LCPS_COLGM
ID LCPS_COLGM Reviewed; 587 AA.
AC E3Q717;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 1.
DT 03-AUG-2022, entry version 43.
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=GLRG_02475;
OS Colletotrichum graminicola (strain M1.001 / M2 / FGSC 10212) (Maize
OS anthracnose fungus) (Glomerella graminicola).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum graminicola species complex.
OX NCBI_TaxID=645133;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M1.001 / M2 / FGSC 10212;
RX PubMed=22885923; DOI=10.1038/ng.2372;
RA O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J.,
RA Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., Altmueller J.,
RA Alvarado-Balderrama L., Bauser C.A., Becker C., Birren B.W., Chen Z.,
RA Choi J., Crouch J.A., Duvick J.P., Farman M.A., Gan P., Heiman D.,
RA Henrissat B., Howard R.J., Kabbage M., Koch C., Kracher B., Kubo Y.,
RA Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., Moore N., Neumann U.,
RA Nordstroem K., Panaccione D.G., Panstruga R., Place M., Proctor R.H.,
RA Prusky D., Rech G., Reinhardt R., Rollins J.A., Rounsley S., Schardl C.L.,
RA Schwartz D.C., Shenoy N., Shirasu K., Sikhakolli U.R., Stueber K.,
RA Sukno S.A., Sweigard J.A., Takano Y., Takahara H., Trail F.,
RA van der Does H.C., Voll L.M., Will I., Young S., Zeng Q., Zhang J.,
RA Zhou S., Dickman M.B., Schulze-Lefert P., Ver Loren van Themaat E.,
RA Ma L.-J., Vaillancourt L.J.;
RT "Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered
RT by genome and transcriptome analyses.";
RL Nat. Genet. 44:1060-1065(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 {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; GG697335; EFQ26655.1; -; Genomic_DNA.
DR RefSeq; XP_008090675.1; XM_008092484.1.
DR AlphaFoldDB; E3Q717; -.
DR SMR; E3Q717; -.
DR STRING; 645133.E3Q717; -.
DR EnsemblFungi; EFQ26655; EFQ26655; GLRG_02475.
DR GeneID; 24407840; -.
DR VEuPathDB; FungiDB:GLRG_02475; -.
DR eggNOG; KOG1459; Eukaryota.
DR HOGENOM; CLU_012965_0_0_1; -.
DR OrthoDB; 303188at2759; -.
DR UniPathway; UPA00799; UER00773.
DR UniPathway; UPA00802; -.
DR Proteomes; UP000008782; 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; PS01044; SQUALEN_PHYTOEN_SYN_1; 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..587
FT /note="Bifunctional lycopene cyclase/phytoene synthase"
FT /id="PRO_0000409235"
FT TRANSMEM 8..28
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 120..140
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 220..240
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..587
FT /note="Phytoene synthase"
FT /evidence="ECO:0000250|UniProtKB:P37295"
SQ SEQUENCE 587 AA; 64983 MW; 6D39085251FBB666 CRC64;
MGYDYALVHV KYTIPLAALL TVFSYPVFTR LDVVRTLFIV TIAFVATIPW DSYLIRTNVW
TYPPDAVLGP TLYDIPAEEL FFFIIQTYIT AQLYIILNKP VLHAQYLNSP ATLPQWIKSG
KLVGQLALSG SVLLGTWLIA KKGEGTYLGL ILVWACTFAL FTWTITAHFL LALPLACTAL
PILLPTVYLW IVDEMALGRG TWAIESGTKL ELQLFGSLEI EEATFFLVTN MLIVFGIAAF
DKAVAVCDAF PEKFDKPADA LAMSLLRARV FPSSKYDMQR ILGIRQAAAR LAKKSRSFHL
ASSVFPGRLR IDLTLLYSYC RLADDLVDDA ATPEEAAVWI SKLDRHLSLL YKDPDATSTP
LASKYAAENF PPSALSALDM LPTSLLPREP LAELLKGFEM DLSFSNSAFP IADPEDLELY
AARVASTVGQ ACLELVFCHC QHGLPDYMKA YLRNTARQMG LALQFVNISR DIAVDAKIGR
VYLPTTWLKE EGLTPEDVLK SPNSEGVGKV RRRILAKALD HYGEARDSMK WIPSEARGPM
IVAVESYMEI GRVLMRNGGS AAADGSGRAT VPKSRRIWVA WSTLMAA
