BSS_BOTBR
ID BSS_BOTBR Reviewed; 461 AA.
AC Q9SDW9; Q9M678;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Squalene synthase BSS {ECO:0000305};
DE EC=2.5.1.21 {ECO:0000269|PubMed:10620354};
GN Name=BSS {ECO:0000305};
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 [GENOMIC DNA / MRNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=Race B;
RX PubMed=10620354; DOI=10.1006/abbi.1999.1568;
RA Okada S., Devarenne T.P., Chappell J.;
RT "Molecular characterization of squalene synthase from the green microalga
RT Botryococcus braunii, race B.";
RL Arch. Biochem. Biophys. 373:307-317(2000).
CC -!- FUNCTION: Converts farnesyl diphosphate (FPP) into squalene, a
CC precursor for sterol biosynthesis in eukaryotes. Does not possess
CC botryococcene synthase activity. {ECO:0000269|PubMed:10620354}.
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:10620354};
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:10620354};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P37268};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Single-pass membrane protein {ECO:0000255}.
CC -!- DEVELOPMENTAL STAGE: Transient induction with an apparent maximum
CC occurring 6 to 8 days after subculturing.
CC {ECO:0000269|PubMed:10620354}.
CC -!- SIMILARITY: Belongs to the phytoene/squalene synthase family.
CC {ECO:0000305}.
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DR EMBL; AF205791; AAF20201.1; -; mRNA.
DR EMBL; AH009227; AAF63255.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9SDW9; -.
DR SMR; Q9SDW9; -.
DR BioCyc; MetaCyc:MON-14640; -.
DR BRENDA; 2.5.1.21; 915.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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; PS01044; SQUALEN_PHYTOEN_SYN_1; 1.
DR PROSITE; PS01045; SQUALEN_PHYTOEN_SYN_2; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Magnesium; Membrane; Metal-binding; NAD; NADP;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..461
FT /note="Squalene synthase BSS"
FT /id="PRO_0000421364"
FT TRANSMEM 430..450
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 51
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P37268"
FT BINDING 76
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
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 82
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P37268"
FT BINDING 83
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P37268"
FT BINDING 219
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P37268"
FT BINDING 322
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P37268"
FT BINDING 324
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P37268"
SQ SEQUENCE 461 AA; 52547 MW; 9C23A7641B22213D CRC64;
MGMLRWGVES LQNPDELIPV LRMIYADKFG KIKPKDEDRG FCYEILNLVS RSFAIVIQQL
PAQLRDPVCI FYLVLRALDT VEDDMKIAAT TKIPLLRDFY EKISDRSFRM TAGDQKDYIR
LLDQYPKVTS VFLKLTPREQ EIIADITKRM GNGMADFVHK GVPDTVGDYD LYCHYVAGVV
GLGLSQLFVA SGLQSPSLTR SEDLSNHMGL FLQKTNIIRD YFEDINELPA PRMFWPREIW
GKYANNLAEF KDPANKAAAM CCLNEMVTDA LRHAVYCLQY MSMIEDPQIF NFCAIPQTMA
FGTLSLCYNN YTIFTGPKAA VKLRRGTTAK LMYTSNNMFA MYRHFLNFAE KLEVRCNTET
SEDPSVTTTL EHLHKIKAAC KAGLARTKDD TFDELRSRLL ALTGGSFYLA WTYNFLDLRG
PGDLPTFLSV TQHWWSILIF LISIAVFFIP SRPSPRPTLS A
