SLSS_SOLLC
ID SLSS_SOLLC Reviewed; 411 AA.
AC D0VFU8;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2009, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Squalene synthase {ECO:0000303|PubMed:27050299};
DE Short=SlSS {ECO:0000303|PubMed:27050299};
DE EC=2.5.1.21 {ECO:0000269|PubMed:27050299};
GN Name=SS {ECO:0000305};
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
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}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the phytoene/squalene synthase family.
CC {ECO:0000305}.
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DR EMBL; GU075687; ACY25092.1; -; mRNA.
DR AlphaFoldDB; D0VFU8; -.
DR SMR; D0VFU8; -.
DR STRING; 4081.Solyc01g110290.2.1; -.
DR Proteomes; UP000004994; Unplaced.
DR ExpressionAtlas; D0VFU8; baseline and differential.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004310; F:farnesyl-diphosphate farnesyltransferase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051996; F:squalene synthase activity; IDA:UniProtKB.
DR GO; GO:0045338; P:farnesyl diphosphate metabolic process; IBA:GO_Central.
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 Magnesium; Membrane; Metal-binding; NAD; NADP; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..411
FT /note="Squalene synthase"
FT /id="PRO_0000446506"
FT TRANSMEM 388..408
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 49
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P37268"
FT BINDING 74
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P37268"
FT BINDING 77
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 81
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P37268"
FT BINDING 212
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 411 AA; 47062 MW; 075F16117F710D13 CRC64;
MGTLRAILKN PDDLYPLIKL KLAARHAEKQ IPPEPHWGFC YLMLQKVSRS FALVIQQLPV
ELRDAVCIFY LVLRALDTVE DDTSIPTDVK VPILISFHQH VYDREWHFAC GTKEYKVLMD
QFHHVSTAFL ELGKLYQQAI EDITMRMGAG MAKFICKEVE TTDDYDEYCH YVAGLVGLGL
SKLFHASGKE DLASDSLSNS MGLFLQKTNI IRDYLEDINE VPKCRMFWPR EIWSKYVNKL
EDLKYEENSV KAVQCLNDMV TNALSHVEDC LTYMFNLHDP AIFRFCAIPQ VMAIGTLAMC
YDNIEVFRGV VKMRRGLTAK VIDRTKTMAD VYGAFFDFSC MLKSKVNNND PNATKTLKRL
DAILKTCRDS GTLNKRKSYI IRNEPNYSPV LIVVIFIILA IILAQLFGSR S
