PHYK_SYNY3
ID PHYK_SYNY3 Reviewed; 233 AA.
AC P74653;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Phytol kinase {ECO:0000303|PubMed:16361393};
DE EC=2.7.1.182 {ECO:0000269|PubMed:16361393};
GN Name=vte5 {ECO:0000303|PubMed:16361393};
GN OrderedLocusNames=slr1652 {ECO:0000312|EMBL:BAA18769.1};
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, DISRUPTION PHENOTYPE,
RP AND PATHWAY.
RC STRAIN=ATCC 27184 / PCC 6803 / N-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 [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX PubMed=17499209; DOI=10.1016/j.bbabio.2007.03.010;
RA Vavilin D., Vermaas W.;
RT "Continuous chlorophyll degradation accompanied by chlorophyllide and
RT phytol reutilization for chlorophyll synthesis in Synechocystis sp. PCC
RT 6803.";
RL Biochim. Biophys. Acta 1767:920-929(2007).
CC -!- FUNCTION: Catalyzes the CTP-dependent phosphorylation of phytol to
CC phytylmonophosphate (PMP). Can also use UTP as an alternative phosphate
CC donor, but not ATP or GTP. Is involved in tocopherol biosynthesis, via
CC the utilization of phytol generated by chlorophyll degradation
CC (PubMed:16361393). Also plays a significant but not critical role in
CC the recycling of phytol for the biosynthesis of new chlorophyll
CC molecules (PubMed:17499209). {ECO:0000269|PubMed:16361393,
CC ECO:0000269|PubMed:17499209}.
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}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene show a reduction in
CC tocopherol levels by 50% or more, and an accumulation of free phytol
CC (PubMed:16361393). When measuring the kinetics of chlorophyll labeling
CC after adding 13C, the mutant cells show a similar rate of chlorophyll
CC synthesis and degradation as the wild type, but show a reduced rate of
CC accumulation of chlorophyll containing labeled porphyrin/unlabeled
CC phytyl (13Por12Phy) (PubMed:17499209). {ECO:0000269|PubMed:16361393,
CC ECO:0000269|PubMed:17499209}.
CC -!- SIMILARITY: Belongs to the polyprenol kinase family. {ECO:0000305}.
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DR EMBL; BA000022; BAA18769.1; -; Genomic_DNA.
DR PIR; S76857; S76857.
DR AlphaFoldDB; P74653; -.
DR IntAct; P74653; 1.
DR STRING; 1148.1653859; -.
DR SwissLipids; SLP:000001497; -.
DR PaxDb; P74653; -.
DR EnsemblBacteria; BAA18769; BAA18769; BAA18769.
DR KEGG; syn:slr1652; -.
DR eggNOG; COG0170; Bacteria.
DR InParanoid; P74653; -.
DR OMA; MAWGDGL; -.
DR PhylomeDB; P74653; -.
DR BRENDA; 2.7.1.182; 382.
DR UniPathway; UPA00160; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0010276; F:phytol kinase activity; IDA:UniProtKB.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0033306; P:phytol metabolic process; IDA:UniProtKB.
DR GO; GO:0010189; P:vitamin E biosynthetic process; IMP:UniProtKB.
PE 1: Evidence at protein level;
KW Cell membrane; Kinase; Membrane; Nucleotide-binding; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..233
FT /note="Phytol kinase"
FT /id="PRO_0000432651"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 56..76
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 96..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..144
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 233 AA; 24737 MW; 19C8EBF4272F08B2 CRC64;
MGIEQNNPMA LPLWIAVGLA ATYLGAVVLT AELLNRLSLS PAEVTRKIVH IGAGQVVLIA
WWLSIPGWVG AIAGVFAAGI AVLSYRLPIL PSLESVGRHS YGTLFYALSI GLLVGGFFSL
GLPIFAAIGI LVMAWGDGLA ALVGQRWGRH RYQVFGFRKS WEGTLTMVLA SFLVTVVFLS
YTFGFTVIVL VVAGTVAIAS AGLESFSRWG IDNLTVPLGS ALIAWAGSYL WLG
