ID   LCPS_PHARH              Reviewed;         673 AA.
AC   Q7Z859; Q7Z856; Q9UUQ0;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   13-SEP-2023, entry version 80.
DE   RecName: Full=Bifunctional lycopene cyclase/phytoene synthase {ECO:0000303|PubMed:10589832};
DE   Includes:
DE     RecName: Full=Lycopene beta-cyclase {ECO:0000303|PubMed:10589832};
DE              EC=5.5.1.19 {ECO:0000269|PubMed:10589832};
DE     AltName: Full=Lycopene cyclase {ECO:0000303|PubMed:10589832};
DE   Includes:
DE     RecName: Full=Phytoene synthase {ECO:0000303|PubMed:10589832};
DE              EC=2.5.1.32 {ECO:0000269|PubMed:10589832};
GN   Name=crtYB {ECO:0000303|PubMed:10589832}; Synonyms=pbs;
OS   Phaffia rhodozyma (Yeast) (Xanthophyllomyces dendrorhous).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Cystofilobasidiales; Mrakiaceae; Phaffia.
OX   NCBI_TaxID=264483;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=CBS 6938 / CCRC 22365 / VKM Y-2793;
RX   PubMed=10589832; DOI=10.1007/s004380051105;
RA   Verdoes J.C., Krubasik K.P., Sandmann G., van Ooyen A.J.;
RT   "Isolation and functional characterisation of a novel type of carotenoid
RT   biosynthetic gene from Xanthophyllomyces dendrorhous.";
RL   Mol. Gen. Genet. 262:453-461(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=ATCC 24230 / UCD 67-385;
RX   PubMed=12902257; DOI=10.1128/aem.69.8.4676-4682.2003;
RA   Lodato P., Alcaino J., Barahona S., Retamales P., Cifuentes V.;
RT   "Alternative splicing of transcripts from crtI and crtYB genes of
RT   Xanthophyllomyces dendrorhous.";
RL   Appl. Environ. Microbiol. 69:4676-4682(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC   STRAIN=ATCC 24230 / UCD 67-385;
RX   PubMed=18769767; DOI=10.4067/s0716-97602008000100011;
RA   Niklitschek M., Alcaino J., Barahona S., Sepulveda D., Lozano C.,
RA   Carmona M., Marcoleta A., Martinez C., Lodato P., Baeza M., Cifuentes V.;
RT   "Genomic organization of the structural genes controlling the astaxanthin
RT   biosynthesis pathway of Xanthophyllomyces dendrorhous.";
RL   Biol. Res. 41:93-108(2008).
RN   [4]
RP   FUNCTION.
RX   PubMed=16928467; DOI=10.1016/j.bbalip.2006.06.002;
RA   Sandmann G., Zhu C., Krubasik P., Fraser P.D.;
RT   "The biotechnological potential of the al-2 gene from Neurospora crassa for
RT   the production of monocyclic keto hydroxy carotenoids.";
RL   Biochim. Biophys. Acta 1761:1085-1092(2006).
RN   [5]
RP   INDUCTION.
RC   STRAIN=ATCC 24230 / UCD 67-385;
RX   PubMed=17657357; DOI=10.4067/s0716-97602007000100008;
RA   Lodato P., Alcaino J., Barahona S., Niklitschek M., Carmona M., Wozniak A.,
RA   Baeza M., Jimenez A., Cifuentes V.;
RT   "Expression of the carotenoid biosynthesis genes in Xanthophyllomyces
RT   dendrorhous.";
RL   Biol. Res. 40:73-84(2007).
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). The cyclase preferentially catalyzes the symmetric
CC       cyclization of both ends of the substrate to produce dicyclic
CC       carotenoids. Beta-carotene is further processed to the acidic
CC       carotenoid astaxanthin. {ECO:0000269|PubMed:10589832,
CC       ECO:0000269|PubMed:16928467}.
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:0000269|PubMed:10589832};
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:0000269|PubMed:10589832};
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:0000269|PubMed:10589832};
CC   -!- PATHWAY: Carotenoid biosynthesis; beta-carotene biosynthesis.
CC       {ECO:0000269|PubMed:10589832}.
CC   -!- PATHWAY: Carotenoid biosynthesis; phytoene biosynthesis; all-trans-
CC       phytoene from geranylgeranyl diphosphate: step 1/1.
CC       {ECO:0000269|PubMed:10589832}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q7Z859-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q7Z859-2; Sequence=VSP_041283;
CC   -!- INDUCTION: Down-regulated in stationary phase.
