LCYB_ARATH
ID LCYB_ARATH Reviewed; 501 AA.
AC Q38933; A8MR53; Q39145;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Lycopene beta cyclase, chloroplastic {ECO:0000303|PubMed:8837512};
DE EC=5.5.1.19 {ECO:0000269|PubMed:8837512};
DE AltName: Full=AtLCY {ECO:0000303|PubMed:21471119};
DE AltName: Full=Protein SUPPRESSOR OF ZEAXANTHIN-LESS 1 {ECO:0000303|PubMed:19549928};
DE Flags: Precursor;
GN Name=LCY1 {ECO:0000303|PubMed:21471119};
GN Synonyms=LCYB {ECO:0000303|PubMed:19549928}, LYC {ECO:0000303|Ref.2},
GN SZL1 {ECO:0000303|PubMed:19549928};
GN OrderedLocusNames=At3g10230 {ECO:0000312|Araport:AT3G10230};
GN ORFNames=F14P13.17 {ECO:0000312|EMBL:AAF02819.1};
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 [MRNA] (ISOFORM 1), FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=cv. Columbia;
RX PubMed=8837512; DOI=10.2307/3870254;
RA Cunningham F.X. Jr., Pogson B., Sun Z., McDonald K.A., Dellapenna D.,
RA Gantt E.;
RT "Functional analysis of the beta and epsilon lycopene cyclase enzymes of
RT Arabidopsis reveals a mechanism for control of cyclic carotenoid
RT formation.";
RL Plant Cell 8:1613-1626(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=cv. Wassilewskija;
RA Scolnik P.A., Bartley G.E.;
RT "Nucleotide sequence of lycopene cyclase from Arabidopsis.";
RL (er) Plant Gene Register PGR95-019(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Giuliano G., Rosati C., Santangelo G.;
RT "Gene structure and regulation of the carotenoid biosynthesis pathway in
RT Arabidopsis thaliana.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [7]
RP FUNCTION, AND MUTAGENESIS OF GLY-451.
RX PubMed=19549928; DOI=10.1105/tpc.109.066571;
RA Li Z., Ahn T.K., Avenson T.J., Ballottari M., Cruz J.A., Kramer D.M.,
RA Bassi R., Fleming G.R., Keasling J.D., Niyogi K.K.;
RT "Lutein accumulation in the absence of zeaxanthin restores nonphotochemical
RT quenching in the Arabidopsis thaliana npq1 mutant.";
RL Plant Cell 21:1798-1812(2009).
RN [8]
RP FUNCTION.
RX PubMed=21471119; DOI=10.1093/pcp/pcr043;
RA Chen X., Han H., Jiang P., Nie L., Bao H., Fan P., Lv S., Feng J., Li Y.;
RT "Transformation of beta-lycopene cyclase genes from Salicornia europaea and
RT Arabidopsis conferred salt tolerance in Arabidopsis and tobacco.";
RL Plant Cell Physiol. 52:909-921(2011).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT VAL-49, CLEAVAGE OF TRANSIT PEPTIDE
RP [LARGE SCALE ANALYSIS] AFTER SER-48, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Involved in carotenoid biosynthesis. Catalyzes the double
CC cyclization reaction which converts lycopene to beta-carotene and
CC neurosporene to beta-zeacarotene (PubMed:8837512). Major lycopene beta-
CC cyclase that does not seem to be involved in neoxanthin synthesis
CC (PubMed:19549928). Involved in salt tolerance improvement by increasing
CC synthesis of carotenoids, which impairs reactive oxygen species (ROS)
CC and protects the photosynthetic system under salt stress
CC (PubMed:21471119). {ECO:0000269|PubMed:19549928,
CC ECO:0000269|PubMed:21471119, ECO:0000269|PubMed:8837512}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a carotenoid psi-end group = a carotenoid beta-end derivative;
CC Xref=Rhea:RHEA:55620, ChEBI:CHEBI:139114, ChEBI:CHEBI:139120;
CC EC=5.5.1.19; Evidence={ECO:0000269|PubMed:8837512};
CC -!- PATHWAY: Carotenoid biosynthesis; beta-carotene biosynthesis.
CC {ECO:0000305}.
CC -!- PATHWAY: Carotenoid biosynthesis; beta-zeacarotene biosynthesis.
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q38933-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q38933-2; Sequence=VSP_035546;
CC -!- MISCELLANEOUS: Plants overexpressing LYC1 exhibit improved tolerance to
CC salt stress. {ECO:0000269|PubMed:21471119}.
CC -!- SIMILARITY: Belongs to the lycopene cyclase family. {ECO:0000305}.
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DR EMBL; U50739; AAB53337.1; -; mRNA.
DR EMBL; L40176; AAA81880.1; -; mRNA.
DR EMBL; AF117256; AAF82388.1; -; Genomic_DNA.
