LCPS_BLATR
ID LCPS_BLATR Reviewed; 608 AA.
AC Q67GH9; Q67GI1;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 63.
DE RecName: Full=Bifunctional lycopene cyclase/phytoene synthase {ECO:0000303|PubMed:15345447};
DE Includes:
DE RecName: Full=Lycopene beta-cyclase {ECO:0000303|PubMed:15345447};
DE EC=5.5.1.19 {ECO:0000269|PubMed:15345447};
DE AltName: Full=Lycopene cyclase {ECO:0000303|PubMed:15345447};
DE Includes:
DE RecName: Full=Phytoene synthase {ECO:0000303|PubMed:15345447};
DE EC=2.5.1.32 {ECO:0000269|PubMed:15345447};
GN Name=carRA {ECO:0000303|PubMed:15345447};
OS Blakeslea trispora (Choanephora trispora).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Choanephoraceae; Choanephoroideae;
OC Blakeslea.
OX NCBI_TaxID=4850;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT SER-143, FUNCTION, CATALYTIC
RP ACTIVITY, AND BIOTECHNOLOGY.
RC STRAIN=ATCC 14272 / CBS 131.59 / IMI 195169 / NRRL 2457 / QM 6309, and
RC F-744 / L25;
RX PubMed=15345447; DOI=10.1128/aem.70.9.5589-5594.2004;
RA Rodriguez-Saiz M., Paz B., De La Fuente J.L., Lopez-Nieto M.J., Cabri W.,
RA Barredo J.L.;
RT "Blakeslea trispora genes for carotene biosynthesis.";
RL Appl. Environ. Microbiol. 70:5589-5594(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=ATCC 14272 / CBS 131.59 / IMI 195169 / NRRL 2457 / QM 6309;
RX PubMed=15744487; DOI=10.1007/s00253-005-1941-2;
RA Schmidt A.D., Heinekamp T., Matuschek M., Liebmann B., Bollschweiler C.,
RA Brakhage A.A.;
RT "Analysis of mating-dependent transcription of Blakeslea trispora
RT carotenoid biosynthesis genes carB and carRA by quantitative real-time
RT PCR.";
RL Appl. Microbiol. Biotechnol. 67:549-555(2005).
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:15345447}.
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:15345447};
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:15345447};
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:15345447};
CC -!- PATHWAY: Carotenoid biosynthesis; beta-carotene biosynthesis.
CC {ECO:0000269|PubMed:15345447}.
CC -!- PATHWAY: Carotenoid biosynthesis; phytoene biosynthesis; all-trans-
CC phytoene from geranylgeranyl diphosphate: step 1/1.
CC {ECO:0000269|PubMed:15345447}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- INDUCTION: Strongly induced during mating of two strains of the
CC opposite sex. {ECO:0000269|PubMed:15744487}.
CC -!- BIOTECHNOLOGY: Beta-carotene is a popular additive for butter, ice
CC cream, orange juice and candies in the food industry. B.trispora is one
CC of the microorganisms of choice for industrial production of this
CC molecule. {ECO:0000269|PubMed:15345447}.
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; AY176662; AAO46893.1; -; Genomic_DNA.
DR EMBL; AY176663; AAO46895.1; -; Genomic_DNA.
DR EMBL; AY884174; AAX20904.1; -; Genomic_DNA.
DR AlphaFoldDB; Q67GH9; -.
DR SMR; Q67GH9; -.
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; 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 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 Carotenoid biosynthesis; Isomerase; Membrane; Multifunctional enzyme;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..608
FT /note="Bifunctional lycopene cyclase/phytoene synthase"
FT /id="PRO_0000409234"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 37..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 80..97
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..240
FT /note="Lycopene beta-cyclase"
FT /evidence="ECO:0000305|PubMed:15345447"
FT REGION 247..608
FT /note="Phytoene synthase"
FT /evidence="ECO:0000305|PubMed:15345447"
FT VARIANT 143
FT /note="P -> S (in strain: F-744 / L25; beta-carotene
FT overproducing strain)"
FT /evidence="ECO:0000269|PubMed:15345447"
SQ SEQUENCE 608 AA; 69592 MW; 346A3950D9DC459D CRC64;
MSILTYLEFH LYYTLPVLAA LCWLLKPFHS QQDNLKYKFL MLMAASTASI WDNYIVYHRA
WWYCPTCVVA VIGYVPLEEY MFFIIMTLMT VAFSNFVMRW HLHTFFIRPN TSWKQTLLVR
LVPVSALLAI TYHAWHLTLP NKPSFYGSCI LWYACPVLAI LWLGAGEYIL RRPVAVLLSI
VIPSVYLCWA DIVAISAGTW HISLRTSTGK MVVPDLPVEE CLFFTLINTV LVFATCAIDR
AQAILHLYKS SVQNQNPKQA ISLFQHVKEL AWAFCLPDQM LNNELFDDLT ISWDILRKAS
KSFYTASAVF PSYVRQDLGV LYAFCRATDD LCDDESKSVQ ERRDQLDLTR QFVRDLFSQK
TSAPIVIDWE LYQNQLPASC ISAFRAFTRL RHVLEVDPVE ELLDGYKWDL ERRPILDEQD
LEAYSACVAS SVGEMCTRVI LAQDQKENDA WIIDRAREMG LVLQYVNIAR DIVTDSETLG
RCYLPQQWLR KEETEQIQQG NARSLGDQRL LGLSLKLVGK ADAIMVRAKK GIDKLPANCQ
GGVRAACQVY AAIGSVLKQQ KTTYPTRAHL KGSERAKIAL LSVYNLYQSE DKPVALRQAR
KIKSFFVD
