LCPS_PHYB8
ID LCPS_PHYB8 Reviewed; 602 AA.
AC Q9P854; Q9P877;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=Bifunctional lycopene cyclase/phytoene synthase {ECO:0000303|PubMed:11172012};
DE Includes:
DE RecName: Full=Lycopene beta-cyclase {ECO:0000303|PubMed:11172012};
DE EC=5.5.1.19 {ECO:0000269|PubMed:11172012};
DE AltName: Full=Lycopene cyclase {ECO:0000303|PubMed:11172012};
DE Includes:
DE RecName: Full=Phytoene synthase {ECO:0000303|PubMed:11172012};
DE EC=2.5.1.32 {ECO:0000269|PubMed:11172012};
GN Name=carRA {ECO:0000303|PubMed:11172012};
OS Phycomyces blakesleeanus (strain ATCC 8743b / DSM 1359 / FGSC 10004 / NBRC
OS 33097 / NRRL 1555).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Phycomycetaceae; Phycomyces.
OX NCBI_TaxID=763407;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF GLU-77; PRO-215; ILE-465
RP AND PRO-482, FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 8743b / DSM 1359 / FGSC 10004 / NBRC 33097 / NRRL 1555;
RX PubMed=11172012; DOI=10.1073/pnas.98.4.1687;
RA Arrach N., Fernandez-Martin R., Cerda-Olmedo E., Avalos J.;
RT "A single gene for lycopene cyclase, phytoene synthase, and regulation of
RT carotene biosynthesis in Phycomyces.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:1687-1692(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 8743b / DSM 1359 / FGSC 10004 / NBRC 33097 / NRRL 1555;
RA Sanz C.S., Benito E.P., Eslava A.P.;
RT "The carRA gene of Phycomyces blakesleeanus.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
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:0000269|PubMed:11172012}.
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:11172012};
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:11172012};
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:11172012};
CC -!- PATHWAY: Carotenoid biosynthesis; beta-carotene biosynthesis.
CC {ECO:0000269|PubMed:11172012}.
CC -!- PATHWAY: Carotenoid biosynthesis; phytoene biosynthesis; all-trans-
CC phytoene from geranylgeranyl diphosphate: step 1/1.
CC {ECO:0000269|PubMed:11172012}.
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; AJ278287; CAB93661.1; -; Genomic_DNA.
DR EMBL; AJ276965; CAB86388.1; -; Genomic_DNA.
DR RefSeq; XP_018294563.1; XM_018438264.1.
DR AlphaFoldDB; Q9P854; -.
DR SMR; Q9P854; -.
DR GeneID; 28999170; -.
DR VEuPathDB; FungiDB:PHYBL_180114; -.
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; IMP:UniProtKB.
DR GO; GO:0004311; F:farnesyltranstransferase activity; IEA:InterPro.
DR GO; GO:0016767; F:geranylgeranyl-diphosphate geranylgeranyltransferase activity; IMP:UniProtKB.
DR GO; GO:0016872; F:intramolecular lyase activity; IEA:InterPro.
DR GO; GO:0045436; F:lycopene beta cyclase activity; IMP:UniProtKB.
DR GO; GO:0016120; P:carotene biosynthetic process; IMP: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; 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 1: Evidence at protein level;
KW Carotenoid biosynthesis; Isomerase; Membrane; Multifunctional enzyme;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..602
FT /note="Bifunctional lycopene cyclase/phytoene synthase"
FT /id="PRO_0000409240"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 211..231
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..238
FT /note="Lycopene beta-cyclase"
FT /evidence="ECO:0000305|PubMed:11172012"
FT REGION 245..602
FT /note="Phytoene synthase"
FT /evidence="ECO:0000305|PubMed:11172012"
FT MUTAGEN 77
FT /note="E->K: In carR23; abolishes lycopene cyclase
FT activity, rich in lycopene and insensitive to retinol."
FT /evidence="ECO:0000269|PubMed:11172012"
FT MUTAGEN 215
FT /note="P->S: In carR21; abolishes lycopene cyclase
FT activity, rich in lycopene and insensitive to retinol."
FT /evidence="ECO:0000269|PubMed:11172012"
FT MUTAGEN 465
FT /note="I->T: In carA113; reduces the response to chemical
FT activation."
FT /evidence="ECO:0000269|PubMed:11172012"
FT MUTAGEN 482
FT /note="P->L: In carA5; abolishes phytoene synthase activity
FT resulting in a 10- to 15-fold reduction of the beta-
FT carotene content."
FT /evidence="ECO:0000269|PubMed:11172012"
FT CONFLICT 436
FT /note="A -> G (in Ref. 2; CAB86388)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 602 AA; 68670 MW; FF2C7525405D7F99 CRC64;
MLTYMEVHLY FTLPVLALLA FLYKPFFTTK DRFKYIFLCT VAFATASPWD NYIVYHKAWS
YCPECVTAVI GYVPLEEYMF FIIMTLITVT FTSLTMRWTL PSFFIRPETP VFQSVCVRYI
PIVGFLTIAA KAWASSIPDS HPFYGACILW YVCPVLALLW IGSGEYMLRR WKAVLFSIAV
PTIFLCWVDQ YAIARGTWDI SRRTSTGIMV LPSLPLEEFL FFLLIDTVLV FASCATDRAH
AIVHIYITPM NHNKVSTWYM DFFYLCWAFL QTDQALSGET LSDLDATWRI LREASASFYT
ASSVFSFEAR QDLGVLYGFC RATDDLADNN DVSVPDRKKQ LELVRGFVRQ MFDSKHGHPD
IDWTQYSGSI PDSFIAAFRS FTRLRDVLEI KAVEELLDGY TFDLEQREVK NEDDLVYYSA
CVASSVGEMC TRVLMASEPG GNRTMLKWTV ERARDMGLAL QLTNIARDIV TDSKQLGRSY
VPRDWLTSQE SALLKAGKAR ELGDERLRQI ALKMVYTADD LNLMASRAID YLPPSSRCGV
RAACNVYTAI GVSLHKANGY PDRAHLTKLE RMKVTFRCVY GFRKGHQGVQ GDRGKSQAFT
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