The amount of VDE in vivo is estimated to be 1 molecule
CC per 20-100 electron transport chains. {ECO:0000305|Ref.2}.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC {ECO:0000305}.
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DR EMBL; AJ250433; CAB59211.2; -; mRNA.
DR AlphaFoldDB; Q9SM43; -.
DR SMR; Q9SM43; -.
DR PRIDE; Q9SM43; -.
DR KEGG; ag:CAB59211; -.
DR OrthoDB; 489088at2759; -.
DR BRENDA; 1.23.5.1; 5812.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046422; F:violaxanthin de-epoxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0010028; P:xanthophyll cycle; IEA:InterPro.
DR Gene3D; 2.40.128.20; -; 1.
DR InterPro; IPR012674; Calycin.
DR InterPro; IPR044682; VDE.
DR InterPro; IPR010788; VDE_dom.
DR PANTHER; PTHR33970; PTHR33970; 1.
DR Pfam; PF07137; VDE; 1.
DR SUPFAM; SSF50814; SSF50814; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Coiled coil; Direct protein sequencing; Disulfide bond;
KW Membrane; Oxidoreductase; Plastid; Thylakoid; Transit peptide.
FT TRANSIT 1..?
FT /note="Chloroplast"
FT TRANSIT ?..124
FT /note="Thylakoid"
FT /evidence="ECO:0000269|Ref.2"
FT CHAIN 125..472
FT /note="Violaxanthin de-epoxidase, chloroplastic"
FT /id="PRO_0000273251"
FT COILED 379..462
FT /evidence="ECO:0000255"
FT DISULFID 133..151
FT /evidence="ECO:0000269|PubMed:25764016"
FT DISULFID 138..145
FT /evidence="ECO:0000269|PubMed:25764016"
FT DISULFID 157..174
FT /evidence="ECO:0000269|PubMed:25764016"
FT DISULFID 161..170
FT /evidence="ECO:0000269|PubMed:25764016"
FT DISULFID 189..196
FT /evidence="ECO:0000269|PubMed:25764016"
FT DISULFID 242..372
FT /evidence="ECO:0000269|PubMed:25764016"
FT MUTAGEN 131
FT /note="C->S: No effect on activity."
FT /evidence="ECO:0000269|PubMed:25764016"
FT MUTAGEN 133
FT /note="C->S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:25764016"
FT MUTAGEN 138
FT /note="C->S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:25764016"
FT MUTAGEN 145
FT /note="C->S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:25764016"
FT MUTAGEN 151
FT /note="C->S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:25764016"
FT MUTAGEN 157
FT /note="C->S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:25764016"
FT MUTAGEN 161
FT /note="C->S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:25764016"
FT MUTAGEN 170
FT /note="C->S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:25764016"
FT MUTAGEN 174
FT /note="C->S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:25764016"
FT MUTAGEN 189
FT /note="C->S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:25764016"
FT MUTAGEN 196
FT /note="C->S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:25764016"
FT MUTAGEN 242
FT /note="C->S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:25764016"
FT MUTAGEN 245
FT /note="H->A: 55% loss of activity; when associated with A-
FT 248. Total loss of activity; when associated with A-248; A-
FT 291 and R-297."
FT /evidence="ECO:0000269|Ref.1"
FT MUTAGEN 245
FT /note="H->R: Total loss of activity; when associated with
FT R-248. Total loss of activity; when associated with R-248;
FT R-291 and R-297."
FT /evidence="ECO:0000269|Ref.1"
FT MUTAGEN 248
FT /note="H->A: 40% loss of activity. 55% loss of activity;
FT when associated with A-245. Total loss of activity; when
FT associated with A-245; A-291 and R-297."
FT /evidence="ECO:0000269|Ref.1"
FT MUTAGEN 248
FT /note="H->R: No effect. Total loss of activity; when
FT associated with R-245. Total loss of activity; when
FT associated with R-245; R-291 and R-297."
FT /evidence="ECO:0000269|Ref.1"
FT MUTAGEN 291
FT /note="H->A: 99% loss of activity. Total loss of activity;
FT when associated with A-245; A-248 and A-297."
FT /evidence="ECO:0000269|Ref.1"
FT MUTAGEN 291
FT /note="H->R: 55% loss of activity; when associated with R-
FT 297. Total loss of activity; when associated with R-245; R-
FT 248 and R-297."
FT /evidence="ECO:0000269|Ref.1"
FT MUTAGEN 297
FT /note="H->R: 55% loss of activity; when associated with R-
FT 291. Total loss of activity; when associated with R-245; R-
FT 248 and R-291. Total loss of activity; when associated with
FT A-245; A-248 and A-291."
FT /evidence="ECO:0000269|Ref.1"
FT MUTAGEN 372
FT /note="C->S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:25764016"
SQ SEQUENCE 472 AA; 53667 MW; 03C48EDE108BEEDB CRC64;
MALVARSICV SYDEIAGICN NVSHRNFKKW VQWKNPFLFQ DDARRNIRFN DRKLSCTKFI
GASEKLQHSK SPKSGLISCG WEVNSSKVVS NAVIPKKWNL LKLKVVEVTA IVACTFFVMS
SAQAVDALKT CTCLLKECRI ELAKCIANPS CAANVACLQT CNNRPDETEC QIKCGDLFAN
KVVDEFNECA VSRKKCVPQK SDVGEFPVPD PSVLVKSFNM ADFNGKWFIS SGLNPTFDAF
DCQLHEFHLE DGKLVGNLSW RIKTPDGGFF TRTAVQKFAQ DPSQPGMLYN HDNAYLHYQD
DWYILSSKIE NQPDDYVFVY YRGRNDAWDG YGGAFLYTRS ATVPENIVPE LNRAAQSVGK
DFNKFIRTDN TCGPEPPLVE RLEKTVEEGE RTIIKEVEQL EGEIEGDLEK VGKTEMTLFQ
RLLEGFQELQ KDEEYFLKEL NKEERELLED LKMEAGEVEK LFGRALPIRK LR
