ID   BOSS_BOTBR              Reviewed;         465 AA.
AC   G0Y287;
DT   06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2011, sequence version 1.
DT   03-AUG-2022, entry version 29.
DE   RecName: Full=Botryococcus squalene synthase;
DE            EC=1.3.1.96;
DE   AltName: Full=Squalene synthase-like 2;
GN   Name=SSL-2;
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 B;
RX   PubMed=21746901; DOI=10.1073/pnas.1106222108;
RA   Niehaus T.D., Okada S., Devarenne T.P., Watt D.S., Sviripa V., Chappell J.;
RT   "Identification of unique mechanisms for triterpene biosynthesis in
RT   Botryococcus braunii.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:12260-12265(2011).
CC   -!- FUNCTION: Produces squalene when coexpressed with SSL-1 and bisfarnesyl
CC       ether and a very small amount of squalene when incubated alone in the
CC       presence of NADPH. {ECO:0000269|PubMed:21746901}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + NADPH + presqualene diphosphate = diphosphate + NADP(+)
CC         + squalene; Xref=Rhea:RHEA:22232, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15440, ChEBI:CHEBI:33019, ChEBI:CHEBI:57310,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.3.1.96;
CC         Evidence={ECO:0000269|PubMed:21746901};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the phytoene/squalene synthase family.
CC       {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; HQ585059; AEL16716.1; -; mRNA.
DR   AlphaFoldDB; G0Y287; -.
DR   SMR; G0Y287; -.
DR   KEGG; ag:AEL16716; -.
DR   BioCyc; MetaCyc:MON-17312; -.
DR   BRENDA; 1.3.1.96; 915.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004310; F:farnesyl-diphosphate farnesyltransferase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008610; P:lipid biosynthetic process; IEA:InterPro.
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; 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.
PE   1: Evidence at protein level;
KW   Magnesium; Membrane; Metal-binding; NADP; Oxidoreductase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..465
FT                   /note="Botryococcus squalene synthase"
FT                   /id="PRO_0000421362"
FT   TRANSMEM        395..415
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        429..449
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"
SQ   SEQUENCE   465 AA;  52149 MW;  51991D7B4F11483D CRC64;
     MVKLVEVLQH PDEIVPILQM LHKTYRAKRS YKDPGLAFCY GMLQRVSRSF SVVIQQLPDE
     LRHPICVFYL ILRALDTVED DMNLPNEVKI PLLRTFHEHL FDRSWKLKCG YGPYVDLMEN
     YPLVTDVFLT LSPGAQEVIR DSTRRMGNGM ADFIGKDEVH SVAEYDLYCH YVAGLVGSAV
     AKIFVDSGLE KENLVAEVDL ANNMGQFLQK TNVIRDYLED INEEPAPRMF WPREIWGKYA
     QELADFKDPA NEKAAVQCLN HMVTDALRHC EIGLNVIPLL QNIGILRSCL IPEVMGLRTL
     TLCYNNPQVF RGVVKMRRGE TAKLFMSIYD KRSFYQTYLR LANELEAKCK GEASGDPMVA
     TTLKHVHGIQ KSCKAALSSK ELLAKSGSAL TDDPAIRLLL LVGVVAYFAY AFNLGDVRGE
     HGVRALGSIL DLSQKGLAVA SVALLLLVLL ARSRLPLLTS ASSKQ