ID LCPS_MUCCL Reviewed; 614 AA. AC Q9UUQ6; DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 13-SEP-2023, entry version 90. DE RecName: Full=Bifunctional lycopene cyclase/phytoene synthase {ECO:0000303|PubMed:10951210}; DE Includes: DE RecName: Full=Lycopene beta-cyclase {ECO:0000303|PubMed:10951210}; DE EC=5.5.1.19 {ECO:0000269|PubMed:10951210}; DE Includes: DE RecName: Full=Phytoene synthase {ECO:0000303|PubMed:10951210}; DE EC=2.5.1.32 {ECO:0000269|PubMed:10951210}; GN Name=CARRP {ECO:0000303|PubMed:10951210}; OS Mucor circinelloides f. lusitanicus (Mucor racemosus var. lusitanicus). OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina; OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor. OX NCBI_TaxID=29924; RN [1] {ECO:0000305} RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, INDUCTION, RP AND VARIANTS LYS-78; ILE-86 AND GLY-409. RC STRAIN=ATCC 1216b / BCRC 32522 / CBS 277.49 / NRRL 3631, MS21, MS35, RC and MS36; RX PubMed=10951210; DOI=10.1046/j.1432-1327.2000.01612.x; RA Velayos A., Eslava A.P., Iturriaga E.A.; RT "A bifunctional enzyme with lycopene cyclase and phytoene synthase RT activities is encoded by the carRP gene of Mucor circinelloides."; RL Eur. J. Biochem. 267:5509-5519(2000). CC -!- FUNCTION: Bifunctional enzyme that catalyzes the reactions from CC prephytoene diphosphate to phytoene and lycopene to beta-carotene via CC the intermediate gamma-carotene. {ECO:0000269|PubMed:10951210}. 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:10951210}; 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:10951210}; 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:10951210}; CC -!- PATHWAY: Carotenoid biosynthesis; beta-carotene biosynthesis. CC {ECO:0000269|PubMed:10951210}. CC -!- PATHWAY: Carotenoid biosynthesis; phytoene biosynthesis; all-trans- CC phytoene from geranylgeranyl diphosphate: step 1/1. CC {ECO:0000269|PubMed:10951210}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane CC protein {ECO:0000305}. CC -!- INDUCTION: By blue light. {ECO:0000269|PubMed:10951210}. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AJ250827; CAB60272.1; -; Genomic_DNA. DR AlphaFoldDB; Q9UUQ6; -. DR SMR; Q9UUQ6; -. DR UniPathway; UPA00799; UER00773. DR UniPathway; UPA00802; -. DR GO; GO:0016020; C:membrane; NAS:UniProtKB. 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; IEA:UniProtKB-EC. DR GO; GO:0016872; F:intramolecular lyase activity; IEA:InterPro. DR GO; GO:0045436; F:lycopene beta cyclase activity; IDA:UniProtKB. DR GO; GO:0016117; P:carotenoid biosynthetic process; IDA:UniProtKB. 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; IPR044843; Trans_IPPS_bact-type. 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; SFLDG01212; Phytoene_synthase_like; 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 Carotenoid biosynthesis; Isomerase; Membrane; Multifunctional enzyme; KW Transferase; Transmembrane; Transmembrane helix. FT CHAIN 1..614 FT /note="Bifunctional lycopene cyclase/phytoene synthase" FT /id="PRO_0000067441" FT TRANSMEM 2..22 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 36..56 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 70..90 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 120..140 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 143..163 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 174..194 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 217..237 FT /note="Helical" FT /evidence="ECO:0000255" FT REGION 1..239 FT /note="Lycopene beta-cyclase" FT /evidence="ECO:0000305|PubMed:10951210" FT REGION 246..614 FT /note="Phytoene synthase" FT /evidence="ECO:0000305|PubMed:10951210" FT VARIANT 78 FT /note="E -> K (in strain: MS21; loss of lycopene cyclase FT activity)" FT /evidence="ECO:0000269|PubMed:10951210" FT VARIANT 86 FT /note="T -> I (in strain: MS35; loss of lycopene cyclase FT activity)" FT /evidence="ECO:0000269|PubMed:10951210" FT VARIANT 409 FT /note="D -> G (in strain: MS36; loss of phytoene cyclase FT activity)" FT /evidence="ECO:0000269|PubMed:10951210" SQ SEQUENCE 614 AA; 69841 MW; 599E6BB541087FE5 CRC64; MLLTYMEVHL YYTLPVLGVL SWLSRPYYTA TDALKFKFLT LVAFTTASAW DNYIVYHKAW SYCPTCVTAV IGYVPLEEYM FFIIMTLLTV AFTNLVMRWH LHSFFIRPET PVMQSVLVRL VPITALLITA YKAWHLAVPG KPLFYGSCIL WYACPVLALL WFGAGEYMMR RPLAVLVSIA LPTLFLCWVD VVAIGAGTWD ISLATSTGKF VVPHLPVEEF MFFALINTVL VFGTCAIDRT MAILHLFKNK SPYQRPYQHS KSFLHQILEM TWAFCLPDQV LHSDTFHDLS VSWDILRKAS KSFYTASAVF PGDVRQELGV LYAFCRATDD LCDNEQVPVQ TRKEQLILTH QFVSDLFGQK TSAPTAIDWD FYNDQLPASC ISAFKSFTRL RHVLEAGAIK ELLDGYKWDL ERRSIRDQED LRYYSACVAS SVGEMCTRII LAHADKPASR QQTQWIIQRA REMGLVLQYT NIARDIVTDS EELGRCYLPQ DWLTEKEVAL IQGGLAREIG EERLLSLSHR LIYQADELMV VANKGIDKLP SHCQGGVRAA CNVYASIGTK LKSYKHHYPS RAHVGNSKRV EIALLSVYNL YTAPIATSST THCRQGKMRN LNTI //