TOCC_ARATH
ID TOCC_ARATH Reviewed; 488 AA.
AC Q94FY7; O65524;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=Tocopherol cyclase, chloroplastic;
DE EC=5.5.1.24;
DE AltName: Full=Sucrose export defective 1;
DE AltName: Full=Vitamin E pathway gene 1 protein;
DE Flags: Precursor;
GN Name=VTE1; Synonyms=SXD1; OrderedLocusNames=At4g32770; ORFNames=F4D11.30;
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 [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11340186; DOI=10.2307/3871368;
RA Provencher L.M., Miao L., Sinha N., Lucas W.J.;
RT "Sucrose export defective 1 encodes a novel protein implicated in
RT chloroplast-to-nucleus signaling.";
RL Plant Cell 13:1127-1141(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
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 [4]
RP FUNCTION.
RX PubMed=12213958; DOI=10.1073/pnas.182330899;
RA Porfirova S., Bergmueller E., Tropf S., Lemke R., Doermann P.;
RT "Isolation of an Arabidopsis mutant lacking vitamin E and identification of
RT a cyclase essential for all tocopherol biosynthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:12495-12500(2002).
RN [5]
RP SUBCELLULAR LOCATION.
RC STRAIN=cv. Col-2;
RX PubMed=16414959; DOI=10.1074/jbc.m511939200;
RA Vidi P.-A., Kanwischer M., Baginsky S., Austin J.R., Csucs G., Doermann P.,
RA Kessler F., Brehelin C.;
RT "Tocopherol cyclase (VTE1) localization and vitamin E accumulation in
RT chloroplast plastoglobule lipoprotein particles.";
RL J. Biol. Chem. 281:11225-11234(2006).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=16461379; DOI=10.1104/pp.105.076083;
RA Ytterberg A.J., Peltier J.-B., van Wijk K.J.;
RT "Protein profiling of plastoglobules in chloroplasts and chromoplasts. A
RT surprising site for differential accumulation of metabolic enzymes.";
RL Plant Physiol. 140:984-997(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=22274653; DOI=10.1104/pp.111.193144;
RA Lundquist P.K., Poliakov A., Bhuiyan N.H., Zybailov B., Sun Q.,
RA van Wijk K.J.;
RT "The functional network of the Arabidopsis plastoglobule proteome based on
RT quantitative proteomics and genome-wide coexpression analysis.";
RL Plant Physiol. 158:1172-1192(2012).
CC -!- FUNCTION: Involved in the synthesis of both tocopherols and
CC tocotrienols (vitamin E), which presumably protect photosynthetic
CC complexes from oxidative stress. Catalyzes the conversion of 2-methyl-
CC 6-phytyl-1,4-hydroquinone and 2,3-dimethyl-5-phytyl-1,4-hydroquinone
CC (DMPQ) to delta- and gamma-tocopherol respectively. Converts also 2,3-
CC dimethyl-5-geranylgeranyl-1,4-hydroquinone (DMGQ) to gamma-tocotrienol.
CC {ECO:0000269|PubMed:12213958}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=delta-tocopherol = 2-methyl-6-phytyl-1,4-benzene-1,4-diol;
CC Xref=Rhea:RHEA:37987, ChEBI:CHEBI:47772, ChEBI:CHEBI:75920;
CC EC=5.5.1.24;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=gamma-tocopherol = 2,3-dimethyl-6-phytylbenzene-1,4-diol;
CC Xref=Rhea:RHEA:37983, ChEBI:CHEBI:18185, ChEBI:CHEBI:75921;
CC EC=5.5.1.24;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=delta-tocotrienol = 6-geranylgeranyl-2-methylbenzene-1,4-diol;
CC Xref=Rhea:RHEA:38015, ChEBI:CHEBI:33276, ChEBI:CHEBI:75411;
CC EC=5.5.1.24;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=gamma-tocotrienol = 6-geranylgeranyl-2,3-dimethylbenzene-1,4-
CC diol; Xref=Rhea:RHEA:38023, ChEBI:CHEBI:33277, ChEBI:CHEBI:75412;
CC EC=5.5.1.24;
CC -!- PATHWAY: Cofactor biosynthesis; tocopherol biosynthesis.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast, plastoglobule
CC {ECO:0000269|PubMed:16414959, ECO:0000269|PubMed:16461379,
CC ECO:0000269|PubMed:22274653}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA18584.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79994.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF302188; AAK60503.1; -; mRNA.
