ID   LCPS_PODAN              Reviewed;         593 AA.
AC   B2ATB0; A0A090CF73;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   27-MAR-2024, entry version 69.
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   OrderedLocusNames=Pa_1_15240; ORFNames=PODANS_1_15240;
OS   Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383)
OS   (Pleurage anserina).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Podosporaceae; Podospora;
OC   Podospora anserina.
OX   NCBI_TaxID=515849;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383;
RX   PubMed=18460219; DOI=10.1186/gb-2008-9-5-r77;
RA   Espagne E., Lespinet O., Malagnac F., Da Silva C., Jaillon O., Porcel B.M.,
RA   Couloux A., Aury J.-M., Segurens B., Poulain J., Anthouard V.,
RA   Grossetete S., Khalili H., Coppin E., Dequard-Chablat M., Picard M.,
RA   Contamine V., Arnaise S., Bourdais A., Berteaux-Lecellier V., Gautheret D.,
RA   de Vries R.P., Battaglia E., Coutinho P.M., Danchin E.G.J., Henrissat B.,
RA   El Khoury R., Sainsard-Chanet A., Boivin A., Pinan-Lucarre B., Sellem C.H.,
RA   Debuchy R., Wincker P., Weissenbach J., Silar P.;
RT   "The genome sequence of the model ascomycete fungus Podospora anserina.";
RL   Genome Biol. 9:R77.1-R77.22(2008).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383;
RX   PubMed=24558260; DOI=10.1534/genetics.113.159988;
RA   Grognet P., Bidard F., Kuchly C., Tong L.C.H., Coppin E., Benkhali J.A.,
RA   Couloux A., Wincker P., Debuchy R., Silar P.;
RT   "Maintaining two mating types: Structure of the mating type locus and its
RT   role in heterokaryosis in Podospora anserina.";
RL   Genetics 197:421-432(2014).
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; CU633899; CAP67633.1; -; Genomic_DNA.
DR   EMBL; FO904936; CDP23892.1; -; Genomic_DNA.
DR   RefSeq; XP_001906962.1; XM_001906927.1.
DR   AlphaFoldDB; B2ATB0; -.
DR   SMR; B2ATB0; -.
DR   STRING; 515849.B2ATB0; -.
DR   GeneID; 6191495; -.
DR   KEGG; pan:PODANSg3995; -.
DR   VEuPathDB; FungiDB:PODANS_1_15240; -.
DR   eggNOG; KOG1459; Eukaryota.
DR   HOGENOM; CLU_012965_0_0_1; -.
DR   InParanoid; B2ATB0; -.
DR   OrthoDB; 1088682at2759; -.
DR   UniPathway; UPA00799; UER00773.
DR   UniPathway; UPA00802; -.
DR   Proteomes; UP000001197; Chromosome 1.
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; 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   3: Inferred from homology;
KW   Carotenoid biosynthesis; Isomerase; Membrane; Multifunctional enzyme;
KW   Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..593
FT                   /note="Bifunctional lycopene cyclase/phytoene synthase"
FT                   /id="PRO_0000409241"
FT   TRANSMEM        8..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        31..51
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        77..97
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        117..136
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        147..167
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        169..189
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        231..251
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..242
FT                   /note="Lycopene beta-cyclase"
FT                   /evidence="ECO:0000250|UniProtKB:P37295"
FT   REGION          249..593
FT                   /note="Phytoene synthase"
FT                   /evidence="ECO:0000250|UniProtKB:P37295"
SQ   SEQUENCE   593 AA;  66914 MW;  B7430708736FDB86 CRC64;
     MAYDYALVHL KYTIPLAALL TVIAYPIFHR IHFLQIGSLI VVSFLATLPW DSYLIRSNIW
     TYPPDAIIGP RLYGIPIEEL FFFVIQTYIT SLFYILLSKP LFHPLYLSTQ RNPPQRIARG
     KVIGQGILVA LTLYGVHQIR TGGPGTYLGL ILAWAFPFAL LTFTVAGRFI LTLPLTSTVV
     PIIIPTVYLW LVDELALGRG TWAIESGTKL GWCLFGVLDI EEATFFLATN ILIVFGMAVF
     DQYLAIIFAF PHLFPKVPRS PTPLMLVQSR FSNTKQYDLE RIAGLSDAVT RLKAKSRSFY
     LANSLFTGRL RIDLILLYSF CRLADDLVDD STSRTEVKSW TTKLYKFLDL HYKSDVKANK
     ARINDYIDEA FPPEAKSALK YLPATILPSQ PLYQLIEGFE LDSQFSFHDS SESAKYPIVD
     EDKLNYYGQC VAGTVGELCV ALIIEHCEPE MPDERKKMLM SVSRTMGVAL QYVNIARDIV
     VDAEMGRVYL PTTWLKEEGL TPEDVVAHPR GKHVENLRRR LLSEAFKLYD EARPKMNGIP
     KEARGPMIGA VETYMEIGRV LRELEGGVEL ERGKATVPGG RRLKTVLKAL FSA
//