VDE_LACSA
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 03-AUG-2022, entry version 88.
DE RecName: Full=Violaxanthin de-epoxidase, chloroplastic;
DE EC=1.23.5.1 {ECO:0000269|PubMed:8742341};
DE Flags: Precursor;
GN Name=VDE1;
OS Lactuca sativa (Garden lettuce).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Cichorioideae; Cichorieae;
OC Lactucinae; Lactuca.
OX NCBI_TaxID=4236;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, FUNCTION, AND CATALYTIC
RP ACTIVITY.
RC STRAIN=cv. Romaine;
RX 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 and
RT 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,
RP BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, AND FUNCTION.
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. 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. {ECO:0000269|PubMed:8692813,
CC ECO:0000269|PubMed:8742341}.
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|PubMed:8692813, ECO:0000269|PubMed:8742341};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-violaxanthin + L-ascorbate = all-trans-
CC antheraxanthin + H2O + L-dehydroascorbate; Xref=Rhea:RHEA:15353,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:27867, ChEBI:CHEBI:35288,
CC ChEBI:CHEBI:38290, ChEBI:CHEBI:58539;
CC Evidence={ECO:0000269|PubMed:8692813};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-antheraxanthin + L-ascorbate = all-trans-zeaxanthin
CC + H2O + L-dehydroascorbate; Xref=Rhea:RHEA:21800, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:27547, ChEBI:CHEBI:27867, ChEBI:CHEBI:38290,
CC ChEBI:CHEBI:58539; Evidence={ECO:0000269|PubMed:8692813};
CC -!- ACTIVITY REGULATION: Inhibited by DTT.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.352 uM for violaxanthin {ECO:0000269|PubMed:8742341};
CC KM=4.4 mM for ascorbate {ECO:0000269|PubMed:8742341};
CC Note=reaction significantly slower in the absence of
CC monogalactosyldiacylglyceride.;
CC pH dependence:
CC Optimum pH is 5.0. {ECO:0000269|PubMed:8742341};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Lumenal side
CC {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Low constitutive expression in etiolated seedlings
CC and immature yellow leaves. Higher expression in mature green leaves.
CC {ECO:0000269|PubMed:8692813}.
CC -!- MISCELLANEOUS: Associates specifically at acidic pH with
CC monogalactosyldiacylglyceride (MGDG), the major lipid of thylakoids.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC {ECO:0000305}.
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DR EMBL; U31462; AAC49373.1; -; mRNA.
DR AlphaFoldDB; Q40251; -.
DR SMR; Q40251; -.
DR SwissLipids; SLP:000001489; -.
DR EnsemblPlants; rna-gnl|WGS:NBSK|LSAT_7X62281_mrna; cds-PLY68074.1; gene-LSAT_7X62281.
DR Gramene; rna-gnl|WGS:NBSK|LSAT_7X62281_mrna; cds-PLY68074.1; gene-LSAT_7X62281.
DR KEGG; ag:AAC49373; -.
DR OrthoDB; 489088at2759; -.
DR BioCyc; MetaCyc:MON-2561; -.
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; IPR022272; Lipocalin_CS.
DR InterPro; IPR044682; VDE.
DR InterPro; IPR010788; VDE_dom.
DR PANTHER; PTHR33970; PTHR33970; 1.
DR Pfam; PF07137; VDE; 1.
DR SUPFAM; SSF50814; SSF50814; 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..?
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT TRANSIT ?..125
FT /note="Thylakoid"
FT /evidence="ECO:0000269|PubMed:8742341"
FT CHAIN 126..473
FT /note="Violaxanthin de-epoxidase, chloroplastic"
FT /id="PRO_5000144686"
FT COILED 383..463
FT /evidence="ECO:0000255"
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
