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[1]
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NUCLEOTIDE SEQUENCE [MRNA], AND MUTAGENESIS OF HIS-245; HIS-248; HIS-291 AND HIS-297.
TISSUE=Leaf;
Emanuelsson A.K.,
Eskling M.,
Aakerlund H.-E.;
"Chemical and mutational modification of histidines in violaxanthinde-epoxidase from Spinacia oleracea.";
Physiol. Plantarum 119:97-104(2003).
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[2]
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PROTEIN SEQUENCE OF 125-144.
Arvidsson P.-O.,
Bratt C.E.,
Carlsson M.,
Aakerlund H.-E.;
"Purification and identification of the violaxanthin deepoxidase as a 43 kDa protein.";
Photosyn. Res. 49:119-129(1996).
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[3]
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SUBCELLULAR LOCATION, AND ENZYME REGULATION.
Hager A.,
Holocher K.;
"Localization of the xanthophyll-cycle enzyme violaxanthin de-epoxidase within the thylakoid lumen and abolition of its mobility by a (light-dependent) pH decrease.";
Planta 192:581-589(1994).
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[4]
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SUBCELLULAR LOCATION AND BIOPHYSICOCHEMICAL PROPERTIES.
Bratt C.E.,
Arvidsson P.-O.,
Carlsson M.,
Aakerlund H.-E.;
"Regulation of violaxanthin de-epoxidase activity by pH and ascorbate concentration.";
Photosyn. Res. 45:169-175(1995).
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[5]
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ENZYME REGULATION.
Arvidsson P.-O.,
Carlsson M.,
Stefansson H.,
Albertsson P.-A.,
Aakerlund H.-E.;
"Violaxanthin accessibility and temperature dependency for de-epoxidation in spinach thylakoid membranes.";
Photosyn. Res. 52:39-48(1997).
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[6]
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ENZYME REGULATION.
DOI=10.1023/A:1006496719927; PubMed=16228481 [NCBI, ExPASy, EBI, Israel, Japan]
Pan R.-S.,
Dilley R.A.;
"Influence of Ca(2+) on the thylakoid lumen violaxanthin de-epoxidase activity through Ca(2+) gating of H(+) flux at the CF(o) H(+) channel.";
Photosyn. Res. 65:141-154(2000).
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[7]
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ENZYME REGULATION.
DOI=10.1021/bi049652g; PubMed=15078086 [NCBI, ExPASy, EBI, Israel, Japan]
Latowski D.,
Aakerlund H.-E.,
Strzalka K.;
"Violaxanthin de-epoxidase, the xanthophyll cycle enzyme, requires lipid inverted hexagonal structures for its activity.";
Biochemistry 43:4417-4420(2004).
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- 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.
- CATALYTIC ACTIVITY: Violaxanthin + ascorbate = antheraxanthin + dehydroascorbate + H2O.
- CATALYTIC ACTIVITY: Antheraxanthin + ascorbate = zeaxanthin + dehydroascorbate + H2O.
- ENZYME REGULATION: Irreversibly inhibited by DTT and iodoacetamide at pH 5.7 or pH 5.2, but not at pH 7.2. Regulated through Ca(2+) gating of H(+) flux at the CFoH(+) channel. Requires the presence of lipids forming reverse hexagonal structures such as monogalactosyldiacylglyceride (MGDG) or phosphatidylethanolamine.
- BIOPHYSICOCHEMICAL PROPERTIES:
| Kinetic parameters: |
KM=10 mM for ascorbate at pH 6.0; | | KM=2.5 mM for ascorbate at pH 5.5; | | KM=1 mM for ascorbate at pH 5.0; | | KM=0.3 mM for ascorbate at pH 4.5; | | Note=KM for ascorbate increased when H-245, H-248, H-291 or H- 297 are mutated; | | pH dependence: |
Optimum pH is 5.0; | |
- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Peripheral membrane protein; Lumenal side. Note=Binds to the thylakoid membrane at pH 5.2 and is released in the lumen at pH 7.2.
- MISCELLANEOUS: The amount of VDE in vivo is estimated to be 1 molecule per 20-100 electron transport chains.
- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
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Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
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 Feature table viewer |
 Feature aligner |
| Key | From To | Length | | Description | FTId |
| TRANSIT | 1 ? | | | Chloroplast. | |
| TRANSIT | ? 124 | | | Thylakoid. | |
| CHAIN | 125 472 | 348 | | Violaxanthin de-epoxidase, chloroplastic. | PRO_0000273251 |
| COILED | 379 462 | 84 | | Potential. | |
| COMPBIAS | 131 174 | 44 | | Cys-rich. | |
| MUTAGEN | 245 245 | | | H->A: 55% loss of activity; when associated with A-248. Total loss of activity; when associated with A-248; A-291 and R-297. | |
| MUTAGEN | 245 245 | | | H->R: Total loss of activity; when associated with R-248. Total loss of activity; when associated with R-248; R-291 and R-297. | |
| MUTAGEN | 248 248 | | | H->A: 40% loss of activity. 55% loss of activity; when associated with A-245. Total loss of activity; when associated with A-245; A-291 and R-297. | |
| MUTAGEN | 248 248 | | | H->R: No effect. Total loss of activity; when associated with R-245. Total loss of activity; when associated with R-245; R-291 and R-297. | |
| MUTAGEN | 291 291 | | | H->A: 99% loss of activity. Total loss of activity; when associated with A-245; A-248 and A-297. | |
| MUTAGEN | 291 291 | | | H->R: 55% loss of activity; when associated with R-297. Total loss of activity; when associated with R-245; R-248 and R-297. | |
| MUTAGEN | 297 297 | | | H->R: 55% loss of activity; when associated with R-291. Total loss of activity; when associated with R-245; R-248 and R-291. Total loss of activity; when associated with A-245; A-248 and A-291. | |
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| Length: 472 AA [This is the length of the unprocessed precursor] |
Molecular weight: 53667 Da [This is the MW of the unprocessed precursor] |
CRC64: 03C48EDE108BEEDB [This is a checksum on the sequence] |
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10 20 30 40 50 60
MALVARSICV SYDEIAGICN NVSHRNFKKW VQWKNPFLFQ DDARRNIRFN DRKLSCTKFI
70 80 90 100 110 120
GASEKLQHSK SPKSGLISCG WEVNSSKVVS NAVIPKKWNL LKLKVVEVTA IVACTFFVMS
130 140 150 160 170 180
SAQAVDALKT CTCLLKECRI ELAKCIANPS CAANVACLQT CNNRPDETEC QIKCGDLFAN
190 200 210 220 230 240
KVVDEFNECA VSRKKCVPQK SDVGEFPVPD PSVLVKSFNM ADFNGKWFIS SGLNPTFDAF
250 260 270 280 290 300
DCQLHEFHLE DGKLVGNLSW RIKTPDGGFF TRTAVQKFAQ DPSQPGMLYN HDNAYLHYQD
310 320 330 340 350 360
DWYILSSKIE NQPDDYVFVY YRGRNDAWDG YGGAFLYTRS ATVPENIVPE LNRAAQSVGK
370 380 390 400 410 420
DFNKFIRTDN TCGPEPPLVE RLEKTVEEGE RTIIKEVEQL EGEIEGDLEK VGKTEMTLFQ
430 440 450 460 470
RLLEGFQELQ KDEEYFLKEL NKEERELLED LKMEAGEVEK LFGRALPIRK LR
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Q9SM43 in FASTA format |
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