LCPS_LEPMJ
ID LCPS_LEPMJ Reviewed; 581 AA.
AC E4ZUB5;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 1.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=Bifunctional lycopene cyclase/phytoene synthase;
DE Includes:
DE RecName: Full=Lycopene beta-cyclase {ECO:0000250|UniProtKB:P37295};
DE EC=5.5.1.19 {ECO:0000250|UniProtKB:P37295};
DE AltName: Full=Lycopene cyclase {ECO:0000250|UniProtKB:P37295};
DE Includes:
DE RecName: Full=Phytoene synthase {ECO:0000250|UniProtKB:P37295};
DE EC=2.5.1.32 {ECO:0000250|UniProtKB:P37295};
GN ORFNames=Lema_P114090.1;
OS Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8)
OS (Blackleg fungus) (Phoma lingam).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC Leptosphaeria; Leptosphaeria maculans species complex.
OX NCBI_TaxID=985895;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8;
RX PubMed=21326234; DOI=10.1038/ncomms1189;
RA Rouxel T., Grandaubert J., Hane J.K., Hoede C., van de Wouw A.P.,
RA Couloux A., Dominguez V., Anthouard V., Bally P., Bourras S.,
RA Cozijnsen A.J., Ciuffetti L.M., Degrave A., Dilmaghani A., Duret L.,
RA Fudal I., Goodwin S.B., Gout L., Glaser N., Linglin J., Kema G.H.J.,
RA Lapalu N., Lawrence C.B., May K., Meyer M., Ollivier B., Poulain J.,
RA Schoch C.L., Simon A., Spatafora J.W., Stachowiak A., Turgeon B.G.,
RA Tyler B.M., Vincent D., Weissenbach J., Amselem J., Quesneville H.,
RA Oliver R.P., Wincker P., Balesdent M.-H., Howlett B.J.;
RT "Effector diversification within compartments of the Leptosphaeria maculans
RT genome affected by Repeat-Induced Point mutations.";
RL Nat. Commun. 2:202-202(2011).
CC -!- FUNCTION: Bifunctional enzyme that catalyzes the reactions from
CC geranylgeranyl diphosphate to phytoene (phytoene synthase) and lycopene
CC to beta-carotene via the intermediate gamma-carotene (lycopene
CC cyclase). {ECO:0000250|UniProtKB:P37295}.
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:0000250|UniProtKB:P37295};
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:0000250|UniProtKB:P37295};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 (2E,6E,10E)-geranylgeranyl diphosphate = 15-cis-phytoene + 2
CC diphosphate; Xref=Rhea:RHEA:34475, ChEBI:CHEBI:27787,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58756; EC=2.5.1.32;
CC Evidence={ECO:0000250|UniProtKB:P37295};
CC -!- PATHWAY: Carotenoid biosynthesis; beta-carotene biosynthesis.
CC {ECO:0000250|UniProtKB:P37295}.
CC -!- PATHWAY: Carotenoid biosynthesis; phytoene biosynthesis; all-trans-
CC phytoene from geranylgeranyl diphosphate: step 1/1.
CC {ECO:0000250|UniProtKB:P37295}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the lycopene beta-
CC cyclase family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the phytoene/squalene
CC synthase family. {ECO:0000305}.
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DR EMBL; FP929126; CBX94994.1; -; Genomic_DNA.
DR RefSeq; XP_003838473.1; XM_003838425.1.
DR AlphaFoldDB; E4ZUB5; -.
DR SMR; E4ZUB5; -.
DR STRING; 985895.E4ZUB5; -.
DR EnsemblFungi; CBX94994; CBX94994; LEMA_P114090.1.
DR GeneID; 13287881; -.
DR eggNOG; KOG1459; Eukaryota.
DR HOGENOM; CLU_012965_0_0_1; -.
DR InParanoid; E4ZUB5; -.
DR OMA; MGFDYAL; -.
DR OrthoDB; 303188at2759; -.
DR UniPathway; UPA00799; UER00773.
DR UniPathway; UPA00802; -.
DR Proteomes; UP000002668; Genome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0046905; F:15-cis-phytoene synthase activity; IEA:UniProt.
DR GO; GO:0004311; F:farnesyltranstransferase activity; IEA:InterPro.
DR GO; GO:0016767; F:geranylgeranyl-diphosphate geranylgeranyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016872; F:intramolecular lyase activity; IEA:InterPro.
DR GO; GO:0045436; F:lycopene beta cyclase activity; IEA:RHEA.
DR GO; GO:0016117; P:carotenoid biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd00683; Trans_IPPS_HH; 1.
DR Gene3D; 1.10.600.10; -; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR017825; Lycopene_cyclase_dom.
DR InterPro; IPR002060; Squ/phyt_synthse.
DR InterPro; IPR019845; Squalene/phytoene_synthase_CS.
DR InterPro; IPR044843; Trans_IPPS_bact-type.
DR InterPro; IPR033904; Trans_IPPS_HH.
DR Pfam; PF00494; SQS_PSY; 1.
DR SFLD; SFLDG01212; Phytoene_synthase_like; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
DR TIGRFAMs; TIGR03462; CarR_dom_SF; 2.
DR PROSITE; PS01045; SQUALEN_PHYTOEN_SYN_2; 1.
PE 3: Inferred from homology;
KW Carotenoid biosynthesis; Isomerase; Membrane; Multifunctional enzyme;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..581
FT /note="Bifunctional lycopene cyclase/phytoene synthase"
FT /id="PRO_0000409237"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 65..85
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 221..241
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..243
FT /note="Lycopene beta-cyclase"
FT /evidence="ECO:0000250|UniProtKB:P37295"
FT REGION 250..581
FT /note="Phytoene synthase"
FT /evidence="ECO:0000250|UniProtKB:P37295"
SQ SEQUENCE 581 AA; 65807 MW; AE5B91B31A0FBDD1 CRC64;
MGFDYALVHL KYTIPPAVLL TLLYRPLLTK IDVYKVAFLV TIAVVATIPW DSYLIRNRIW
SYPDHVIIGP TLFDIPLEEV FFFVVQTYNT SLLYLVLSKP TFQPVYLCTE RDELHGSWRL
KRLIGQAILL GAIAWGWFCV RERGLGTYTG LILIWAGPFL LLLWSLAYQF IIGLPFTNTL
LPIVLPTLYL WIVDTLALRR GTWVISPGTK FGVHLWDGLE IEEALFFLLT NVLIVFGQLA
FDNALAVLYA FPHLFPDPSL LPSPATLIRS LLTSCAQYDE ARLTGFREAV SRLKRKSRSF
YLASSTFQGP LRMDLLLLYS FCRVADDLVD NAATTEEARQ WIAKLHKFLD NVYRKDVVCS
SVTDQVRKEF PLDTHSALLQ LPCCKLSAEP LRDLLRGFEM DLEFNSTSPI QSTEDLVLYS
ERVAGTVAQM CIQLIFHLYP SSLTAEKRHK VVAAGNSMGV ALQYVNIARD IGVDAKIGRV
YLPTDWLSEV GLNCDTVLKD PKDPRIEALR GRLLDDAFSF YEEAKLAIAQ LPIEAQGPIR
VAVESYMEIG RTLKQDGFIV KAGRATVPKW RRVLVAWRTL N
