LCYB_SYNE7
ID LCYB_SYNE7 Reviewed; 411 AA.
AC Q55276; Q31LH7;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Lycopene beta cyclase {ECO:0000305};
DE EC=5.5.1.19 {ECO:0000269|PubMed:7919981, ECO:0000269|PubMed:8344419};
DE AltName: Full=Lycopene cyclase {ECO:0000303|PubMed:8344419};
GN Name=crtL {ECO:0000303|PubMed:7919981};
GN Synonyms=lcy {ECO:0000303|PubMed:8344419};
GN OrderedLocusNames=Synpcc7942_2062;
OS Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS R2).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=1140;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, AND PATHWAY.
RC STRAIN=PCC 7942 / FACHB-805;
RX PubMed=7919981; DOI=10.2307/3869889;
RA Cunningham F.X. Jr., Sun Z., Chamovitz D., Hirschberg J., Gannt E.;
RT "Molecular structure and enzymatic function of lycopene cyclase from the
RT cyanobacterium Synechococcus sp strain PCC7942.";
RL Plant Cell 6:1107-1121(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND PATHWAY.
RC STRAIN=PCC 7942 / FACHB-805;
RX PubMed=8344419; DOI=10.1016/0014-5793(93)80980-9;
RA Cunningham F.X. Jr., Chamovitz D., Misawa N., Gantt E., Hirschberg J.;
RT "Cloning and functional expression in Escherichia coli of a cyanobacterial
RT gene for lycopene cyclase, the enzyme that catalyzes the biosynthesis of
RT beta-carotene.";
RL FEBS Lett. 328:130-138(1993).
CC -!- FUNCTION: Catalyzes the double cyclization reaction which converts
CC lycopene to beta-carotene (PubMed:7919981, PubMed:8344419). It also
CC converts neurosporene to the monocyclic beta-zeacarotene but does not
CC cyclize zeta-carotene (PubMed:7919981). {ECO:0000269|PubMed:7919981,
CC ECO:0000269|PubMed:8344419}.
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:7919981,
CC ECO:0000269|PubMed:8344419};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55621;
CC Evidence={ECO:0000269|PubMed:7919981, ECO:0000269|PubMed:8344419};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-lycopene = gamma-carotene; Xref=Rhea:RHEA:32219,
CC ChEBI:CHEBI:15948, ChEBI:CHEBI:27740; EC=5.5.1.19;
CC Evidence={ECO:0000269|PubMed:7919981, ECO:0000269|PubMed:8344419};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32220;
CC Evidence={ECO:0000269|PubMed:7919981, ECO:0000269|PubMed:8344419};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=gamma-carotene = all-trans-beta-carotene;
CC Xref=Rhea:RHEA:32239, ChEBI:CHEBI:17579, ChEBI:CHEBI:27740;
CC EC=5.5.1.19; Evidence={ECO:0000269|PubMed:7919981,
CC ECO:0000269|PubMed:8344419};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32240;
CC Evidence={ECO:0000269|PubMed:7919981, ECO:0000269|PubMed:8344419};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-neurosporene = beta-zeacarotene;
CC Xref=Rhea:RHEA:67976, ChEBI:CHEBI:16833, ChEBI:CHEBI:27533;
CC EC=5.5.1.19; Evidence={ECO:0000269|PubMed:7919981};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67977;
CC Evidence={ECO:0000269|PubMed:7919981};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P21687};
CC -!- ACTIVITY REGULATION: Inhibited by the bleaching herbicide 2-(4-
CC methylphenoxy)triethylamine hydrochloride (MPTA).
CC {ECO:0000269|PubMed:7919981, ECO:0000269|PubMed:8344419}.
CC -!- PATHWAY: Carotenoid biosynthesis; beta-carotene biosynthesis.
CC {ECO:0000269|PubMed:7919981, ECO:0000269|PubMed:8344419}.
CC -!- PATHWAY: Carotenoid biosynthesis; beta-zeacarotene biosynthesis.
CC {ECO:0000269|PubMed:7919981}.
CC -!- SIMILARITY: Belongs to the lycopene cyclase family. {ECO:0000305}.
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DR EMBL; X74599; CAA52677.1; -; Genomic_DNA.
DR EMBL; CP000100; ABB58092.1; -; Genomic_DNA.
DR RefSeq; WP_011378296.1; NC_007604.1.
DR AlphaFoldDB; Q55276; -.
DR SMR; Q55276; -.
DR STRING; 1140.Synpcc7942_2062; -.
DR PRIDE; Q55276; -.
DR EnsemblBacteria; ABB58092; ABB58092; Synpcc7942_2062.
DR KEGG; syf:Synpcc7942_2062; -.
DR eggNOG; COG0644; Bacteria.
DR HOGENOM; CLU_032956_1_0_3; -.
DR OMA; QTCYGIV; -.
DR OrthoDB; 1597893at2; -.
DR BioCyc; SYNEL:SYNPCC7942_2062-MON; -.
DR BRENDA; 5.5.1.19; 7781.
DR UniPathway; UPA00802; -.
DR UniPathway; UPA00805; -.
DR GO; GO:0045436; F:lycopene beta cyclase activity; IEA:RHEA.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR GO; GO:0016117; P:carotenoid biosynthetic process; IEA:UniProtKB-KW.
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; FAD; Flavoprotein; Isomerase; NAD; NADP.
FT CHAIN 1..411
FT /note="Lycopene beta cyclase"
FT /id="PRO_0000134985"
FT BINDING 4..32
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
SQ SEQUENCE 411 AA; 46085 MW; C46CC5B2E85E7AC2 CRC64;
MFDALVIGSG PAGLAIAAEL AQRGLKVQGL SPVDPFHPWE NTYGIWGPEL DSLGLEHLFG
HRWSNCVSYF GEAPVQHQYN YGLFDRAQLQ QHWLRQCEQG GLQWQLGKAA AIAHDSHHSC
VTTAAGQELQ ARLVVDTTGH QAAFIQRPHS DAIAYQAAYG IIGQFSQPPI EPHQFVLMDY
RSDHLSPEER QLPPTFLYAM DLGNDVYFVE ETSLAACPAI PYDRLKQRLY QRLATRGVTV
QVIQHEEYCL FPMNLPLPDL TQSVVGFGGA ASMVHPASGY MVGALLRRAP DLANAIAAGL
NASSSLTTAE LATQAWRGLW PTEKIRKHYI YQFGLEKLMR FSEAQLNHHF QTFFGLPKEQ
WYGFLTNTLS LPELIQAMLR LFAQAPNDVR WGLMEQQGRE LQLFWQAIAA R
