ID   LCPS_ASPNC              Reviewed;         582 AA.
AC   A2QM49;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   27-MAR-2024, entry version 75.
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=An07g00800;
OS   Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=425011;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4892 / CBS 513.88 / FGSC A1513;
RX   PubMed=17259976; DOI=10.1038/nbt1282;
RA   Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA   Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA   Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA   Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA   Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA   d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA   Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA   van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA   Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA   van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA   Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA   Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA   Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA   Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT   "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT   niger CBS 513.88.";
RL   Nat. Biotechnol. 25:221-231(2007).
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; AM270119; CAK39303.1; -; Genomic_DNA.
DR   AlphaFoldDB; A2QM49; -.
DR   EnsemblFungi; CAK39303; CAK39303; An07g00800.
DR   VEuPathDB; FungiDB:An07g00800; -.
DR   HOGENOM; CLU_012965_0_0_1; -.
DR   UniPathway; UPA00799; UER00773.
DR   UniPathway; UPA00802; -.
DR   Proteomes; UP000006706; Chromosome 4L.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046905; F:15-cis-phytoene synthase activity; IEA:UniProt.
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   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   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   SUPFAM; SSF48576; Terpenoid synthases; 1.
PE   3: Inferred from homology;
KW   Carotenoid biosynthesis; Isomerase; Membrane; Multifunctional enzyme;
KW   Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..582
FT                   /note="Bifunctional lycopene cyclase/phytoene synthase"
FT                   /id="PRO_0000409232"
FT   TRANSMEM        34..54
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        59..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        99..121
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        142..162
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        170..190
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        242..262
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..261
FT                   /note="Lycopene beta-cyclase"
FT                   /evidence="ECO:0000250|UniProtKB:P37295"
FT   REGION          268..582
FT                   /note="Phytoene synthase"
FT                   /evidence="ECO:0000250|UniProtKB:P37295"
SQ   SEQUENCE   582 AA;  65647 MW;  88E8322BC29400BA CRC64;
     MNQNGTRLCY SVREVPPTSF VSAPANYKRA SSHCTYTIPA ASALTVLYYP FFTAQDRCKI
     CILITIAILA TLPWDSYLIR SAIWTYPPDA VVGLKILDIP IEEVFFFAIQ TYITSLTYCI
     FTKPLVRPMY LRSHLERRGT RYVVATVILA LMGGGTACLL LGRRMTYLGL ILVWACPILL
     FQWMMSYPFL SELPWKPTIT SICLPTLHLW FADSRAMGTG TWRIEEGTKL NFRIGGLELE
     EALFFLVSNM MVVLGLVGCD YAYALQEYES LSQPASDVYI TLRKALSLLA RPLPIDASLI
     SALSQAVYRL QEKSQSMFLG SALFQGQLRI DLIFLYSFCR VMDDLIDEAE DEQEARFWVT
     ECRHLLDSTH RSEPHSDHFY TGKKGEEHER LRQSISYLPP SHLSNDSFDD LLKGFEIDLK
     FNPQREAFPI QSEYCLDQYA GFVAGTVGVL VFDLTLFHCG HYFIQDVPRL RRAAKDMGKA
     MQCQPRGDGG ATSGRKRAIA GNRGELYGYW TTAEGAERHK PGASVEDEGA FGATAKSWLA
     GDVITELCHC FIQAEYVIYL VRHQNASADT LVLLSALVYR LE
//