LCPS_PHARH
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 03-AUG-2022, entry version 77.
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:MON-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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; -; 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 Pfam; PF00494; SQS_PSY; 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 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 / VKM Y-
FT 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
