ID   LCPS_TRIVH              Reviewed;         595 AA.
AC   D4D802;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   02-SEP-2026, entry version 62.
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=TRV_03236;
OS   Trichophyton verrucosum (strain HKI 0517).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=663202;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HKI 0517;
RX   PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA   Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA   Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA   Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA   Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA   Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT   "Comparative and functional genomics provide insights into the
RT   pathogenicity of dermatophytic fungi.";
RL   Genome Biol. 12:R7.1-R7.16(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       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:34476;
CC         Evidence={ECO:0000250|UniProtKB:P37295};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 (2E,6E,10E)-geranylgeranyl diphosphate = (1R,2R,3R)-
CC         prephytoene diphosphate + diphosphate; Xref=Rhea:RHEA:22296,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:58011, ChEBI:CHEBI:58756;
CC         Evidence={ECO:0000250|UniProtKB:P37295};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22297;
CC         Evidence={ECO:0000250|UniProtKB:P37295};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(1R,2R,3R)-prephytoene diphosphate = 15-cis-phytoene +
CC         diphosphate; Xref=Rhea:RHEA:34479, ChEBI:CHEBI:27787,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:58011;
CC         Evidence={ECO:0000250|UniProtKB:P37295};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:34480;
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:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
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; ACYE01000166; EFE42031.1; -; Genomic_DNA.
DR   RefSeq; XP_003022649.1; XM_003022603.1.
DR   AlphaFoldDB; D4D802; -.
DR   SMR; D4D802; -.
DR   GeneID; 9581308; -.
DR   KEGG; tve:TRV_03236; -.
DR   HOGENOM; CLU_012965_0_0_1; -.
DR   OrthoDB; 3294at34384; -.
DR   UniPathway; UPA00799; UER00773.
DR   UniPathway; UPA00802; -.
DR   Proteomes; UP000008383; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046905; F:15-cis-phytoene synthase activity; ISS:UniProtKB.
DR   GO; GO:0004311; F:geranylgeranyl diphosphate synthase activity; IEA:InterPro.
DR   GO; GO:0016872; F:intramolecular lyase activity; IEA:InterPro.
DR   GO; GO:0045436; F:lycopene beta cyclase activity; ISS:UniProtKB.
DR   GO; GO:0051996; F:squalene synthase [NAD(P)H] activity; IEA:InterPro.
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   Pfam; PF00494; SQS_PSY; 1.
DR   SFLD; SFLDS00005; Isoprenoid_Synthase_Type_I; 1.
DR   SFLD; SFLDG01212; Phytoene_synthase_like; 1.
DR   SFLD; SFLDG01018; Squalene/Phytoene_Synthase_Lik; 1.
DR   SUPFAM; SSF48576; Terpenoid synthases; 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..595
FT                   /note="Bifunctional lycopene cyclase/phytoene synthase"
FT                   /id="PRO_0000409245"
FT   TRANSMEM        3..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        35..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        77..97
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        130..150
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        153..173
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        176..196
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        231..251
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..249
FT                   /note="Lycopene beta-cyclase"
FT                   /evidence="ECO:0000250|UniProtKB:P37295"
FT   REGION          256..595
FT                   /note="Phytoene synthase"
FT                   /evidence="ECO:0000250|UniProtKB:P37295"
SQ   SEQUENCE   595 AA;  67801 MW;  E0171F8312E69275 CRC64;
     MGLDYLMVHV KYNIPPALLL TILYKPFFTR LEVYKIVFLC TIAVVWTTPW DSYLIRTRVW
     SYPADSVIGH TIFRIPLEEA FFFIIQTYNT SLIYILFNKR LILLPYLSGP IKPLTQGLFG
     TVALRTWRDF GILFFTGISV LGISCIRAGG EYMYLGLILS WISPILLLQW PLMYRFLLGL
     PPASLWVPIV LPTLYLWIVD TLALRRGTWV IESGTKVDIQ LWDGLELEEA LFFLVTNVMI
     VLGIAGMDNA IALFEYKAFV STTAVGETPS IPRLLTLFFT RSRRYCDTNV LREMSQAVTL
     LKQKSQTMYL GSAMFEGQLR LDLVALYSFC RKADDLIDDA PNRATAQYWI KQCEKALELR
     FKLKGAALDN TAAYQQLTKS IPPQLHAAVH LLPASRLPKG PLSDLLKGFE IDMKFDSERG
     IFPIATEHDL EVYAYHVAGT IATLLLELVF RHHPVSISDS ERLRVISAGE GMGRALQYTN
     IARDIVRDAE IGRVYIPSVW LAEQGLTPSM VVNQPRNPKL IPLRRRLLDK AEKCYRDTQE
     AISELPANVR APVRATVTVY MDIGQVIREN EMKVWNGKLK VSRWRRFKGA WLAMS
//