CC       {ECO:0000269|PubMed:17657357, ECO:0000269|PubMed:18769767}.
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; AJ133646; CAB51949.1; -; Genomic_DNA.
DR   EMBL; AY174117; AAO73816.1; -; mRNA.
DR   EMBL; AY177204; AAO47570.1; -; mRNA.
DR   EMBL; DQ016503; AAY33923.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q7Z859; -.
DR   BioCyc; MetaCyc:MONOMER-17247; -.
DR   BRENDA; 2.5.1.32; 4710.
DR   BRENDA; 5.5.1.19; 4710.
DR   UniPathway; UPA00799; UER00773.
DR   UniPathway; UPA00802; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046905; F:15-cis-phytoene synthase activity; IDA:UniProtKB.
DR   GO; GO:0004311; F:farnesyltranstransferase activity; IEA:InterPro.
DR   GO; GO:0016767; F:geranylgeranyl-diphosphate geranylgeranyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0016872; F:intramolecular lyase activity; IEA:InterPro.
DR   GO; GO:0045436; F:lycopene beta cyclase activity; IDA:UniProtKB.
DR   GO; GO:0016120; P:carotene biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0016117; P:carotenoid biosynthetic process; IEA:UniProtKB-KW.
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; IPR002060; Squ/phyt_synthse.
DR   InterPro; IPR019845; Squalene/phytoene_synthase_CS.
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; PF00494; SQS_PSY; 1.
DR   SFLD; SFLDS00005; Isoprenoid_Synthase_Type_I; 1.
DR   SFLD; SFLDG01018; Squalene/Phytoene_Synthase_Lik; 1.
DR   SUPFAM; SSF48576; Terpenoid synthases; 1.
DR   PROSITE; PS01045; SQUALEN_PHYTOEN_SYN_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Carotenoid biosynthesis; Isomerase; Membrane;
KW   Multifunctional enzyme; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..673
FT                   /note="Bifunctional lycopene cyclase/phytoene synthase"
FT                   /id="PRO_0000409239"
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        36..56
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        81..101
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        117..137
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        157..177
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        187..207
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        226..246
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..251
FT                   /note="Lycopene beta-cyclase"
FT                   /evidence="ECO:0000305|PubMed:10589832"
FT   REGION          258..673
FT                   /note="Phytoene synthase"
FT                   /evidence="ECO:0000305|PubMed:10589832"
FT   REGION          376..399
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        384..399
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1..46
FT                   /note="MTALAYYQIHLIYTLPILGLLGLLTSPILTKFDIYKISILVFIAFS -> MS
FT                   PYLFFVLHTTHVCICV (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12902257"
FT                   /id="VSP_041283"
FT   VARIANT         307
FT                   /note="E -> K (in strain: CBS 6938 / CCRC 22365 /
FT                   VKMY-2793)"
SQ   SEQUENCE   673 AA;  74736 MW;  ECAB54AF256240A2 CRC64;
     MTALAYYQIH LIYTLPILGL LGLLTSPILT KFDIYKISIL VFIAFSATTP WDSWIIRNGA
     WTYPSAESGQ GVFGTFLDVP YEEYAFFVIQ TVITGLVYVL ATRHLLPSLA LPKTRSSALS
     LALKALIPLP IIYLFTAHPS PSPDPLVTDH YFYMRALSLL ITPPTMLLAA LSGEYAFDWK
     SGRAKSTIAA IMIPTVYLIW VDYVAVGQDS WSINDEKIVG WRLGGVLPIE EAMFFLLTNL
     MIVLGLSACD HTQALYLLHG RTIYGNKKMP SSFPLITPPV LSLFFSSRPY SSQPKRDLEL
     AVKLLEEKSR SFFVASAGFP SEVRERLVGL YAFCRVTDDL IDSPEVSSNP HATIDMVSDF
     LTLLFGPPLH PSQPDKILSS PLLPPSHPSR PTGMYPLPPP PSLSPAELVQ FLTERVPVQY
     HFAFRLLAKL QGLIPRYPLD ELLRGYTTDL IFPLSTEAVQ ARKTPIETTA DLLDYGLCVA
     GSVAELLVYV SWASAPSQVP ATIEEREAVL VASREMGTAL QLVNIARDIK GDATEGRFYL
     PLSFFGLRDE SKLAIPTDWT EPRPQDFDKL LSLSPSSTLP SSNASESFRF EWKTYSLPLV
     AYAEDLAKHS YKGIDRLPTE VQAGMRAACA SYLLIGREIK VVWKGDVGER RTVAGWRRVR
     KVLSVVMSGW EGQ
//