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Protein

Phytol kinase 1, chloroplastic

Gene

VTE5

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Kinase involved in the activation and reutilization of phytol from chlorophyll degradation in plant metabolism, including tocopherol biosynthesis. Catalyzes the conversion of phytol to phytol monophosphate (PMP) in the presence of CTP or UTP. No activity with ATP or GTP as phosphoryl donnor.1 Publication

Catalytic activityi

CTP + phytol = CDP + phytyl phosphate.1 Publication

Pathwayi: tocopherol biosynthesis

This protein is involved in the pathway tocopherol biosynthesis, which is part of Cofactor biosynthesis.2 Publications
View all proteins of this organism that are known to be involved in the pathway tocopherol biosynthesis and in Cofactor biosynthesis.

GO - Molecular functioni

  • phytol kinase activity Source: TAIR

GO - Biological processi

  • vitamin E biosynthetic process Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Enzyme and pathway databases

BioCyciARA:AT5G04490-MONOMER.
MetaCyc:AT5G04490-MONOMER.
BRENDAi2.7.1.182. 399.
UniPathwayiUPA00160.

Names & Taxonomyi

Protein namesi
Recommended name:
Phytol kinase 1, chloroplasticCurated (EC:2.7.1.1821 Publication)
Alternative name(s):
Vitamin E pathway gene 5 protein1 Publication
Gene namesi
Name:VTE51 Publication
Ordered Locus Names:At5g04490Imported
ORF Names:T32M21_90Imported
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G04490.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei71 – 9121HelicalSequence analysisAdd
BLAST
Transmembranei105 – 12521HelicalSequence analysisAdd
BLAST
Transmembranei129 – 14921HelicalSequence analysisAdd
BLAST
Transmembranei167 – 18721HelicalSequence analysisAdd
BLAST
Transmembranei191 – 21121HelicalSequence analysisAdd
BLAST
Transmembranei227 – 24721HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

  • chloroplast Source: TAIR
  • chloroplast membrane Source: UniProtKB-SubCell
  • integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Membrane, Plastid

Pathology & Biotechi

Disruption phenotypei

50% reduction in tocopherol content in leaves. Plants able to grow on soil and to produce fertile seeds. Vte5 and vte6 double mutants can grow photoautotrophically and show a stay-green phenotype with strongly delayed senescence and extended lifetime.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi227 – 30478Missing in lt1/vte5-1; 80% reduction in total seed tocopherols. Add
BLAST

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5959ChloroplastSequence analysisAdd
BLAST
Chaini60 – 304245Phytol kinase 1, chloroplasticPRO_0000226591Add
BLAST

Proteomic databases

PaxDbiQ9LZ76.
PRIDEiQ9LZ76.

Expressioni

Developmental stagei

Highly expressed early in seed development and in 6-week-old senescent leaves.1 Publication

Gene expression databases

GenevisibleiQ9LZ76. AT.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT5G04490.1.

Structurei

3D structure databases

ProteinModelPortaliQ9LZ76.
SMRiQ9LZ76. Positions 170-278.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the polyprenol kinase family.Curated

Keywords - Domaini

Transit peptide, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4453. Eukaryota.
COG0170. LUCA.
HOGENOMiHOG000265019.
InParanoidiQ9LZ76.
KOiK18678.
OMAiGYFQLDW.
PhylomeDBiQ9LZ76.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9LZ76-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAATLPLSPI NHQLCRFGNN SLTTHRFCSP GFLISSPCFI GLTGMGSATQ
60 70 80 90 100
LRARRSLISS AVATNSLLHD VGATVAVLGG AYALVLSFES LTKRNVIQQS
110 120 130 140 150
LSRKLVHILS GLLFVLAWPI FSGSTEARYF AAFVPLVNGL RLVINGLSIS
160 170 180 190 200
PNSMLIKSVT REGRAEELLK GPLFYVLALL FSAVFFWRES PIGMISLAMM
210 220 230 240 250
CGGDGIADIM GRKFGSTKIP YNPRKSWAGS ISMFIFGFFI SIALLYYYSS
260 270 280 290 300
LGYLHMNWET TLQRVAMVSM VATVVESLPI TDQLDDNISV PLATILAAYL