DR EMBL; AL022537; CAA18584.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161582; CAB79994.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE86116.1; -; Genomic_DNA.
DR RefSeq; NP_567906.1; NM_119430.5.
DR AlphaFoldDB; Q94FY7; -.
DR STRING; 3702.AT4G32770.1; -.
DR SwissLipids; SLP:000001491; -.
DR iPTMnet; Q94FY7; -.
DR PaxDb; Q94FY7; -.
DR PRIDE; Q94FY7; -.
DR ProteomicsDB; 234311; -.
DR EnsemblPlants; AT4G32770.1; AT4G32770.1; AT4G32770.
DR GeneID; 829413; -.
DR Gramene; AT4G32770.1; AT4G32770.1; AT4G32770.
DR KEGG; ath:AT4G32770; -.
DR Araport; AT4G32770; -.
DR TAIR; locus:2125657; AT4G32770.
DR eggNOG; ENOG502QQ9P; Eukaryota.
DR HOGENOM; CLU_048962_0_0_1; -.
DR InParanoid; Q94FY7; -.
DR OMA; FAFMYSI; -.
DR OrthoDB; 1312305at2759; -.
DR PhylomeDB; Q94FY7; -.
DR BRENDA; 5.5.1.24; 399.
DR UniPathway; UPA00160; -.
DR PRO; PR:Q94FY7; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q94FY7; baseline and differential.
DR Genevisible; Q94FY7; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009706; C:chloroplast inner membrane; TAS:TAIR.
DR GO; GO:0009534; C:chloroplast thylakoid; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0010287; C:plastoglobule; IDA:TAIR.
DR GO; GO:0052604; F:delta-tocopherol cyclase activity; IEA:RHEA.
DR GO; GO:0052605; F:gamma-tocopherol cyclase activity; IEA:RHEA.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0009976; F:tocopherol cyclase activity; IDA:TAIR.
DR GO; GO:0015994; P:chlorophyll metabolic process; IGI:TAIR.
DR GO; GO:0006631; P:fatty acid metabolic process; IGI:TAIR.
DR GO; GO:0009915; P:phloem sucrose loading; IMP:TAIR.
DR GO; GO:0031347; P:regulation of defense response; IMP:TAIR.
DR GO; GO:0009644; P:response to high light intensity; IEP:TAIR.
DR GO; GO:0006979; P:response to oxidative stress; IEP:TAIR.
DR GO; GO:0009266; P:response to temperature stimulus; IMP:TAIR.
DR GO; GO:0010189; P:vitamin E biosynthetic process; IDA:TAIR.
DR GO; GO:0016122; P:xanthophyll metabolic process; IMP:TAIR.
DR InterPro; IPR025893; Tocopherol_cyclase.
DR PANTHER; PTHR35309; PTHR35309; 1.
DR Pfam; PF14249; Tocopherol_cycl; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Isomerase; Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..76
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 77..488
FT /note="Tocopherol cyclase, chloroplastic"
FT /id="PRO_0000022561"
SQ SEQUENCE 488 AA; 54721 MW; 4FA43FB015DF5806 CRC64;
MEIRSLIVSM NPNLSSFELS RPVSPLTRSL VPFRSTKLVP RSISRVSASI STPNSETDKI
SVKPVYVPTS PNRELRTPHS GYHFDGTPRK FFEGWYFRVS IPEKRESFCF MYSVENPAFR
QSLSPLEVAL YGPRFTGVGA QILGANDKYL CQYEQDSHNF WGDRHELVLG NTFSAVPGAK
APNKEVPPEE FNRRVSEGFQ ATPFWHQGHI CDDGRTDYAE TVKSARWEYS TRPVYGWGDV
GAKQKSTAGW PAAFPVFEPH WQICMAGGLS TGWIEWGGER FEFRDAPSYS EKNWGGGFPR
KWFWVQCNVF EGATGEVALT AGGGLRQLPG LTETYENAAL VCVHYDGKMY EFVPWNGVVR
WEMSPWGYWY ITAENENHVV ELEARTNEAG TPLRAPTTEV GLATACRDSC YGELKLQIWE
RLYDGSKGKV ILETKSSMAA VEIGGGPWFG TWKGDTSNTP ELLKQALQVP LDLESALGLV
PFFKPPGL
