SQS11_PANGI
ID SQS11_PANGI Reviewed; 415 AA.
AC A0A1P7Y0D4;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2017, sequence version 1.
DT 25-MAY-2022, entry version 14.
DE RecName: Full=Squalene synthase 11 {ECO:0000303|PubMed:25642758};
DE Short=PgSS11 {ECO:0000305};
DE Short=SQS 11 {ECO:0000305};
DE EC=2.5.1.21 {ECO:0000250|UniProtKB:P53799};
DE AltName: Full=FPP:FPP farnesyltransferase SS11 {ECO:0000305};
DE AltName: Full=Farnesyl-diphosphate farnesyltransferase SS11 {ECO:0000305};
GN Name=SS11 {ECO:0000303|PubMed:25642758};
OS Panax ginseng (Korean ginseng).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Apiales; Araliaceae; Panax.
OX NCBI_TaxID=4054;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND INDUCTION BY METHYL JASMONATE.
RC STRAIN=cv. Damaya;
RX PubMed=25642758; DOI=10.3390/ijms16023035;
RA Cao H., Nuruzzaman M., Xiu H., Huang J., Wu K., Chen X., Li J., Wang L.,
RA Jeong J.-H., Park S.-J., Yang F., Luo J., Luo Z.;
RT "Transcriptome analysis of methyl jasmonate-elicited Panax ginseng
RT adventitious roots to discover putative ginsenoside biosynthesis and
RT transport genes.";
RL Int. J. Mol. Sci. 16:3035-3057(2015).
RN [2]
RP REVIEW.
RX PubMed=29378087; DOI=10.1002/bab.1649;
RA Lu J., Li J., Wang S., Yao L., Liang W., Wang J., Gao W.;
RT "Advances in ginsenoside biosynthesis and metabolic regulation.";
RL Biotechnol. Appl. Biochem. 65:514-522(2018).
RN [3]
RP REVIEW.
RX PubMed=29509695; DOI=10.3390/molecules23030589;
RA Yang J.-L., Hu Z.-F., Zhang T.-T., Gu A.-D., Gong T., Zhu P.;
RT "Progress on the studies of the key enzymes of ginsenoside biosynthesis.";
RL Molecules 23:0-0(2018).
CC -!- FUNCTION: Component of the triterpene saponins (e.g. ginsenosides or
CC panaxosides) and phytosterols biosynthetic pathways (PubMed:29378087).
CC Catalyzes the biosynthesis of squalene (By similarity).
CC {ECO:0000250|UniProtKB:O48666, ECO:0000303|PubMed:29378087}.
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:0000250|UniProtKB:P53799};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32300;
CC Evidence={ECO:0000250|UniProtKB:D2K762};
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:0000250|UniProtKB:P53799};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32296;
CC Evidence={ECO:0000250|UniProtKB:D2K762};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P53799};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P53799};
CC -!- PATHWAY: Terpene metabolism; lanosterol biosynthesis; lanosterol from
CC farnesyl diphosphate: step 1/3. {ECO:0000250|UniProtKB:P53799}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P53799}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- INDUCTION: Induced methyl jasmonate (MeJA) in adventitious roots.
CC {ECO:0000269|PubMed:25642758}.
CC -!- SIMILARITY: Belongs to the phytoene/squalene synthase family.
CC {ECO:0000305}.
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DR EMBL; KP689321; AJK30633.1; -; mRNA.
DR AlphaFoldDB; A0A1P7Y0D4; -.
DR SMR; A0A1P7Y0D4; -.
DR UniPathway; UPA00767; UER00751.
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:0051996; F:squalene synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009753; P:response to jasmonic acid; IEP: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 2: Evidence at transcript level;
KW Endoplasmic reticulum; Isoprene biosynthesis; Membrane; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..415
FT /note="Squalene synthase 11"
FT /id="PRO_0000446957"
FT TRANSMEM 281..301
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 392..412
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 415 AA; 46996 MW; 2B524DA1DC5475FA CRC64;
MGSLGAILKH PEDFYPLLKL KIAARHAEKQ IPSEPHWAFC YSMLHKVSRS FGLVIQQLGP
QLRDAVCIFY LVLRALDTVE DDTSISTEVK VPILMAFHRH IYDNDWHFSC GTKEYKVLMD
EFHHVSNAFL DLGSGYKEAI EDITMRMGAG MAKFICKEVE TIDDYDEYCH YVAGLVGLGL
SKLFHASGAE DLATDSLSNS MGLFLQKTNI IRDYLEDINE IPKSRMFWPR QIWSKYVDKL
EDLKYEENSA KAVQCLNDMV TDALVHAEDC LKYMSDLRGP AIFRFCAIPQ IMAIGTLALC
FNNTQVFRGV VKMRRGLTAK VIDQTKTMSD VYGAFFDFSC LLKSKVDNND PNATKTLSRL
EAIQKICKNS GALTTKRKSY IIENESGYNS TLIIILFIIL AILYAYLSSN LPNSL