SFGY
Length:304
Mass (Da):33,090
Last modified:October 1, 2000 - v1
Checksum:i770CA569C9F50A50
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti74 – 741T → A in AAO42044 (PubMed:14593172).Curated
Sequence conflicti256 – 2561M → I in AAM61593 (Ref. 4) Curated
Sequence conflicti267 – 2671M → I in AAM61593 (Ref. 4) Curated
Sequence conflicti288 – 2881I → V in AAM61593 (Ref. 4) Curated
Sequence conflicti297 – 2971A → T in AAM61593 (Ref. 4) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL162875 Genomic DNA. Translation: CAB85555.1.
CP002688 Genomic DNA. Translation: AED90752.1.
BT004006 mRNA. Translation: AAO42044.1.
AY085036 mRNA. Translation: AAM61593.1.
BT021123 mRNA. Translation: AAX22258.1.
PIRiT48445.
RefSeqiNP_196069.1. NM_120531.2.
UniGeneiAt.33117.

Genome annotation databases

EnsemblPlantsiAT5G04490.1; AT5G04490.1; AT5G04490.
GeneIDi830328.
GrameneiAT5G04490.1; AT5G04490.1; AT5G04490.
KEGGiath:AT5G04490.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL162875 Genomic DNA. Translation: CAB85555.1.
CP002688 Genomic DNA. Translation: AED90752.1.
BT004006 mRNA. Translation: AAO42044.1.
AY085036 mRNA. Translation: AAM61593.1.
BT021123 mRNA. Translation: AAX22258.1.
PIRiT48445.
RefSeqiNP_196069.1. NM_120531.2.
UniGeneiAt.33117.

3D structure databases

ProteinModelPortaliQ9LZ76.
SMRiQ9LZ76. Positions 170-278.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT5G04490.1.

Proteomic databases

PaxDbiQ9LZ76.
PRIDEiQ9LZ76.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G04490.1; AT5G04490.1; AT5G04490.
GeneIDi830328.
GrameneiAT5G04490.1; AT5G04490.1; AT5G04490.
KEGGiath:AT5G04490.

Organism-specific databases

TAIRiAT5G04490.

Phylogenomic databases

eggNOGiKOG4453. Eukaryota.
COG0170. LUCA.
HOGENOMiHOG000265019.
InParanoidiQ9LZ76.
KOiK18678.
OMAiGYFQLDW.
PhylomeDBiQ9LZ76.

Enzyme and pathway databases

UniPathwayiUPA00160.
BioCyciARA:AT5G04490-MONOMER.
MetaCyc:AT5G04490-MONOMER.
BRENDAi2.7.1.182. 399.

Miscellaneous databases

PROiQ9LZ76.

Gene expression databases

GenevisibleiQ9LZ76. AT.

Family and domain databases

ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
    Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.
    , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
    Nature 408:823-826(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  4. "Full-length cDNA from Arabidopsis thaliana."
    Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. "Arabidopsis ORF clones."
    Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  6. "The Arabidopsis vitamin E pathway gene5-1 mutant reveals a critical role for phytol kinase in seed tocopherol biosynthesis."
    Valentin H.E., Lincoln K., Moshiri F., Jensen P.K., Qi Q., Venkatesh T.V., Karunanandaa B., Baszis S.R., Norris S.R., Savidge B., Gruys K.J., Last R.L.
    Plant Cell 18:212-224(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, DEVELOPMENTAL STAGE, MUTANT LT1/VTE5-1.
  7. "Remobilization of phytol from chlorophyll degradation is essential for tocopherol synthesis and growth of Arabidopsis."
    Vom Dorp K., Hoelzl G., Plohmann C., Eisenhut M., Abraham M., Weber A.P., Hanson A.D., Doermann P.
    Plant Cell 27:2846-2859(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, GENE FAMILY.

Entry informationi

Entry nameiPHYK1_ARATH
AccessioniPrimary (citable) accession number: Q9LZ76
Secondary accession number(s): Q84WC0, Q8LF61
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: October 1, 2000
Last modified: April 13, 2016
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.