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LCPS_ARTGP
ID   LCPS_ARTGP              Reviewed;         594 AA.
AC   E4UPP6;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 1.
DT   03-AUG-2022, entry version 46.
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=MGYG_02096;
OS   Arthroderma gypseum (strain ATCC MYA-4604 / CBS 118893) (Microsporum
OS   gypseum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Nannizzia.
OX   NCBI_TaxID=535722;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4604 / CBS 118893;
RX   PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA   Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(2012).
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   -!- PATHWAY: Carotenoid biosynthesis; phytoene biosynthesis; all-trans-
CC       phytoene from geranylgeranyl diphosphate: step 1/1.
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; DS989823; EFQ99083.1; -; Genomic_DNA.
DR   RefSeq; XP_003174566.1; XM_003174518.1.
DR   AlphaFoldDB; E4UPP6; -.
DR   SMR; E4UPP6; -.
DR   STRING; 63402.XP_003174566.1; -.
DR   EnsemblFungi; EFQ99083; EFQ99083; MGYG_02096.
DR   GeneID; 10029862; -.
DR   eggNOG; KOG1459; Eukaryota.
DR   HOGENOM; CLU_012965_0_0_1; -.
DR   InParanoid; E4UPP6; -.
DR   OMA; MGFDYAL; -.
DR   OrthoDB; 303188at2759; -.
DR   UniPathway; UPA00799; UER00773.
DR   UniPathway; UPA00802; -.
DR   Proteomes; UP000002669; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; -; 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   Pfam; PF00494; SQS_PSY; 1.
DR   SFLD; SFLDG01212; Phytoene_synthase_like; 1.
DR   SUPFAM; SSF48576; SSF48576; 1.
DR   TIGRFAMs; TIGR03462; CarR_dom_SF; 2.
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..594
FT                   /note="Bifunctional lycopene cyclase/phytoene synthase"
FT                   /id="PRO_0000409231"
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        227..247
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..594
FT                   /note="Phytoene synthase"
FT                   /evidence="ECO:0000250|UniProtKB:P37295"
SQ   SEQUENCE   594 AA;  67784 MW;  481889862E516E29 CRC64;
     MGLDYLMVHV KYNLPPALLL TILYKPFFTR LEVHKIVLLC TIAVVWTIPW DSYLIRTRIW
     SYPADSVLGQ TLFQIPLEEV FFFIIQTYNT SLLYIIFNKR LVLPSYLSGP TKPLAQGLFG
     PITHRTQRDL GTLFFTGILI LGISFIYIGG EYMYLGLILS WVSPILVMQW VLMYRFLLAL
     PPASVWVPIA LPTLYLWVVD TLALRRGTWV IESGTKVDIQ LWEGLEIEEA LFFLVTNVMV
     VFGIAAMHNA AALFEYKAFI STTAMGDTPS IYQLITLFLT SSRLYDTNVL QEMSQAVTLL
     KQKSQSMYLG SAMFEGQLRL DLIALYSFCR KADDLIDDAP DRETAKYWIE QCEKALELRF
     KLKETALDDT EAYQLLTKSI PQPLHAAAHL LPASRLPKEP LSCLLQGFEI DLKFDFEKGS
     FPIATEHDLE VYAYHVAGTV ASLLLELVFR HHPVSISEAE RLRVISAGEV MGRALQYTNI
     ARDITRDAEI GRVYIPSSWL AEEGLTPSMV ISHPRNSKLI PLRRRILEKA DKCYCETQEA
     ISKLPSNVQG PVRATVTAYM EIGQVIRENE TKIWNGKLKV SRWRRFKRAW LAML
 
 
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