ID   LCPS_SORMK              Reviewed;         602 AA.
AC   D1Z4K7; F7VQC8;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   09-FEB-2010, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   RecName: Full=Bifunctional lycopene cyclase/phytoene synthase {ECO:0000250|UniProtKB:P37295};
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=SMAC_01277;
OS   Sordaria macrospora (strain ATCC MYA-333 / DSM 997 / K(L3346) / K-hell).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Sordaria.
OX   NCBI_TaxID=771870;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-333 / DSM 997 / K(L3346) / K-hell;
RX   PubMed=20386741; DOI=10.1371/journal.pgen.1000891;
RA   Nowrousian M., Stajich J.E., Chu M., Engh I., Espagne E., Halliday K.,
RA   Kamerewerd J., Kempken F., Knab B., Kuo H.-C., Osiewacz H.D., Poeggeler S.,
RA   Read N.D., Seiler S., Smith K.M., Zickler D., Kueck U., Freitag M.;
RT   "De novo assembly of a 40 Mb eukaryotic genome from short sequence reads:
RT   Sordaria macrospora, a model organism for fungal morphogenesis.";
RL   PLoS Genet. 6:E1000891-E1000891(2010).
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; CABT02000004; CCC07710.1; -; Genomic_DNA.
DR   RefSeq; XP_003352443.1; XM_003352395.1.
DR   AlphaFoldDB; D1Z4K7; -.
DR   SMR; D1Z4K7; -.
DR   STRING; 771870.D1Z4K7; -.
DR   GeneID; 10810077; -.
DR   KEGG; smp:SMAC_01277; -.
DR   VEuPathDB; FungiDB:SMAC_01277; -.
DR   eggNOG; KOG1459; Eukaryota.
DR   HOGENOM; CLU_012965_0_0_1; -.
DR   InParanoid; D1Z4K7; -.
DR   OMA; WACPFLL; -.
DR   OrthoDB; 1088682at2759; -.
DR   UniPathway; UPA00799; UER00773.
DR   UniPathway; UPA00802; -.
DR   Proteomes; UP000001881; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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:UniProt.
DR   GO; GO:0016117; P:carotenoid biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd00683; Trans_IPPS_HH; 1.
DR   Gene3D; 1.10.600.10; Farnesyl Diphosphate Synthase; 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   NCBIfam; TIGR03462; CarR_dom_SF; 2.
DR   PANTHER; PTHR31480; BIFUNCTIONAL LYCOPENE CYCLASE/PHYTOENE SYNTHASE; 1.
DR   PANTHER; PTHR31480:SF2; PHYTOENE SYNTHASE, CHLOROPLASTIC; 1.
DR   Pfam; PF18916; Lycopene_cyc; 1.
DR   Pfam; PF00494; SQS_PSY; 1.
DR   SFLD; SFLDS00005; Isoprenoid_Synthase_Type_I; 1.
DR   SFLD; SFLDG01212; Phytoene_synthase_like; 1.
DR   SUPFAM; SSF48576; Terpenoid synthases; 1.
DR   PROSITE; PS01044; SQUALEN_PHYTOEN_SYN_1; 1.
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..602
FT                   /note="Bifunctional lycopene cyclase/phytoene synthase"
FT                   /id="PRO_0000409243"
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        30..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        76..96
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        118..138
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        146..166
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        168..188
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        230..250
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..241
FT                   /note="Lycopene beta-cyclase"
FT                   /evidence="ECO:0000250|UniProtKB:P37295"
FT   REGION          248..602
FT                   /note="Phytoene synthase"
FT                   /evidence="ECO:0000250|UniProtKB:P37295"
SQ   SEQUENCE   602 AA;  68953 MW;  D691CC1ED7B51622 CRC64;
     MYDYAFVHLK FTIPLAVLLT AIAYPVLNRI HVIQTGCLIF IAFTAALPWD AYLIEQKVWS
     YPPEAIVGPR LLGIPFEELF FFVIQTYITA LVYILFNKPV LHALHLNNQR NPPAWMRIAK
     VTGQLILVAL SVWGWKAAQV NQKTTYLGLI LVWACPFLLA IWTLAGRFIL SLPWFVTVLP
     VVLPTFYLWA VDELALHRGT WSIGSGTKLE YCLFGKLDIE EATFFLVTNM LIVSGMAVFD
     QYLAVIYAFP TLFPKVNRYP TPLMLVQSRL VNTTKYDLER IEGLREAVER LRLKSRSFYL
     ANSLFSGRLR IDLILLYSFC RLADDLVDDA KSRLEVLSWT AKLNHFLDQH YGDSDATEDP
     KQKAERIDAY IKEAFPPFAY QALHLLPTHI LPPKPLYELI KGFEMDSQFT FHGSSDSTNL
     KFPIAHDKDL KTYAIRVAGT VGELCIALII HHCLPDMSDS QKRRLESAAC RMGIALQYVN
     IARDILVDAQ IGRVYLPTSW LKEEGLTHKA VLDNPEGPEV IEKMRRRLLD NAFELYREAR
     PEMQQIPSEA RGPMIGAVEN YMEIGRVLRE KKVGQVFVRK EGRATVPKQR RLRTLLRALY
     EQ
//