LOS_BOTBR
ID LOS_BOTBR Reviewed; 444 AA.
AC A0A142ZC57;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 08-JUN-2016, sequence version 1.
DT 03-AUG-2022, entry version 21.
DE RecName: Full=Lycopaoctaene synthase {ECO:0000303|PubMed:27050299};
DE EC=2.5.1.148 {ECO:0000269|PubMed:27050299};
DE AltName: Full=Squalene synthase-like LOS {ECO:0000305};
DE EC=2.5.1.21 {ECO:0000269|PubMed:27050299};
GN Name=LOS {ECO:0000303|PubMed:27050299};
OS Botryococcus braunii (Green alga).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Trebouxiophyceae incertae sedis; Elliptochloris clade; Botryococcus.
OX NCBI_TaxID=38881;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=Race L;
RX PubMed=27050299; DOI=10.1038/ncomms11198;
RA Thapa H.R., Naik M.T., Okada S., Takada K., Molnar I., Xu Y.,
RA Devarenne T.P.;
RT "A squalene synthase-like enzyme initiates production of tetraterpenoid
RT hydrocarbons in Botryococcus braunii Race L.";
RL Nat. Commun. 7:11198-11198(2016).
RN [2]
RP FUNCTION, AND MUTAGENESIS OF SER-276 AND ALA-288.
RC STRAIN=Race L;
RX PubMed=28813599; DOI=10.1021/acschembio.7b00457;
RA Thapa H.R., Tang S., Sacchettini J.C., Devarenne T.P.;
RT "Tetraterpene synthase substrate and product specificity in the green
RT microalga Botryococcus braunii race L.";
RL ACS Chem. Biol. 12:2408-2416(2017).
CC -!- FUNCTION: Converts the C20 geranylgeranyl diphosphate (GGPP) to the C40
CC lycopaoctaene, the first committed intermediate in the production of
CC lycopadiene (PubMed:27050299, PubMed:28813599). Converts farnesyl
CC diphosphate (FPP) into squalene, a precursor for sterol biosynthesis in
CC eukaryotes (PubMed:27050299, PubMed:28813599). Converts with low
CC efficiency the C20 phytyl diphosphate (PPP) to the C40 lycopadiene in
CC vitro. This reaction may not have biological significance in vivo
CC (PubMed:27050299). {ECO:0000269|PubMed:27050299,
CC ECO:0000269|PubMed:28813599}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 (2E,6E)-farnesyl diphosphate + H(+) + NADH = 2 diphosphate +
CC NAD(+) + squalene; Xref=Rhea:RHEA:32299, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15440, ChEBI:CHEBI:33019, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:175763; EC=2.5.1.21;
CC Evidence={ECO:0000269|PubMed:27050299};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 (2E,6E)-farnesyl diphosphate + H(+) + NADPH = 2 diphosphate
CC + NADP(+) + squalene; Xref=Rhea:RHEA:32295, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15440, ChEBI:CHEBI:33019, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:175763; EC=2.5.1.21;
CC Evidence={ECO:0000269|PubMed:27050299};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 (2E,6E,10E)-geranylgeranyl diphosphate + H(+) + NADPH = all-
CC trans-lycopaoctaene + 2 diphosphate + NADP(+); Xref=Rhea:RHEA:58176,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:58756, ChEBI:CHEBI:142538;
CC EC=2.5.1.148; Evidence={ECO:0000269|PubMed:27050299};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P37268};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.07 mM for geranylgeranyl diphosphate
CC {ECO:0000269|PubMed:27050299};
CC KM=0.13 mM for farnesyl diphosphate {ECO:0000269|PubMed:27050299};
CC KM=0.11 mM for phytil diphosphate {ECO:0000269|PubMed:27050299};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the phytoene/squalene synthase family.
CC {ECO:0000305}.
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DR EMBL; KT388101; AMV49169.1; -; mRNA.
DR AlphaFoldDB; A0A142ZC57; -.
DR SMR; A0A142ZC57; -.
DR KEGG; ag:AMV49169; -.
DR BioCyc; MetaCyc:MON-20363; -.
DR BRENDA; 2.5.1.148; 915.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004310; F:farnesyl-diphosphate farnesyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051996; F:squalene synthase activity; IDA:UniProtKB.
DR GO; GO:0016126; P:sterol biosynthetic process; IDA:UniProtKB.
DR CDD; cd00683; Trans_IPPS_HH; 1.
DR Gene3D; 1.10.600.10; -; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR002060; Squ/phyt_synthse.
DR InterPro; IPR006449; Squal_synth-like.
DR InterPro; IPR019845; Squalene/phytoene_synthase_CS.
DR InterPro; IPR044844; Trans_IPPS_euk-type.
DR InterPro; IPR033904; Trans_IPPS_HH.
DR PANTHER; PTHR11626; PTHR11626; 1.
DR Pfam; PF00494; SQS_PSY; 1.
DR SFLD; SFLDG01018; Squalene/Phytoene_Synthase_Lik; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
DR TIGRFAMs; TIGR01559; squal_synth; 1.
DR PROSITE; PS01045; SQUALEN_PHYTOEN_SYN_2; 1.
PE 1: Evidence at protein level;
KW Magnesium; Membrane; Metal-binding; NAD; NADP; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..444
FT /note="Lycopaoctaene synthase"
FT /id="PRO_0000446504"
FT TRANSMEM 391..411
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 415..435
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 48
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P37268"
FT BINDING 73
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P37268"
FT BINDING 76
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P37268"
FT BINDING 79
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P37268"
FT BINDING 80
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P37268"
FT BINDING 215
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P37268"
FT BINDING 315
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P37268"
FT BINDING 317
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P37268"
FT MUTAGEN 276
FT /note="S->Y: Loss of lycopaoctaene synthase activity; when
FT associated with F-288."
FT /evidence="ECO:0000269|PubMed:28813599"
FT MUTAGEN 288
FT /note="A->F: Loss of lycopaoctaene synthase activity; when
FT associated with Y-276."
FT /evidence="ECO:0000269|PubMed:28813599"
SQ SEQUENCE 444 AA; 50278 MW; 5820ABC9F5045FA9 CRC64;
MKYTDFLAHP DEIIPTIRMM YADYRLKNME IKDPSVRFCY NMLNRVSRSF AMVIQQLPVE
LRDATCVFYL ILRALDTVED DMAIPKEVKI PMLRTFHEHL SDRSWKIKCG YGPYVDLMDN
YPLVTDVYLR FDEGTKAVIK DITRRMGNGM ADFIDLDEVL TIPQYDLYCH YVAGLCGIGM
CKLFVDSGLE KEDLVAEEDL ANQMGLFLQK NNIVRDYLED INELPAPRMF WPKEIWGNYA
KQLDEFKDPK NLDKAMLCLN HMVTDALRHC EVGLRSLSLL HNPNILRAVL IPQVMGVRTL
TLVYNNPEVF RGVVKMRRGE TAKIFVTTTS KLSFFRTYLQ FANEMEQKCL TEAKNDPMVA
LTLKRVQGVQ AACRAAIVKA EIAEGAKGPS TAMVLAGALL IAALAYFAYV YSAGGTSLKA
LPLFGVVIIL AIGLFGRNLA LKTV
