Reviewed, UniProtKB/Swiss-Prot Q40251 (VDE_LACSA)

Names and origin

Protein names

Recommended name:
    Violaxanthin de-epoxidase, chloroplastic
    EC=1.10.99.3

Gene names

Name:

VDE1

Organism

Lactuca sativa (Garden lettuce)

Taxonomic identifier

4236 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › campanulids › Asterales › Asteraceae › Cichorioideae › Cichorieae › Lactuca

Protein attributes

Sequence length	473 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (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. Ref.1
Catalytic activity	Violaxanthin + ascorbate = antheraxanthin + dehydroascorbate + H2O. Antheraxanthin + ascorbate = zeaxanthin + dehydroascorbate + H2O.
Enzyme regulation	Inhibited by DTT.
Subcellular location	Plastid › chloroplast thylakoid membrane; Peripheral membrane protein; Lumenal side By similarity.
Developmental stage	Low constitutive expression in etiolated seedlings and immature yellow leaves. Higher expression in mature green leaves. Ref.1
Miscellaneous	Associates specificaly at acidic pH with monogalactosyldiacylglyceride (MGDG), the major lipid of thylakoids.
Sequence similarities	Belongs to the calycin superfamily. Lipocalin family.
Biophysicochemical properties	Kinetic parameters: reaction significantly slower in the absence of monogalactosyldiacylglyceride. KM=0.352 µM for violaxanthin KM=4.4 mM for ascorbate pH dependence: Optimum pH is 5.0.

Ontologies

Keywords
Cellular component	Chloroplast Membrane Plastid Thylakoid
Domain	Coiled coil Transit peptide
Molecular function	Oxidoreductase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW transport Inferred from electronic annotation. Source: InterPro
Cellular component	chloroplast Inferred from electronic annotation. Source: UniProtKB-KW extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell thylakoid Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	binding Inferred from electronic annotation. Source: InterPro transporter activity Inferred from electronic annotation. Source: InterPro violaxanthin de-epoxidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – ?		Chloroplast Potential
	Transit peptide	? – 125		Thylakoid Ref.2
	Chain	126 – 473	348	Violaxanthin de-epoxidase, chloroplastic		PRO_5000144686
Regions
	Coiled coil	383 – 463	81	Potential
	Compositional bias	132 – 175	44	Cys-rich

Sequences

	Sequence		Length	Mass (Da)
	Q40251-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 1B22522DC2C62699	FASTA	473	54,448
	10 20 30 40 50 60 MALSLHTVFL CKEEALNLYA RSPCNERFHR SGQPPTNIIM MKIRSNNGYF NSFRLFTSYK 70 80 90 100 110 120 TSSFSDSSHC KDKSQICSID TSFEEIQRFD LKRGMTLILE KQWRQFIQLA IVLVCTFVIV 130 140 150 160 170 180 PRVDAVDALK TCACLLKECR IELAKCIANP SCAANVACLQ TCNNRPDETE CQIKCGDLFE 190 200 210 220 230 240 NSVVDQFNEC AVSRKKCVPR KSDVGEFPVP DRNAVVQNFN MKDFSGKWYI TSGLNPTFDA 250 260 270 280 290 300 FDCQLHEFHM ENDKLVGNLT WRIKTLDGGF FTRSAVQTFV QDPDLPGALY NHDNEFLHYQ 310 320 330 340 350 360 DDWYILSSQI ENKPDDYIFV YYRGRNDAWD GYGGSVIYTR SPTLPESIIP NLQKAAKSVG 370 380 390 400 410 420 RDFNNFITTD NSCGPEPPLV ERLEKTAEEG EKLLIKEAVE IEEEVEKEVE KVRDTEMTLF 430 440 450 460 470 QRLLEGFKEL QQDEENFVRE LSKEEKEILN ELQMEATEVE KLFGRALPIR KLR

References

[1]	"Molecular cloning of violaxanthin de-epoxidase from romaine lettuce and expression in Escherichia coli." Bugos R.C., Yamamoto H.Y. Proc. Natl. Acad. Sci. U.S.A. 93:6320-6325(1996) [PubMed: 8692813] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, FUNCTION. Strain: cv. Romaine.
[2]	"Violaxanthin de-epoxidase." Rockholm D.C., Yamamoto H.Y. Plant Physiol. 110:697-703(1996) [PubMed: 8742341] [Abstract] Cited for: PROTEIN SEQUENCE OF 126-138; 265-272; 275-289 AND 341-353, BIOPHYSICOCHEMICAL PROPERTIES. Strain: cv. Romaine.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U31462 mRNA. Translation: AAC49373.1.
3D structure databases
SMR	Q40251. Positions 214-376.
ModBase	Search...
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-2561.
BRENDA	1.10.99.3. 1470.
Family and domain databases
InterPro	IPR012674. Calycin. IPR011038. Calycin-like. IPR002345. Lipocalin. IPR010788. VDE. [Graphical view]
Gene3D	G3DSA:2.40.128.20. Calycin. 1 hit.
Pfam	PF07137. VDE. 1 hit. [Graphical view]
PROSITE	PS00213. LIPOCALIN. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

VDE_LACSA

Accession

Primary (citable) accession number: Q40251

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 23, 2007
Last sequence update:	November 1, 1996
Last modified:	February 9, 2010
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)