LCPS_PYRTR
ID LCPS_PYRTR Reviewed; 583 AA.
AC B2WAQ3;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 54.
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=PTRG_07366;
OS Pyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spot fungus)
OS (Drechslera tritici-repentis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=426418;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pt-1C-BFP;
RX PubMed=23316438; DOI=10.1534/g3.112.004044;
RA Manning V.A., Pandelova I., Dhillon B., Wilhelm L.J., Goodwin S.B.,
RA Berlin A.M., Figueroa M., Freitag M., Hane J.K., Henrissat B., Holman W.H.,
RA Kodira C.D., Martin J., Oliver R.P., Robbertse B., Schackwitz W.,
RA Schwartz D.C., Spatafora J.W., Turgeon B.G., Yandava C., Young S., Zhou S.,
RA Zeng Q., Grigoriev I.V., Ma L.-J., Ciuffetti L.M.;
RT "Comparative genomics of a plant-pathogenic fungus, Pyrenophora tritici-
RT repentis, reveals transduplication and the impact of repeat elements on
RT pathogenicity and population divergence.";
RL G3 (Bethesda) 3:41-63(2013).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DS231621; EDU50285.1; -; Genomic_DNA.
DR RefSeq; XP_001937698.1; XM_001937663.1.
DR AlphaFoldDB; B2WAQ3; -.
DR SMR; B2WAQ3; -.
DR STRING; 45151.EDU50285; -.
DR EnsemblFungi; EDU50285; EDU50285; PTRG_07366.
DR GeneID; 6345639; -.
DR eggNOG; KOG1459; Eukaryota.
DR HOGENOM; CLU_012965_0_0_1; -.
DR InParanoid; B2WAQ3; -.
DR OMA; MGFDYAL; -.
DR OrthoDB; 303188at2759; -.
DR UniPathway; UPA00799; UER00773.
DR UniPathway; UPA00802; -.
DR Proteomes; UP000001471; 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:RHEA.
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 SFLD; SFLDG01018; Squalene/Phytoene_Synthase_Lik; 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..583
FT /note="Bifunctional lycopene cyclase/phytoene synthase"
FT /id="PRO_0000409242"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..97
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 221..241
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..243
FT /note="Lycopene beta-cyclase"
FT /evidence="ECO:0000250|UniProtKB:P37295"
FT REGION 250..583
FT /note="Phytoene synthase"
FT /evidence="ECO:0000250|UniProtKB:P37295"
SQ SEQUENCE 583 AA; 66281 MW; F0851DA16FAE327E CRC64;
MGFDYALVHL KYTIPPAVLL TWLYRPFFTK LDVYKVGYLV SIAVASTIPW DSYLIRTGIW
SYPTHVIIGP KLCDIPLEEV FFFIIQTYNT SLLYLLLSRP TFQPVYLNTE RGAARRQWRY
MRLAGQVFFL ALIAWGWRCI RHGGLGTYTG LILVWAGPFL LMLWSLAYQF ILALPVTNTA
LPIFLPTLYL WVVDTLALRR GTWVISTGTK YGLHLWDGLE IEEALFFLAT NALIVFGQLA
FDNALAVLYT FPHLFTGPSL LPSPVLLMRA LLTPCSKYHD ARIKGLDEAV NRLKRKSRSF
YLASATFPGP LRADLLLLYS FCRVADDLVD NASDADEARA WIAKMRKFLN NVYSDKLPQS
VVHSQICDDF PPSTQSALLQ LPATKLSPQP LEDLLHGFEM DLAFQQGPII RTMEDLRVYS
ERVAGTVAQM CIQLIFYWYP STLDTEEKNV IVAAGNSMGV ALQYVNIARD IEVDAQIGRV
YLPLNWLSEA GLSYDDVLKK PNQAQIQTLR KHLLNHAFSV YEKAKDSIER LPIEARGPIR
VAVESYMEIG RILRSEQYQV KAGRATVPKS RRIMVAWRTL NSK
