BOCS_BOTBR
ID BOCS_BOTBR Reviewed; 383 AA.
AC G0Y288;
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=Botryococcene synthase {ECO:0000303|PubMed:21746901};
DE EC=1.3.1.97 {ECO:0000269|PubMed:21746901};
DE AltName: Full=Squalene synthase-like 3 {ECO:0000303|PubMed:21746901};
GN Name=SSL-3 {ECO:0000303|PubMed:21746901};
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 botryococcene when coexpressed with SSL-1. No
CC activity with farnesyl diphosphate (FPP) as substrate.
CC {ECO:0000269|PubMed:21746901}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=C30 botryococcene + diphosphate + NADP(+) = H(+) + NADPH +
CC presqualene diphosphate; Xref=Rhea:RHEA:34571, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57310, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:70786; EC=1.3.1.97;
CC Evidence={ECO:0000269|PubMed:21746901};
CC -!- SIMILARITY: Belongs to the phytoene/squalene synthase family.
CC {ECO:0000305}.
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DR EMBL; HQ585060; AEL16717.1; -; mRNA.
DR AlphaFoldDB; G0Y288; -.
DR SMR; G0Y288; -.
DR KEGG; ag:AEL16717; -.
DR BioCyc; MetaCyc:MON-17326; -.
DR BRENDA; 1.3.1.97; 915.
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 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 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; Metal-binding; NADP; Oxidoreductase.
FT CHAIN 1..383
FT /note="Botryococcene synthase"
FT /id="PRO_0000421363"
FT BINDING 47
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P37268"
FT BINDING 72
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P37268"
FT BINDING 75
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 213
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P37268"
FT BINDING 312
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"
SQ SEQUENCE 383 AA; 44156 MW; F22D548DF591B0F1 CRC64;
MKLREVLQHP GEIIPLLQMM VMAYRRKRKP QDPNLAWCWE TLIKVSRSYV LVIQQLPEVL
QDPICVNYLV LRGLDTLQDD MAIPAEKRVP LLLDYYNHIG DITWKPPCGY GQYVELIEEY
PRVTKEFLKL NKQDQQFITD MCMRLGAEMT VFLKRDVLTV PDLDLYAFTN NGPVAICLTK
LWVDRKFADP KLLDREDLSG HMAMFLGKIN VIRDIKEDVL EDPPRIWWPK EIWGKYLKDL
RDIIKPEYQK EALACLNDIL TDALRHIEPC LQYMEMVWDE GVFKFCAVPE LMSLATISVC
YNNPKVFTGV VKMRRGETAK LFLSVTNMPA LYKSFSAIAE EMEAKCVRED PNFALTVKRL
QDVQALCKAG LAKSNGKVSA KGA
