VTE6_ARATH
ID VTE6_ARATH Reviewed; 333 AA.
AC Q9SYM0; Q8LBN5;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Protein VTE6, chloroplastic {ECO:0000303|PubMed:26452599};
DE AltName: Full=Phytyl-P kinase {ECO:0000303|PubMed:26452599};
DE EC=2.7.4.- {ECO:0000305};
DE AltName: Full=Vitamin E deficient 6 {ECO:0000303|PubMed:26452599};
DE Flags: Precursor;
GN Name=VTE6 {ECO:0000303|PubMed:26452599};
GN OrderedLocusNames=At1g78620 {ECO:0000312|Araport:AT1G78620};
GN ORFNames=T30F21.5 {ECO:0000312|EMBL:AAD30574.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE,
RP 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).
RN [6]
RP FUNCTION.
RX PubMed=28007557; DOI=10.1016/j.molp.2016.12.006;
RA Wang L., Li Q., Zhang A., Zhou W., Jiang R., Yang Z., Yang H., Qin X.,
RA Ding S., Lu Q., Wen X., Lu C.;
RT "The phytol phosphorylation pathway is essential for the biosynthesis of
RT phylloquinone, which is required for photosystem I stability in
RT Arabidopsis.";
RL Mol. Plant 10:183-196(2017).
CC -!- FUNCTION: Phytyl-phosphate kinase catalyzing the conversion of phytyl-
CC monophosphate to phytyl-diphosphate (PubMed:26452599). Involved in the
CC activation and reutilization of phytol from chlorophyll degradation in
CC plant metabolism, including tocopherol (vitamin E) biosynthesis
CC (PubMed:26452599). Involved in the biosynthesis of phylloquinone
CC (vitamin K), which is required for the photosystem I (PSI) complex
CC stability (PubMed:28007557). {ECO:0000269|PubMed:26452599,
CC ECO:0000269|PubMed:28007557}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + phytyl phosphate = a
CC ribonucleoside 5'-diphosphate + phytyl diphosphate;
CC Xref=Rhea:RHEA:38099, ChEBI:CHEBI:57930, ChEBI:CHEBI:61557,
CC ChEBI:CHEBI:75434, ChEBI:CHEBI:75483;
CC Evidence={ECO:0000269|PubMed:26452599};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38100;
CC Evidence={ECO:0000269|PubMed:26452599};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CTP + phytyl phosphate = CDP + phytyl diphosphate;
CC Xref=Rhea:RHEA:49276, ChEBI:CHEBI:37563, ChEBI:CHEBI:58069,
CC ChEBI:CHEBI:75434, ChEBI:CHEBI:75483;
CC Evidence={ECO:0000269|PubMed:26452599};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49277;
CC Evidence={ECO:0000269|PubMed:26452599};
CC -!- PATHWAY: Cofactor biosynthesis; tocopherol biosynthesis.
CC {ECO:0000269|PubMed:26452599}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane
CC {ECO:0000269|PubMed:26452599}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9SYM0-1; Sequence=Displayed;
CC -!- DISRUPTION PHENOTYPE: Lethal when homozygous. Tocopherol-deficient
CC plants are unable to grow photoautotrophically and infertile. Vte5 and
CC vte6 double mutants can grow photoautotrophically and display a stay-
CC green phenotype with strongly delayed senescence and an extended
CC lifetime. {ECO:0000269|PubMed:26452599}.
CC -!- MISCELLANEOUS: Overexpression of VTE6 results in increased phytyl-PP
CC and tocopherol levels in seeds. {ECO:0000269|PubMed:26452599}.
CC -!- SIMILARITY: Belongs to the TMEM19 family. {ECO:0000305}.
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DR EMBL; AC007260; AAD30574.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE36128.1; -; Genomic_DNA.
DR EMBL; AY035002; AAK59507.1; -; mRNA.
DR EMBL; AY063010; AAL34184.1; -; mRNA.
DR EMBL; AY087104; AAM64662.1; -; mRNA.
DR PIR; H96814; H96814.
DR RefSeq; NP_565184.1; NM_106509.4. [Q9SYM0-1]
DR AlphaFoldDB; Q9SYM0; -.
DR STRING; 3702.AT1G78620.2; -.
DR SwissLipids; SLP:000001501; -.
DR PaxDb; Q9SYM0; -.
DR PRIDE; Q9SYM0; -.
DR EnsemblPlants; AT1G78620.1; AT1G78620.1; AT1G78620. [Q9SYM0-1]
DR GeneID; 844198; -.
DR Gramene; AT1G78620.1; AT1G78620.1; AT1G78620. [Q9SYM0-1]
DR KEGG; ath:AT1G78620; -.
DR Araport; AT1G78620; -.
DR eggNOG; ENOG502QU2J; Eukaryota.
DR HOGENOM; CLU_036918_0_0_1; -.
DR OMA; AYGKRTF; -.
DR PhylomeDB; Q9SYM0; -.
DR UniPathway; UPA00160; -.
DR PRO; PR:Q9SYM0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SYM0; baseline and differential.
DR GO; GO:0009706; C:chloroplast inner membrane; IBA:GO_Central.
DR GO; GO:0031969; C:chloroplast membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0010276; F:phytol kinase activity; IDA:UniProtKB.
DR GO; GO:0102763; F:phytyl-P kinase activity; IEA:RHEA.
DR GO; GO:0033306; P:phytol metabolic process; IDA:UniProtKB.
DR GO; GO:0010189; P:vitamin E biosynthetic process; IMP:UniProtKB.
DR GO; GO:0042371; P:vitamin K biosynthetic process; IDA:UniProtKB.
DR InterPro; IPR002794; DUF92_TMEM19.
DR PANTHER; PTHR13353; PTHR13353; 1.
DR Pfam; PF01940; DUF92; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chloroplast; Membrane; Plastid; Reference proteome;
KW Transferase; Transit peptide; Transmembrane; Transmembrane helix.
FT TRANSIT 1..65
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 66..333
FT /note="Protein VTE6, chloroplastic"
FT /evidence="ECO:0000255"
FT /id="PRO_0000435963"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 171..191
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 248..268
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 274..294
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 307..327
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 34
FT /note="A -> P (in Ref. 4; AAM64662)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 333 AA; 34874 MW; F385BFE9A93F92D1 CRC64;
MATISSTLLL NSSRSALPLR FPKFSGFSSS SPFARSYRFG RRNLEPLSNG MLSSGSRADG
ATAAAASMEG VMTEAMKLIQ SASPTWKSAV ANNLLIFVLG SPLLVTGLSA SGIAAAFLLG
TLTWRAYGSA GFLLVAAYFV IGTAATKVKM TQKEAQGVAE KRKGRRGPRS VIGSSAAGCV
CAFLSIYQVG GAAFSQLFRL GFVSSFCTKV SDTVSSEIGK AYGKTTYLAT TFKIVPRGTE
GAMSLEGTLA GLLASFFLAS VGCFLGQITP PEAAVCVLAS QIANLGESII GASFQDKEGF
KWLNNDVVNV INISLGSIVA ILMQQFILQN WVK
