LCPS_PODAN
ID LCPS_PODAN Reviewed; 593 AA.
AC B2ATB0; A0A090CF73;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 62.
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 OrderedLocusNames=Pa_1_15240; ORFNames=PODANS_1_15240;
OS Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383)
OS (Pleurage anserina).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Podosporaceae; Podospora;
OC Podospora anserina.
OX NCBI_TaxID=515849;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383;
RX PubMed=18460219; DOI=10.1186/gb-2008-9-5-r77;
RA Espagne E., Lespinet O., Malagnac F., Da Silva C., Jaillon O., Porcel B.M.,
RA Couloux A., Aury J.-M., Segurens B., Poulain J., Anthouard V.,
RA Grossetete S., Khalili H., Coppin E., Dequard-Chablat M., Picard M.,
RA Contamine V., Arnaise S., Bourdais A., Berteaux-Lecellier V., Gautheret D.,
RA de Vries R.P., Battaglia E., Coutinho P.M., Danchin E.G.J., Henrissat B.,
RA El Khoury R., Sainsard-Chanet A., Boivin A., Pinan-Lucarre B., Sellem C.H.,
RA Debuchy R., Wincker P., Weissenbach J., Silar P.;
RT "The genome sequence of the model ascomycete fungus Podospora anserina.";
RL Genome Biol. 9:R77.1-R77.22(2008).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383;
RX PubMed=24558260; DOI=10.1534/genetics.113.159988;
RA Grognet P., Bidard F., Kuchly C., Tong L.C.H., Coppin E., Benkhali J.A.,
RA Couloux A., Wincker P., Debuchy R., Silar P.;
RT "Maintaining two mating types: Structure of the mating type locus and its
RT role in heterokaryosis in Podospora anserina.";
RL Genetics 197:421-432(2014).
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; CU633899; CAP67633.1; -; Genomic_DNA.
DR EMBL; FO904936; CDP23892.1; -; Genomic_DNA.
DR RefSeq; XP_001906962.1; XM_001906927.1.
DR AlphaFoldDB; B2ATB0; -.
DR SMR; B2ATB0; -.
DR STRING; 515849.B2ATB0; -.
DR EnsemblFungi; CAP67633; CAP67633; PODANS_1_15240.
DR GeneID; 6191495; -.
DR KEGG; pan:PODANSg3995; -.
DR VEuPathDB; FungiDB:PODANS_1_15240; -.
DR eggNOG; KOG1459; Eukaryota.
DR HOGENOM; CLU_012965_0_0_1; -.
DR OrthoDB; 303188at2759; -.
DR UniPathway; UPA00799; UER00773.
DR UniPathway; UPA00802; -.
DR Proteomes; UP000001197; Chromosome 1.
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..593
FT /note="Bifunctional lycopene cyclase/phytoene synthase"
FT /id="PRO_0000409241"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..136
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 231..251
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..593
FT /note="Phytoene synthase"
FT /evidence="ECO:0000250|UniProtKB:P37295"
SQ SEQUENCE 593 AA; 66914 MW; B7430708736FDB86 CRC64;
MAYDYALVHL KYTIPLAALL TVIAYPIFHR IHFLQIGSLI VVSFLATLPW DSYLIRSNIW
TYPPDAIIGP RLYGIPIEEL FFFVIQTYIT SLFYILLSKP LFHPLYLSTQ RNPPQRIARG
KVIGQGILVA LTLYGVHQIR TGGPGTYLGL ILAWAFPFAL LTFTVAGRFI LTLPLTSTVV
PIIIPTVYLW LVDELALGRG TWAIESGTKL GWCLFGVLDI EEATFFLATN ILIVFGMAVF
DQYLAIIFAF PHLFPKVPRS PTPLMLVQSR FSNTKQYDLE RIAGLSDAVT RLKAKSRSFY
LANSLFTGRL RIDLILLYSF CRLADDLVDD STSRTEVKSW TTKLYKFLDL HYKSDVKANK
ARINDYIDEA FPPEAKSALK YLPATILPSQ PLYQLIEGFE LDSQFSFHDS SESAKYPIVD
EDKLNYYGQC VAGTVGELCV ALIIEHCEPE MPDERKKMLM SVSRTMGVAL QYVNIARDIV
VDAEMGRVYL PTTWLKEEGL TPEDVVAHPR GKHVENLRRR LLSEAFKLYD EARPKMNGIP
KEARGPMIGA VETYMEIGRV LRELEGGVEL ERGKATVPGG RRLKTVLKAL FSA
