PHYK1_ARATH
ID PHYK1_ARATH Reviewed; 304 AA.
AC Q9LZ76; Q84WC0; Q8LF61;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Phytol kinase 1, chloroplastic {ECO:0000305};
DE EC=2.7.1.182 {ECO:0000269|PubMed:16361393};
DE AltName: Full=Vitamin E pathway gene 5 protein {ECO:0000303|PubMed:16361393};
DE Flags: Precursor;
GN Name=VTE5 {ECO:0000303|PubMed:16361393};
GN OrderedLocusNames=At5g04490 {ECO:0000312|Araport:AT5G04490};
GN ORFNames=T32M21_90 {ECO:0000312|EMBL:CAB85555.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, DEVELOPMENTAL STAGE, AND MUTANT LT1/VTE5-1.
RX PubMed=16361393; DOI=10.1105/tpc.105.037077;
RA Valentin H.E., Lincoln K., Moshiri F., Jensen P.K., Qi Q., Venkatesh T.V.,
RA Karunanandaa B., Baszis S.R., Norris S.R., Savidge B., Gruys K.J.,
RA Last R.L.;
RT "The Arabidopsis vitamin E pathway gene5-1 mutant reveals a critical role
RT for phytol kinase in seed tocopherol biosynthesis.";
RL Plant Cell 18:212-224(2006).
RN [7]
RP DISRUPTION PHENOTYPE, AND GENE FAMILY.
RX PubMed=26452599; DOI=10.1105/tpc.15.00395;
RA Vom Dorp K., Hoelzl G., Plohmann C., Eisenhut M., Abraham M., Weber A.P.,
RA Hanson A.D., Doermann P.;
RT "Remobilization of phytol from chlorophyll degradation is essential for
RT tocopherol synthesis and growth of Arabidopsis.";
RL Plant Cell 27:2846-2859(2015).
CC -!- FUNCTION: Kinase involved in the activation and reutilization of phytol
CC from chlorophyll degradation in plant metabolism, including tocopherol
CC biosynthesis. Catalyzes the conversion of phytol to phytol
CC monophosphate (PMP) in the presence of CTP or UTP. No activity with ATP
CC or GTP as phosphoryl donor. {ECO:0000269|PubMed:16361393}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CTP + phytol = CDP + H(+) + phytyl phosphate;
CC Xref=Rhea:RHEA:38055, ChEBI:CHEBI:15378, ChEBI:CHEBI:17327,
CC ChEBI:CHEBI:37563, ChEBI:CHEBI:58069, ChEBI:CHEBI:75483;
CC EC=2.7.1.182; Evidence={ECO:0000269|PubMed:16361393};
CC -!- PATHWAY: Cofactor biosynthesis; tocopherol biosynthesis.
CC {ECO:0000269|PubMed:16361393, ECO:0000269|PubMed:26452599}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed early in seed development and in
CC 6-week-old senescent leaves. {ECO:0000269|PubMed:16361393}.
CC -!- DISRUPTION PHENOTYPE: 50% reduction in tocopherol content in leaves.
CC Plants able to grow on soil and to produce fertile seeds. Vte5 and vte6
CC double mutants can grow photoautotrophically and show a stay-green
CC phenotype with strongly delayed senescence and extended lifetime.
CC {ECO:0000269|PubMed:26452599}.
CC -!- SIMILARITY: Belongs to the polyprenol kinase family. {ECO:0000305}.
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DR EMBL; AL162875; CAB85555.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90752.1; -; Genomic_DNA.
DR EMBL; BT004006; AAO42044.1; -; mRNA.
DR EMBL; AY085036; AAM61593.1; -; mRNA.
DR EMBL; BT021123; AAX22258.1; -; mRNA.
DR PIR; T48445; T48445.
DR RefSeq; NP_196069.1; NM_120531.3.
DR AlphaFoldDB; Q9LZ76; -.
DR STRING; 3702.AT5G04490.1; -.
DR SwissLipids; SLP:000001494; -.
DR PaxDb; Q9LZ76; -.
DR PRIDE; Q9LZ76; -.
DR ProteomicsDB; 234911; -.
DR EnsemblPlants; AT5G04490.1; AT5G04490.1; AT5G04490.
DR GeneID; 830328; -.
DR Gramene; AT5G04490.1; AT5G04490.1; AT5G04490.
DR KEGG; ath:AT5G04490; -.
DR Araport; AT5G04490; -.
DR TAIR; locus:2184447; AT5G04490.
DR eggNOG; KOG4453; Eukaryota.
DR HOGENOM; CLU_058561_3_0_1; -.
DR InParanoid; Q9LZ76; -.
DR OMA; SWPIFST; -.
DR OrthoDB; 1323987at2759; -.
DR PhylomeDB; Q9LZ76; -.
DR BioCyc; ARA:AT5G04490-MON; -.
DR BioCyc; MetaCyc:AT5G04490-MON; -.
DR BRENDA; 2.7.1.182; 399.
DR UniPathway; UPA00160; -.
DR PRO; PR:Q9LZ76; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LZ76; baseline and differential.
DR Genevisible; Q9LZ76; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IBA:GO_Central.
DR GO; GO:0010276; F:phytol kinase activity; IDA:TAIR.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0010189; P:vitamin E biosynthetic process; IMP:TAIR.
DR InterPro; IPR039606; Phytol/farnesol_kinase.
DR PANTHER; PTHR32523; PTHR32523; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Kinase; Membrane; Plastid; Reference proteome; Transferase;
KW Transit peptide; Transmembrane; Transmembrane helix.
FT TRANSIT 1..59
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 60..304
FT /note="Phytol kinase 1, chloroplastic"
FT /id="PRO_0000226591"
FT TRANSMEM 71..91
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 129..149
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MUTAGEN 227..304
FT /note="Missing: In lt1/vte5-1; 80% reduction in total seed
FT tocopherols."
FT CONFLICT 74
FT /note="T -> A (in Ref. 3; AAO42044)"
FT /evidence="ECO:0000305"
FT CONFLICT 256
FT /note="M -> I (in Ref. 4; AAM61593)"
FT /evidence="ECO:0000305"
FT CONFLICT 267
FT /note="M -> I (in Ref. 4; AAM61593)"
FT /evidence="ECO:0000305"
FT CONFLICT 288
FT /note="I -> V (in Ref. 4; AAM61593)"
FT /evidence="ECO:0000305"
FT CONFLICT 297
FT /note="A -> T (in Ref. 4; AAM61593)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 304 AA; 33090 MW; 770CA569C9F50A50 CRC64;
MAATLPLSPI NHQLCRFGNN SLTTHRFCSP GFLISSPCFI GLTGMGSATQ LRARRSLISS
AVATNSLLHD VGATVAVLGG AYALVLSFES LTKRNVIQQS LSRKLVHILS GLLFVLAWPI
FSGSTEARYF AAFVPLVNGL RLVINGLSIS PNSMLIKSVT REGRAEELLK GPLFYVLALL
FSAVFFWRES PIGMISLAMM CGGDGIADIM GRKFGSTKIP YNPRKSWAGS ISMFIFGFFI
SIALLYYYSS LGYLHMNWET TLQRVAMVSM VATVVESLPI TDQLDDNISV PLATILAAYL
SFGY
