ID   LCPS_GIBFU              Reviewed;         612 AA.
AC   Q8X0Z1;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   13-SEP-2023, entry version 68.
DE   RecName: Full=Bifunctional lycopene cyclase/phytoene synthase {ECO:0000303|PubMed:12172798};
DE   Includes:
DE     RecName: Full=Lycopene beta-cyclase {ECO:0000303|PubMed:12172798};
DE              EC=5.5.1.19 {ECO:0000269|PubMed:12172798};
DE     AltName: Full=Carotene cyclase {ECO:0000303|PubMed:12172798};
DE     AltName: Full=Lycopene cyclase {ECO:0000303|PubMed:12172798};
DE   Includes:
DE     RecName: Full=Phytoene synthase {ECO:0000303|PubMed:12172798};
DE              EC=2.5.1.32 {ECO:0000269|PubMed:12172798};
GN   Name=carRA {ECO:0000303|PubMed:12172798};
OS   Gibberella fujikuroi (Bakanae and foot rot disease fungus) (Fusarium
OS   fujikuroi).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium fujikuroi species complex.
OX   NCBI_TaxID=5127;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   INDUCTION.
RX   PubMed=12172798; DOI=10.1007/s00438-002-0690-5;
RA   Linnemannstons P., Prado M.M., Fernandez-Martin R., Tudzynski B.,
RA   Avalos J.;
RT   "A carotenoid biosynthesis gene cluster in Fusarium fujikuroi: the genes
RT   carB and carRA.";
RL   Mol. Genet. Genomics 267:593-602(2002).
CC   -!- FUNCTION: Bifunctional enzyme; part of the car gene cluster that
CC       mediates the biosynthesis of neurosporaxanthin, a carboxylic
CC       apocarotenoid acting as an essential protective pigments and leading to
CC       orange pigmentation (PubMed:12172798). CarAR catalyzes the first step
CC       of the pathway by converting geranylgeranyl diphosphate to phytoene, as
CC       well as the later cyclization step that transforms the carB product
CC       lycopene into gamma-carotene (PubMed:12172798). CarAR also converts
CC       part of gamma-carotene into beta-carotene (PubMed:12172798).
CC       Neurosporaxanthin is synthesized from geranyl-geranyl pyrophosphate
CC       (GGPP) through several enzymatic activities. Phytoene synthase activity
CC       performed by the bifunctional enzyme carAR first produces phytoene from
CC       geranyl-geranyl pyrophosphate (GGPP). The phytoene dehydrogenase carB
CC       then introduces 4 desaturations to lead to lycopene which is substrate
CC       of the carotene cyclase activity of carAR that leads to the production
CC       of gamma-carotene. CarB then performs a 5th desaturation reaction to
CC       yield torulene. Torulene is the substrate of the dioxidase carT that
CC       breaks the molecule, removing five carbon atoms to yield beta-apo-4'-
CC       carotenal, whereas the aldehyde dehydrogenase carD mediates the last
CC       step by converting beta-apo-4'-carotenal into neurosporaxanthin
CC       (Probable). {ECO:0000269|PubMed:12172798, ECO:0000305|PubMed:12172798}.
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:12172798};
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:12172798};
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:12172798};
CC   -!- PATHWAY: Carotenoid biosynthesis; beta-carotene biosynthesis.
CC       {ECO:0000269|PubMed:12172798}.
CC   -!- PATHWAY: Carotenoid biosynthesis; phytoene biosynthesis; all-trans-
CC       phytoene from geranylgeranyl diphosphate: step 1/1.
CC       {ECO:0000269|PubMed:12172798}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- INDUCTION: Induced by light. {ECO:0000269|PubMed:12172798}.
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; AJ426417; CAD19988.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8X0Z1; -.
DR   SMR; Q8X0Z1; -.
DR   eggNOG; KOG1459; Eukaryota.
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; IMP:UniProtKB.
DR   GO; GO:0004311; F:farnesyltranstransferase activity; IEA:InterPro.
DR   GO; GO:0016767; F:geranylgeranyl-diphosphate geranylgeranyltransferase activity; IMP:UniProtKB.
DR   GO; GO:0016872; F:intramolecular lyase activity; IEA:InterPro.
DR   GO; GO:0045436; F:lycopene beta cyclase activity; IMP:UniProtKB.
DR   GO; GO:0016120; P:carotene biosynthetic process; IMP:UniProtKB.
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; 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; 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..612
FT                   /note="Bifunctional lycopene cyclase/phytoene synthase"
FT                   /id="PRO_0000409236"
FT   TRANSMEM        3..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        31..51
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        112..130
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        148..168
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        171..191
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        203..223
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        246..266
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..268
FT                   /note="Lycopene beta-cyclase"
FT                   /evidence="ECO:0000305|PubMed:12172798"
FT   REGION          275..612
FT                   /note="Phytoene synthase"
FT                   /evidence="ECO:0000305|PubMed:12172798"
SQ   SEQUENCE   612 AA;  69458 MW;  14F7D731B993AB65 CRC64;
     MGWEYAQVHL KYTIPFGVVL AAVYRPLMSR LDVFKLVFLI TVSFFWVVKG LEANSCRLLL
     FLPCMLILRG VLLRLTNADS PWDSYLIKNR IWTYPPGVVV GLTAWDIPAE ELFFFVIQTF
     NTSLLYMILS KPTFHPIYLS KKTGWGKIAG QILFASAIIF GLVSVSSGGE GMYMGLILIW
     ACPFLLFLWS ISYQFIVNLP WTNTALPIAL PTLYLWVVDT FALRRGTWSI TSGTKYGVVL
     WDGLEIEEAV FFLLTNTLIV FGLIACDNNL AILDTFPEHF PRTKGVPSLL TIIRTLILPK
     EKYDEERIQG LVSAVALLRK KSRSFYLASG TFEGRLRIDL IRLYAFCRAA DDLVDEAPSV
     DDSRASIEKL RKFLDLAYEE NQEEPSQRLR EYVTSSIPEM FHMALLQLPT YYLPKQPLDD
     LLKGFDTDLL FDRKSGAFPI ETTEDLDIYG SRVAGTVAEL CNHLILYHTP EAVPEDIQRE
     VVASGQEMGI ALQYVNIARD IKTDAEIDRV YLPLSWLKEA QLTPEDVIQQ PHGPTIEALR
     HKLLDRAFEK YNMAKGAIDK LPSEGKGPIR VAVESYMEIG RVLREKGPTM KKGRATVPKM
     RRIRVAWSAL NK
//