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LCYB_CAPAN
ID   LCYB_CAPAN              Reviewed;         498 AA.
AC   Q43415; A0A1U8GKZ7; D7P7Y0;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   12-AUG-2020, sequence version 2.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Lycopene beta cyclase, chloroplastic/chromoplastic {ECO:0000303|PubMed:7550379};
DE            EC=5.5.1.19 {ECO:0000269|PubMed:7550379};
DE   Flags: Precursor;
GN   Name=LCY1 {ECO:0000303|PubMed:7550379}; Synonyms=CRTL;
GN   ORFNames=LOC107869983, T459_13595 {ECO:0000312|EMBL:PHT80580.1};
OS   Capsicum annuum (Capsicum pepper).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Capsiceae; Capsicum.
OX   NCBI_TaxID=4072;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR
RP   LOCATION.
RC   STRAIN=cv. Lamuyo; TISSUE=Fruit;
RX   PubMed=7550379; DOI=10.1046/j.1365-313x.1995.08030417.x;
RA   Hugueney P., Badillo A., Chen H.C., Klein A., Hirschberg J., Camara B.,
RA   Kuntz M.;
RT   "Metabolism of cyclic carotenoids: a model for the alteration of this
RT   biosynthetic pathway in Capsicum annuum chromoplasts.";
RL   Plant J. 8:417-424(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Pericarp;
RX   PubMed=20582146; DOI=10.1016/j.plantsci.2010.04.014;
RA   Guzman I., Hamby S., Romero J., Bosland P.W., O'Connell M.A.;
RT   "Variability of carotenoid biosynthesis in orange colored Capsicum spp.";
RL   Plant Sci. 179:49-59(2010).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=24441736; DOI=10.1038/ng.2877;
RA   Kim S., Park M., Yeom S.I., Kim Y.M., Lee J.M., Lee H.A., Seo E., Choi J.,
RA   Cheong K., Kim K.T., Jung K., Lee G.W., Oh S.K., Bae C., Kim S.B.,
RA   Lee H.Y., Kim S.Y., Kim M.S., Kang B.C., Jo Y.D., Yang H.B., Jeong H.J.,
RA   Kang W.H., Kwon J.K., Shin C., Lim J.Y., Park J.H., Huh J.H., Kim J.S.,
RA   Kim B.D., Cohen O., Paran I., Suh M.C., Lee S.B., Kim Y.K., Shin Y.,
RA   Noh S.J., Park J., Seo Y.S., Kwon S.Y., Kim H.A., Park J.M., Kim H.J.,
RA   Choi S.B., Bosland P.W., Reeves G., Jo S.H., Lee B.W., Cho H.T., Choi H.S.,
RA   Lee M.S., Yu Y., Do Choi Y., Park B.S., van Deynze A., Ashrafi H., Hill T.,
RA   Kim W.T., Pai H.S., Ahn H.K., Yeam I., Giovannoni J.J., Rose J.K.,
RA   Soerensen I., Lee S.J., Kim R.W., Choi I.Y., Choi B.S., Lim J.S., Lee Y.H.,
RA   Choi D.;
RT   "Genome sequence of the hot pepper provides insights into the evolution of
RT   pungency in Capsicum species.";
RL   Nat. Genet. 46:270-278(2014).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Zunla-1;
RX   PubMed=24591624; DOI=10.1073/pnas.1400975111;
RA   Qin C., Yu C., Shen Y., Fang X., Chen L., Min J., Cheng J., Zhao S., Xu M.,
RA   Luo Y., Yang Y., Wu Z., Mao L., Wu H., Ling-Hu C., Zhou H., Lin H.,
RA   Gonzalez-Morales S., Trejo-Saavedra D.L., Tian H., Tang X., Zhao M.,
RA   Huang Z., Zhou A., Yao X., Cui J., Li W., Chen Z., Feng Y., Niu Y., Bi S.,
RA   Yang X., Li W., Cai H., Luo X., Montes-Hernandez S., Leyva-Gonzalez M.A.,
RA   Xiong Z., He X., Bai L., Tan S., Tang X., Liu D., Liu J., Zhang S.,
RA   Chen M., Zhang L., Zhang L., Zhang Y., Liao W., Zhang Y., Wang M., Lv X.,
RA   Wen B., Liu H., Luan H., Zhang Y., Yang S., Wang X., Xu J., Li X., Li S.,
RA   Wang J., Palloix A., Bosland P.W., Li Y., Krogh A., Rivera-Bustamante R.F.,
RA   Herrera-Estrella L., Yin Y., Yu J., Hu K., Zhang Z.;
RT   "Whole-genome sequencing of cultivated and wild peppers provides insights
RT   into Capsicum domestication and specialization.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:5135-5140(2014).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. CM334;
RX   PubMed=29089032; DOI=10.1186/s13059-017-1341-9;
RA   Kim S., Park J., Yeom S.I., Kim Y.M., Seo E., Kim K.T., Kim M.S., Lee J.M.,
RA   Cheong K., Shin H.S., Kim S.B., Han K., Lee J., Park M., Lee H.A.,
RA   Lee H.Y., Lee Y., Oh S., Lee J.H., Choi E., Choi E., Lee S.E., Jeon J.,
RA   Kim H., Choi G., Song H., Lee J., Lee S.C., Kwon J.K., Lee H.Y., Koo N.,
RA   Hong Y., Kim R.W., Kang W.H., Huh J.H., Kang B.C., Yang T.J., Lee Y.H.,
RA   Bennetzen J.L., Choi D.;
RT   "New reference genome sequences of hot pepper reveal the massive evolution
RT   of plant disease-resistance genes by retroduplication.";
RL   Genome Biol. 18:R210.1-R210.11(2017).
