ID   LSS_BOTBR               Reviewed;         462 AA.
AC   A0A144YEA5;
DT   10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT   08-JUN-2016, sequence version 1.
DT   03-AUG-2022, entry version 18.
DE   RecName: Full=Squalene synthase LSS {ECO:0000303|PubMed:27050299};
DE            EC=2.5.1.21 {ECO:0000269|PubMed:27050299};
GN   Name=LSS {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, AND CATALYTIC ACTIVITY.
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).
CC   -!- FUNCTION: Converts farnesyl diphosphate (FPP) into squalene, a
CC       precursor for sterol biosynthesis in eukaryotes.
CC       {ECO:0000269|PubMed:27050299}.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P37268};
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; KT388100; AMV49168.1; -; mRNA.
DR   AlphaFoldDB; A0A144YEA5; -.
DR   SMR; A0A144YEA5; -.
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..462
FT                   /note="Squalene synthase LSS"
FT                   /id="PRO_0000446505"
FT   TRANSMEM        399..419
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        436..456
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         214
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P37268"
FT   BINDING         314
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P37268"
FT   BINDING         316
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P37268"
SQ   SEQUENCE   462 AA;  51965 MW;  EE2180875262689F CRC64;
     MGKLQEVLKH PDELVPLMQM LVSDYYTKIV PRDPGLGFCY RMLNKVSRSF AIVIQQLPEL
     LRDPICVFYL VLRALDTVED DMALPNDIKL PLLRAFHKKI YDRKWSMKCG YGPYVQLMEE
     YPMVTGVFLK LDPGPREVIT EICRKMGAGM AEFIPKEVLT VKDYDQYCHY AAGLVGEGLS
     KLAVGSGLEN PVLLQKEDLS NHMGLFLQKT NIVRDYLEDI NEEPAPRMFW PKEIWGKYTK
     DLADFKDPAN EKGAVQCLNH MVTDALRHGE HALKYMALLR DPQYFNFCAI PQVMAFGTLS
     LCYNNPQVFK GVVKLRKGES AKLMTTVKSM PALYRTFLRM ADDMVARCKG EARQDPNVAT
     TLKRLQAIQA VCKTGLRSSI KSRKKQAATP LSDDFISKLV LVLGLGYCVY AFNLLPLLWK
     SALIPGPPPP ALTSSLGLPH QIIAVFCVLT AGYQVFLRGG LA