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Database: UniProt
Entry: G3LUM7_CUCMO
LinkDB: G3LUM7_CUCMO
Original site: G3LUM7_CUCMO 
ID   G3LUM7_CUCMO            Unreviewed;       331 AA.
AC   G3LUM7;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Lycopene epsilon cyclase {ECO:0000313|EMBL:AEN94903.1};
DE   Flags: Fragment;
GN   Name=LCYE {ECO:0000313|EMBL:AEN94903.1};
OS   Cucurbita moschata (Winter crookneck squash) (Cucurbita pepo var.
OS   moschata).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Cucurbitales; Cucurbitaceae; Cucurbiteae; Cucurbita.
OX   NCBI_TaxID=3662 {ECO:0000313|EMBL:AEN94903.1};
RN   [1] {ECO:0000313|EMBL:AEN94903.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf {ECO:0000313|EMBL:AEN94903.1};
RX   PubMed=22574777;
RA   Nakkanong K., Yang J.H., Zhang M.F.;
RT   "Carotenoid Accumulation and Carotenogenic Gene Expression during Fruit
RT   Development in Novel Interspecific Inbred Squash Lines and Their Parents.";
RL   J. Agric. Food Chem. 60:5936-5944(2012).
CC   -!- PATHWAY: Carotenoid biosynthesis. {ECO:0000256|ARBA:ARBA00004829}.
CC   -!- SIMILARITY: Belongs to the lycopene cyclase family.
CC       {ECO:0000256|ARBA:ARBA00006599}.
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DR   EMBL; JN559396; AEN94903.1; -; mRNA.
DR   AlphaFoldDB; G3LUM7; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016860; F:intramolecular oxidoreductase activity; IEA:UniProt.
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:InterPro.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR010108; Lycopene_cyclase_b/e.
DR   NCBIfam; TIGR01790; carotene-cycl; 1.
DR   PANTHER; PTHR39757; -; 1.
DR   PANTHER; PTHR39757:SF3; LYCOPENE EPSILON CYCLASE, CHLOROPLASTIC; 1.
DR   Pfam; PF05834; Lycopene_cycl; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   2: Evidence at transcript level;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        246..267
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        279..302
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AEN94903.1"
SQ   SEQUENCE   331 AA;  37101 MW;  71DFA1455B07189A CRC64;
     RCVEAGVSYL NSRVDSIIET TSGHSLLACE HDIFVPCRLA TVASGAASGK LLQYEVGGPK
     VSVQTAYGVE VEVENNPYDP RLMVFMDYRD YSKQENSSME AQYPTFLYAM PMTPTKVFFE
     ETCLASKEAM PFDLLKKKLM SRLKTMGIRI VKTYEEEWSY IPVGGSLPNT EQKNLAFGAA
     ASMVHPATGY SVVRSLSEAP KYASVIARVL KRGQLKDGLA NGRTYGNISM QAWNTLWPQE
     RKRQRAFFLF GLALIVQLDI EGIRTFFRTF FQLPDWMWQG FLGSTLSSAD LALFALYMFV
     LAPNDLRMCL VKHLVSDPTG ATMIRTYLTV S
//
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