RN   [6]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP   SUBUNIT, AND MUTAGENESIS OF ASP-127; GLU-128; ASP-259; GLU-295; GLU-296;
RP   GLU-332 AND HIS-360.
RX   PubMed=20460582; DOI=10.1104/pp.110.155440;
RA   Mialoundama A.S., Heintz D., Jadid N., Nkeng P., Rahier A., Deli J.,
RA   Camara B., Bouvier F.;
RT   "Characterization of plant carotenoid cyclases as members of the
RT   flavoprotein family functioning with no net redox change.";
RL   Plant Physiol. 153:970-979(2010).
CC   -!- FUNCTION: Catalyzes the double cyclization reaction which converts
CC       lycopene to beta-carotene (PubMed:7550379, PubMed:20460582). Catalyzes
CC       the double cyclization reaction which converts neurosporene to 7,8-
CC       dihydro-beta-carotene (PubMed:20460582). {ECO:0000269|PubMed:20460582,
CC       ECO:0000269|PubMed:7550379}.
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:7550379};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55621;
CC         Evidence={ECO:0000269|PubMed:7550379};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=all-trans-lycopene = gamma-carotene; Xref=Rhea:RHEA:32219,
CC         ChEBI:CHEBI:15948, ChEBI:CHEBI:27740;
CC         Evidence={ECO:0000269|PubMed:20460582};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32220;
CC         Evidence={ECO:0000269|PubMed:20460582};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=gamma-carotene = all-trans-beta-carotene;
CC         Xref=Rhea:RHEA:32239, ChEBI:CHEBI:17579, ChEBI:CHEBI:27740;
CC         Evidence={ECO:0000269|PubMed:20460582};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32240;
CC         Evidence={ECO:0000269|PubMed:20460582};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=all-trans-neurosporene = beta-zeacarotene;
CC         Xref=Rhea:RHEA:67976, ChEBI:CHEBI:16833, ChEBI:CHEBI:27533;
CC         Evidence={ECO:0000269|PubMed:20460582};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67977;
CC         Evidence={ECO:0000269|PubMed:20460582};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=beta-zeacarotene = 7,8-dihydro-beta-carotene;
CC         Xref=Rhea:RHEA:67980, ChEBI:CHEBI:27533, ChEBI:CHEBI:80427;
CC         Evidence={ECO:0000269|PubMed:20460582};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67981;
CC         Evidence={ECO:0000269|PubMed:20460582};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000269|PubMed:20460582};
CC       Note=Binds 1 FAD per subunit non-covalently.
CC       {ECO:0000269|PubMed:20460582};
CC   -!- COFACTOR:
CC       Name=NADPH; Xref=ChEBI:CHEBI:57783;
CC         Evidence={ECO:0000269|PubMed:20460582};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.22 mM for NADPH {ECO:0000269|PubMed:20460582};
CC   -!- PATHWAY: Carotenoid biosynthesis; beta-carotene biosynthesis.
CC       {ECO:0000305}.
CC   -!- PATHWAY: Carotenoid biosynthesis; beta-zeacarotene biosynthesis.
CC       {ECO:0000305}.
CC   -!- SUBUNIT: Monomer. {ECO:0000305|PubMed:20460582}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}. Plastid,
CC       chromoplast {ECO:0000305|PubMed:7550379}.
CC   -!- SIMILARITY: Belongs to the lycopene cyclase family. {ECO:0000305}.
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DR   EMBL; X86221; CAA60119.1; -; mRNA.
DR   EMBL; GU085266; ADH04271.1; -; Genomic_DNA.
DR   EMBL; GU085267; ADH04272.1; -; Genomic_DNA.
DR   EMBL; GU085268; ADH04273.1; -; Genomic_DNA.
DR   EMBL; GU085269; ADH04274.1; -; Genomic_DNA.
DR   EMBL; GU085270; ADH04275.1; -; Genomic_DNA.
DR   EMBL; GU085271; ADH04276.1; -; Genomic_DNA.
DR   EMBL; GU085272; ADH04277.1; -; Genomic_DNA.
