ID   LCPS_BLATR              Reviewed;         608 AA.
AC   Q67GH9; Q67GI1;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   02-SEP-2026, entry version 73.
DE   RecName: Full=Bifunctional lycopene cyclase/phytoene synthase {ECO:0000303|PubMed:15345447};
DE   Includes:
DE     RecName: Full=Lycopene beta-cyclase {ECO:0000303|PubMed:15345447};
DE              EC=5.5.1.19 {ECO:0000269|PubMed:15345447};
DE     AltName: Full=Lycopene cyclase {ECO:0000303|PubMed:15345447};
DE   Includes:
DE     RecName: Full=Phytoene synthase {ECO:0000303|PubMed:15345447};
DE              EC=2.5.1.32 {ECO:0000269|PubMed:15345447};
GN   Name=carRA {ECO:0000303|PubMed:15345447};
OS   Blakeslea trispora (Choanephora trispora).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Choanephoraceae; Choanephoroideae;
OC   Blakeslea.
OX   NCBI_TaxID=4850;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT SER-143, FUNCTION, CATALYTIC
RP   ACTIVITY, AND BIOTECHNOLOGY.
RC   STRAIN=ATCC 14272 / CBS 131.59 / IMI 195169 / NRRL 2457 / QM 6309, and
RC   F-744 / L25;
RX   PubMed=15345447; DOI=10.1128/aem.70.9.5589-5594.2004;
RA   Rodriguez-Saiz M., Paz B., De La Fuente J.L., Lopez-Nieto M.J., Cabri W.,
RA   Barredo J.L.;
RT   "Blakeslea trispora genes for carotene biosynthesis.";
RL   Appl. Environ. Microbiol. 70:5589-5594(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC   STRAIN=ATCC 14272 / CBS 131.59 / IMI 195169 / NRRL 2457 / QM 6309;
RX   PubMed=15744487; DOI=10.1007/s00253-005-1941-2;
RA   Schmidt A.D., Heinekamp T., Matuschek M., Liebmann B., Bollschweiler C.,
RA   Brakhage A.A.;
RT   "Analysis of mating-dependent transcription of Blakeslea trispora
RT   carotenoid biosynthesis genes carB and carRA by quantitative real-time
RT   PCR.";
RL   Appl. Microbiol. Biotechnol. 67:549-555(2005).
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:0000269|PubMed:15345447}.
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:15345447};
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:15345447};
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:0000269|PubMed:15345447};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:34476;
CC         Evidence={ECO:0000269|PubMed:15345447};
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:0000269|PubMed:15345447};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22297;
CC         Evidence={ECO:0000269|PubMed:15345447};
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:0000269|PubMed:15345447};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:34480;
CC         Evidence={ECO:0000269|PubMed:15345447};
CC   -!- PATHWAY: Carotenoid biosynthesis; beta-carotene biosynthesis.
CC       {ECO:0000269|PubMed:15345447}.
CC   -!- PATHWAY: Carotenoid biosynthesis; phytoene biosynthesis; all-trans-
CC       phytoene from geranylgeranyl diphosphate: step 1/1.
CC       {ECO:0000269|PubMed:15345447}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- INDUCTION: Strongly induced during mating of two strains of the
CC       opposite sex. {ECO:0000269|PubMed:15744487}.
CC   -!- BIOTECHNOLOGY: Beta-carotene is a popular additive for butter, ice
CC       cream, orange juice and candies in the food industry. B.trispora is one
CC       of the microorganisms of choice for industrial production of this
CC       molecule. {ECO:0000269|PubMed:15345447}.
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; AY176662; AAO46893.1; -; Genomic_DNA.
DR   EMBL; AY176663; AAO46895.1; -; Genomic_DNA.
DR   EMBL; AY884174; AAX20904.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q67GH9; -.
DR   SMR; Q67GH9; -.
DR   OrthoDB; 6600518at2759; -.
DR   UniPathway; UPA00799; UER00773.
DR   UniPathway; UPA00802; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046905; F:15-cis-phytoene synthase activity; IDA: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; IDA:UniProtKB.
DR   GO; GO:0051996; F:squalene synthase [NAD(P)H] activity; IEA:InterPro.
DR   GO; GO:0016120; P:carotene biosynthetic process; IDA:UniProtKB.
DR   CDD; cd00683; Trans_IPPS_HH; 1.
DR   FunFam; 1.10.600.10:FF:000020; Phytoene synthase; 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   1: Evidence at protein level;
KW   Carotenoid biosynthesis; Isomerase; Membrane; Multifunctional enzyme;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..608
FT                   /note="Bifunctional lycopene cyclase/phytoene synthase"
FT                   /id="PRO_0000409234"
FT   TRANSMEM        3..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        37..56
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        80..97
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        117..137
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        150..170
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        175..195
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        218..238
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..240
FT                   /note="Lycopene beta-cyclase"
FT                   /evidence="ECO:0000305|PubMed:15345447"
FT   REGION          247..608
FT                   /note="Phytoene synthase"
FT                   /evidence="ECO:0000305|PubMed:15345447"
FT   VARIANT         143
FT                   /note="P -> S (in strain: F-744 / L25; beta-carotene
FT                   overproducing strain)"
FT                   /evidence="ECO:0000269|PubMed:15345447"
SQ   SEQUENCE   608 AA;  69592 MW;  346A3950D9DC459D CRC64;
     MSILTYLEFH LYYTLPVLAA LCWLLKPFHS QQDNLKYKFL MLMAASTASI WDNYIVYHRA
     WWYCPTCVVA VIGYVPLEEY MFFIIMTLMT VAFSNFVMRW HLHTFFIRPN TSWKQTLLVR
     LVPVSALLAI TYHAWHLTLP NKPSFYGSCI LWYACPVLAI LWLGAGEYIL RRPVAVLLSI
     VIPSVYLCWA DIVAISAGTW HISLRTSTGK MVVPDLPVEE CLFFTLINTV LVFATCAIDR
     AQAILHLYKS SVQNQNPKQA ISLFQHVKEL AWAFCLPDQM LNNELFDDLT ISWDILRKAS
     KSFYTASAVF PSYVRQDLGV LYAFCRATDD LCDDESKSVQ ERRDQLDLTR QFVRDLFSQK
     TSAPIVIDWE LYQNQLPASC ISAFRAFTRL RHVLEVDPVE ELLDGYKWDL ERRPILDEQD
     LEAYSACVAS SVGEMCTRVI LAQDQKENDA WIIDRAREMG LVLQYVNIAR DIVTDSETLG
     RCYLPQQWLR KEETEQIQQG NARSLGDQRL LGLSLKLVGK ADAIMVRAKK GIDKLPANCQ
     GGVRAACQVY AAIGSVLKQQ KTTYPTRAHL KGSERAKIAL LSVYNLYQSE DKPVALRQAR
     KIKSFFVD
//