DR EMBL; AC009400; AAF02819.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74874.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74875.1; -; Genomic_DNA.
DR EMBL; AY059749; AAL24097.1; -; mRNA.
DR EMBL; AY091396; AAM14335.1; -; mRNA.
DR RefSeq; NP_001078131.1; NM_001084662.1. [Q38933-2]
DR RefSeq; NP_187634.1; NM_111858.2. [Q38933-1]
DR AlphaFoldDB; Q38933; -.
DR SMR; Q38933; -.
DR STRING; 3702.AT3G10230.1; -.
DR iPTMnet; Q38933; -.
DR PaxDb; Q38933; -.
DR PRIDE; Q38933; -.
DR ProteomicsDB; 250738; -. [Q38933-1]
DR EnsemblPlants; AT3G10230.1; AT3G10230.1; AT3G10230. [Q38933-1]
DR EnsemblPlants; AT3G10230.2; AT3G10230.2; AT3G10230. [Q38933-2]
DR GeneID; 820185; -.
DR Gramene; AT3G10230.1; AT3G10230.1; AT3G10230. [Q38933-1]
DR Gramene; AT3G10230.2; AT3G10230.2; AT3G10230. [Q38933-2]
DR KEGG; ath:AT3G10230; -.
DR Araport; AT3G10230; -.
DR TAIR; locus:2076319; AT3G10230.
DR eggNOG; ENOG502QT2F; Eukaryota.
DR InParanoid; Q38933; -.
DR OMA; FVLMDFR; -.
DR PhylomeDB; Q38933; -.
DR BioCyc; ARA:AT3G10230-MON; -.
DR BioCyc; MetaCyc:AT3G10230-MON; -.
DR UniPathway; UPA00802; -.
DR UniPathway; UPA00805; -.
DR PRO; PR:Q38933; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q38933; baseline and differential.
DR Genevisible; Q38933; AT.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0045436; F:lycopene beta cyclase activity; IDA:UniProtKB.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR GO; GO:0016120; P:carotene biosynthetic process; IBA:GO_Central.
DR GO; GO:0016117; P:carotenoid biosynthetic process; IDA:UniProtKB.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; IBA:GO_Central.
DR GO; GO:0016123; P:xanthophyll biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR010108; Lycopene_cyclase_b/e.
DR SUPFAM; SSF51905; SSF51905; 1.
DR TIGRFAMs; TIGR01790; carotene-cycl; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Carotenoid biosynthesis; Chloroplast;
KW Isomerase; NAD; Plastid; Reference proteome; Stress response;
KW Transit peptide.
FT TRANSIT 1..48
FT /note="Chloroplast"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 49..501
FT /note="Lycopene beta cyclase, chloroplastic"
FT /id="PRO_0000018429"
FT BINDING 85..113
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
FT MOD_RES 49
FT /note="N-acetylvaline"
FT /evidence="ECO:0007744|PubMed:22223895"
FT VAR_SEQ 1..132
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_035546"
FT MUTAGEN 451
FT /note="G->E: In szl1; slight reduction in plant growth,
FT increased content of lutein, and decreased content of
FT xanthophyll pigments (violaxanthin, antheraxanthin and
FT zeaxanthin)."
FT /evidence="ECO:0000269|PubMed:19549928"
FT CONFLICT 31
FT /note="H -> P (in Ref. 2; AAA81880)"
FT /evidence="ECO:0000305"
FT CONFLICT 243
FT /note="V -> I (in Ref. 2; AAA81880)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 501 AA; 56177 MW; C3014578D0BDC4E2 CRC64;
MDTLLKTPNK LDFFIPQFHG FERLCSNNPY HSRVRLGVKK RAIKIVSSVV SGSAALLDLV
PETKKENLDF ELPLYDTSKS QVVDLAIVGG GPAGLAVAQQ VSEAGLSVCS IDPSPKLIWP
NNYGVWVDEF EAMDLLDCLD TTWSGAVVYV DEGVKKDLSR PYGRVNRKQL KSKMLQKCIT
NGVKFHQSKV TNVVHEEANS TVVCSDGVKI QASVVLDATG FSRCLVQYDK PYNPGYQVAY
GIVAEVDGHP FDVDKMVFMD WRDKHLDSYP ELKERNSKIP TFLYAMPFSS NRIFLEETSL
VARPGLRMED IQERMAARLK HLGINVKRIE EDERCVIPMG GPLPVLPQRV VGIGGTAGMV
HPSTGYMVAR TLAAAPIVAN AIVRYLGSPS SNSLRGDQLS AEVWRDLWPI ERRRQREFFC
FGMDILLKLD LDATRRFFDA FFDLQPHYWH GFLSSRLFLP ELLVFGLSLF SHASNTSRLE
IMTKGTVPLA KMINNLVQDR D
