ID E3RN48_PYRTT Unreviewed; 755 AA.
AC E3RN48;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Bifunctional lycopene cyclase/phytoene synthase {ECO:0000256|ARBA:ARBA00018909};
DE EC=2.5.1.32 {ECO:0000256|ARBA:ARBA00012396};
DE EC=5.5.1.19 {ECO:0000256|ARBA:ARBA00012242};
GN ORFNames=PTT_09938 {ECO:0000313|EMBL:EFQ92860.1};
OS Pyrenophora teres f. teres (strain 0-1) (Barley net blotch fungus)
OS (Drechslera teres f. teres).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=861557 {ECO:0000313|Proteomes:UP000001067};
RN [1] {ECO:0000313|EMBL:EFQ92860.1, ECO:0000313|Proteomes:UP000001067}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0-1 {ECO:0000313|EMBL:EFQ92860.1,
RC ECO:0000313|Proteomes:UP000001067};
RX PubMed=21067574; DOI=10.1186/gb-2010-11-11-r109;
RA Ellwood S.R., Liu Z., Syme R.A., Lai Z., Hane J.K., Keiper F., Moffat C.S.,
RA Oliver R.P., Friesen T.L.;
RT "A first genome assembly of the barley fungal pathogen Pyrenophora teres f.
RT teres.";
RL Genome Biol. 11:R109.1-R109.14(2010).
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:0000256|ARBA:ARBA00001805};
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:0000256|ARBA:ARBA00029335};
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:0000256|ARBA:ARBA00029313};
CC -!- PATHWAY: Carotenoid biosynthesis; beta-carotene biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005089}.
CC -!- PATHWAY: Carotenoid biosynthesis; phytoene biosynthesis; all-trans-
CC phytoene from geranylgeranyl diphosphate: step 1/1.
CC {ECO:0000256|ARBA:ARBA00005172}.
CC -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC biosynthesis. {ECO:0000256|ARBA:ARBA00004687}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the PIGC family.
CC {ECO:0000256|ARBA:ARBA00008321}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the phytoene/squalene
CC synthase family. {ECO:0000256|ARBA:ARBA00008406}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the lycopene beta-
CC cyclase family. {ECO:0000256|ARBA:ARBA00008247}.
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DR EMBL; GL534142; EFQ92860.1; -; Genomic_DNA.
DR RefSeq; XP_003299027.1; XM_003298979.1.
DR AlphaFoldDB; E3RN48; -.
DR STRING; 861557.E3RN48; -.
DR EnsemblFungi; EFQ92860; EFQ92860; PTT_09938.
DR KEGG; pte:PTT_09938; -.
DR eggNOG; KOG1459; Eukaryota.
DR eggNOG; KOG3059; Eukaryota.
DR HOGENOM; CLU_012965_0_0_1; -.
DR OrthoDB; 1088682at2759; -.
DR UniPathway; UPA00196; -.
DR UniPathway; UPA00799; UER00773.
DR UniPathway; UPA00802; -.
DR Proteomes; UP000001067; Unassembled WGS sequence.
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 GO; GO:0006506; P:GPI anchor biosynthetic process; IEA:UniProtKB-UniPathway.
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; IPR009450; Plno_GlcNAc_GPI2.
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; PF06432; GPI2; 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 {ECO:0000256|ARBA:ARBA00022746};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Reference proteome {ECO:0000313|Proteomes:UP000001067};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 36..55
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 80..97
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 118..137
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 170..192
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 607..635
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 641..659
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 698..717
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 729..747
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 755 AA; 85669 MW; A6908AB754A1F77D CRC64;
MGFDYALVHL KYTIPPAVLL TWLYRPFFTK LDVYKVGYLV FVAVVSTIPW DSYLIRTGIW
SYPSHVIIGP KLYDIPLEEV FFFIIQTYNT SLLYLLLSRP TFQPVYLKTE RGTAQRQWRY
MRLAGQVFFL ALIAWGWRCI RRGGLGTYTG LILVWAGPFL LMLWTLAYQF ILALPLTNTA
LPIFLPTLYL WVVDTLALRR GTWVISTGTK YGLNLWDGLE IEEAVFFLAT NVLIVFGQLA
FDNALAVLYT FPHLFTDPSL LPSPVLLMRA LLTPCSKYDD LRIKGLDEAV HRLKRKSRSF
YLASATFPGP LRADLLLLYS FCRVADDLVD NASDADEARA WIAKMRNFLN NVYNDKLPQS
AVHTQIYDDF PPSTQSAFLQ LPATKLSPQP LEDLLHGFEM DLAFQQGPII STAENLRVYS
ERVAGTVAQM CIQLIFYWYP STLAIGEKNA IVAAGNSMGV ALQYVNIARD IEVDAQIGRV
YLPLNWLFEA GLSYDDVLKK PNQAQIQTLR KHLLNDAFSV YEKAKDSIER LPIEARGPIR
VAVESYMEIG RILRNEQYQV KAGRATVPKS RRIVVAWRTL NLPDNYTDET TFLDHLQRNP
RLQPYEFWSL MSDATVIVQH LASVIIFCCC FVAIIQNRVS PIAVVGWASI CTVLAWLLWD
HWMGQEFDII ANVPTSNTEE SVPNAPQAYS LRTQQRIATA KSAVLIYAAL LGLSPILKSL
TRSTTSDSIW ALSTWLLMMN VAFFDYTGGT GAQYE
//
