LCYE_ARATH
ID LCYE_ARATH Reviewed; 524 AA.
AC Q38932; Q9LDV8;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2003, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Lycopene epsilon cyclase, chloroplastic {ECO:0000303|PubMed:8837512};
DE EC=5.5.1.18 {ECO:0000269|PubMed:11226339, ECO:0000269|PubMed:8837512};
DE AltName: Full=Protein LUTEIN DEFICIENT 2 {ECO:0000303|PubMed:9789087};
DE Flags: Precursor;
GN Name=LUT2 {ECO:0000303|PubMed:9789087};
GN OrderedLocusNames=At5g57030 {ECO:0000312|Araport:AT5G57030};
GN ORFNames=MHM17.16 {ECO:0000312|EMBL:BAA97033.1};
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], 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 [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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
RN [4]
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 [5]
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 [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=9789087; DOI=10.1073/pnas.95.22.13324;
RA Pogson B.J., Niyogi K.K., Bjoerkman O., DellaPenna D.;
RT "Altered xanthophyll compositions adversely affect chlorophyll accumulation
RT and nonphotochemical quenching in Arabidopsis mutants.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:13324-13329(1998).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ALA-447; 447-ALA--PHE-452
RP AND LEU-448.
RX PubMed=11226339; DOI=10.1073/pnas.051618398;
RA Cunningham F.X. Jr., Gantt E.;
RT "One ring or two? Determination of ring number in carotenoids by lycopene
RT epsilon-cyclases.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:2905-2910(2001).
CC -!- FUNCTION: Involved in carotenoid biosynthesis. Catalyzes the single
CC epsilon-cyclization reaction which converts lycopene to delta-carotene
CC and neurosporene to alpha-zeacarotene (PubMed:8837512,
CC PubMed:11226339). Required for lutein biosynthesis (PubMed:9789087).
CC {ECO:0000269|PubMed:11226339, ECO:0000269|PubMed:8837512,
CC ECO:0000269|PubMed:9789087}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a carotenoid psi-end group = a carotenoid epsilon-end group;
CC Xref=Rhea:RHEA:55616, ChEBI:CHEBI:139114, ChEBI:CHEBI:139115;
CC EC=5.5.1.18; Evidence={ECO:0000269|PubMed:11226339,
CC ECO:0000269|PubMed:8837512};
CC -!- PATHWAY: Carotenoid biosynthesis; alpha-zeacarotene biosynthesis.
CC {ECO:0000305}.
CC -!- PATHWAY: Carotenoid biosynthesis; delta-carotene biosynthesis.
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane {ECO:0000255};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Delayed greening and virescent seedlings.
CC {ECO:0000269|PubMed:9789087}.
CC -!- SIMILARITY: Belongs to the lycopene cyclase family. {ECO:0000305}.
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DR EMBL; U50738; AAB53336.1; -; mRNA.
DR EMBL; AF117257; AAF82389.1; -; Genomic_DNA.
DR EMBL; AB024035; BAA97033.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96836.1; -; Genomic_DNA.
DR EMBL; AY040024; AAK64181.1; -; mRNA.
DR EMBL; AY079371; AAL85102.1; -; mRNA.
DR RefSeq; NP_200513.1; NM_125085.5.
DR AlphaFoldDB; Q38932; -.
DR SMR; Q38932; -.
DR STRING; 3702.AT5G57030.1; -.
DR PaxDb; Q38932; -.
DR PRIDE; Q38932; -.
DR ProteomicsDB; 237157; -.
DR EnsemblPlants; AT5G57030.1; AT5G57030.1; AT5G57030.
DR GeneID; 835806; -.
DR Gramene; AT5G57030.1; AT5G57030.1; AT5G57030.
DR KEGG; ath:AT5G57030; -.
DR Araport; AT5G57030; -.
DR TAIR; locus:2164590; AT5G57030.
DR eggNOG; ENOG502QT61; Eukaryota.
DR HOGENOM; CLU_032956_1_0_1; -.
DR InParanoid; Q38932; -.
DR OMA; QTCYGIV; -.
DR OrthoDB; 815606at2759; -.
DR PhylomeDB; Q38932; -.
DR BioCyc; ARA:AT5G57030-MON; -.
DR BioCyc; MetaCyc:AT5G57030-MON; -.
DR BRENDA; 5.5.1.18; 399.
DR UniPathway; UPA00801; -.
DR UniPathway; UPA00804; -.
DR PRO; PR:Q38932; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q38932; baseline and differential.
DR Genevisible; Q38932; AT.
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:0045435; F:lycopene epsilon cyclase activity; TAS:TAIR.
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; IMP:TAIR.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; IBA:GO_Central.
DR GO; GO:0016123; P:xanthophyll biosynthetic process; IGI:TAIR.
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 Carotenoid biosynthesis; Chloroplast; Isomerase; Membrane; NAD; Plastid;
KW Reference proteome; Transit peptide; Transmembrane; Transmembrane helix.
FT TRANSIT 1..45
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 46..524
FT /note="Lycopene epsilon cyclase, chloroplastic"
FT /id="PRO_0000018434"
FT TRANSMEM 441..461
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 475..495
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 111..139
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
FT MUTAGEN 447..452
FT /note="ALIVQF->HIVLM: Converts the enzyme from a mono- to a
FT bi-epsilon-cyclase."
FT /evidence="ECO:0000269|PubMed:11226339"
FT MUTAGEN 447
FT /note="A->D: No effect on catalytic activity."
FT /evidence="ECO:0000269|PubMed:11226339"
FT MUTAGEN 448
FT /note="L->D: Partial loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:11226339"
FT MUTAGEN 448
FT /note="L->H,R: Converts the enzyme from a mono- to a bi-
FT epsilon-cyclase."
FT /evidence="ECO:0000269|PubMed:11226339"
FT CONFLICT 111
FT /note="L -> H (in Ref. 1; AAB53336)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 524 AA; 58491 MW; 4C1F98CC72EDD074 CRC64;
MECVGARNFA AMAVSTFPSW SCRRKFPVVK RYSYRNIRFG LCSVRASGGG SSGSESCVAV
REDFADEEDF VKAGGSEILF VQMQQNKDMD EQSKLVDKLP PISIGDGALD LVVIGCGPAG
LALAAESAKL GLKVGLIGPD LPFTNNYGVW EDEFNDLGLQ KCIEHVWRET IVYLDDDKPI
TIGRAYGRVS RRLLHEELLR RCVESGVSYL SSKVDSITEA SDGLRLVACD DNNVIPCRLA
TVASGAASGK LLQYEVGGPR VCVQTAYGVE VEVENSPYDP DQMVFMDYRD YTNEKVRSLE
AEYPTFLYAM PMTKSRLFFE ETCLASKDVM PFDLLKTKLM LRLDTLGIRI LKTYEEEWSY
IPVGGSLPNT EQKNLAFGAA ASMVHPATGY SVVRSLSEAP KYASVIAEIL REETTKQINS
NISRQAWDTL WPPERKRQRA FFLFGLALIV QFDTEGIRSF FRTFFRLPKW MWQGFLGSTL
TSGDLVLFAL YMFVISPNNL RKGLINHLIS DPTGATMIKT YLKV