DR   EMBL; AYRZ02000005; PHT80580.1; -; Genomic_DNA.
DR   RefSeq; NP_001311908.1; NM_001324979.1.
DR   RefSeq; XP_016571835.1; XM_016716349.1.
DR   RefSeq; XP_016571836.1; XM_016716350.1.
DR   AlphaFoldDB; Q43415; -.
DR   SMR; Q43415; -.
DR   STRING; 4072.D7P7Y0; -.
DR   SwissLipids; SLP:000001511; -.
DR   EnsemblPlants; PHT80580; PHT80580; T459_13595.
DR   GeneID; 107869983; -.
DR   Gramene; PHT80580; PHT80580; T459_13595.
DR   KEGG; ag:CAA60119; -.
DR   KEGG; cann:107869983; -.
DR   OMA; FVLMDFR; -.
DR   OrthoDB; 815606at2759; -.
DR   BRENDA; 5.5.1.19; 1169.
DR   UniPathway; UPA00802; -.
DR   UniPathway; UPA00805; -.
DR   Proteomes; UP000189700; Chromosome 5.
DR   Proteomes; UP000222542; Chromosome 5.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0009509; C:chromoplast; IDA:UniProtKB.
DR   GO; GO:0045436; F:lycopene beta cyclase activity; IDA:UniProtKB.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   GO; GO:1901812; P:beta-carotene biosynthetic process; IDA:UniProtKB.
DR   GO; GO:1901818; P:beta-zeacarotene biosynthetic process; IDA:UniProtKB.
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; Chromoplast; Flavoprotein; Isomerase;
KW   NAD; Plastid; Reference proteome; Transit peptide.
FT   TRANSIT         1..79
FT                   /note="Chloroplast and chromoplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           80..498
FT                   /note="Lycopene beta cyclase, chloroplastic/chromoplastic"
FT                   /id="PRO_0000018430"
FT   MOTIF           293..297
FT                   /note="FLEET motif"
FT                   /evidence="ECO:0000305|PubMed:20460582"
FT   BINDING         84..112
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         127
FT                   /note="D->A: Reduces catalytic activity 2-fold."
FT                   /evidence="ECO:0000269|PubMed:20460582"
FT   MUTAGEN         128
FT                   /note="E->A: Reduces catalytic activity 20-fold."
FT                   /evidence="ECO:0000269|PubMed:20460582"
FT   MUTAGEN         259
FT                   /note="D->A: Reduces catalytic activity 4-fold."
FT                   /evidence="ECO:0000269|PubMed:20460582"
FT   MUTAGEN         295
FT                   /note="E->A,K,R: Abolishes catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:20460582"
FT   MUTAGEN         296
FT                   /note="E->A,K,R: Almost abolishes catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:20460582"
FT   MUTAGEN         332
FT                   /note="E->A: Reduces catalytic activity 20-fold."
FT                   /evidence="ECO:0000269|PubMed:20460582"
FT   MUTAGEN         360
FT                   /note="H->A: Abolishes catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:20460582"
FT   MUTAGEN         360
FT                   /note="H->K: Reduces catalytic activity 7-fold."
FT                   /evidence="ECO:0000269|PubMed:20460582"
FT   MUTAGEN         360
FT                   /note="H->R: Reduces catalytic activity 5-fold."
FT                   /evidence="ECO:0000269|PubMed:20460582"
FT   CONFLICT        146
FT                   /note="T -> A (in Ref. 1; CAA60119)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        152
FT                   /note="N -> K (in Ref. 1; CAA60119)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   498 AA;  55626 MW;  6C7EC6B760E72C36 CRC64;
     MDTLLRTPNN LEFLHGFGVK VSAFSSVKSQ KFGAKKFCEG LGSRSVCVKA SSSALLELVP
     ETKKENLDFE LPMYDPSKGV VVDLAVVGGG PAGLAVAQQV SEAGLSVCSI DPNPKLIWPN
     NYGVWVDEFE AMDLLDCLDA TWSGATVYID DNTTKDLNRP YGRVNRKQLK SKMMQKCILN
     GVKFHQAKVI KVIHEESKSM LICNDGITIQ ATVVLDATGF SRSLVQYDKP YNPGYQVAYG
     ILAEVEEHPF DVNKMVFMDW RDSHLKNNVE LKERNSRIPT FLYAMPFSSN RIFLEETSLV
     ARPGLGMDDI QERMVARLSH LGIKVKSIEE DEHCVIPMGG PLPVLPQRVV GIGGTAGMVH
     PSTGYMVART LAAAPVVANA IIQYLSSERS HSGDELSAAV WKDLWPIERR RQREFFCFGM
     DILLKLDLPA TRRFFDAFFD LEPRYWHGFL SSRLFLPELI VFGLSLFSHA SNTSRLEIMT
     KGTLPLVHMI NNLLQDKE
 
 
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