ID   CAS1_PANGI              Reviewed;         758 AA.
AC   O82139;
DT   16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Cycloartenol Synthase {ECO:0000303|PubMed:9746369};
DE            Short=PgCAS {ECO:0000305};
DE            EC=5.4.99.8 {ECO:0000269|PubMed:9746369};
DE   AltName: Full=Phytosterol synthase {ECO:0000303|PubMed:24198659};
GN   Name=OSCPNX1 {ECO:0000303|PubMed:9746369};
GN   Synonyms=CAS {ECO:0000305}, PNX {ECO:0000303|PubMed:24198659};
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 [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC   TISSUE=Root;
RX   PubMed=9746369; DOI=10.1046/j.1432-1327.1998.2560238.x;
RA   Kushiro T., Shibuya M., Ebizuka Y.;
RT   "Beta-amyrin synthase--cloning of oxidosqualene cyclase that catalyzes the
RT   formation of the most popular triterpene among higher plants.";
RL   Eur. J. Biochem. 256:238-244(1998).
RN   [2]
RP   GENE FAMILY.
RX   PubMed=24198659; DOI=10.5142/jgr.2013.37.332;
RA   Kim D.S., Song M., Kim S.-H., Jang D.-S., Kim J.-B., Ha B.-K., Kim S.H.,
RA   Lee K.J., Kang S.-Y., Jeong I.Y.;
RT   "The improvement of ginsenoside accumulation in Panax ginseng as a result
RT   of gamma-irradiation.";
RL   J. Ginseng Res. 37:332-340(2013).
CC   -!- FUNCTION: Component of the phytosterols biosynthetic pathways
CC       (Probable). Oxidosqualene cyclase converting oxidosqualene to
CC       cycloartenol (PubMed:9746369). {ECO:0000269|PubMed:9746369,
CC       ECO:0000305}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-2,3-epoxysqualene = cycloartenol; Xref=Rhea:RHEA:21308,
CC         ChEBI:CHEBI:15441, ChEBI:CHEBI:17030; EC=5.4.99.8;
CC         Evidence={ECO:0000269|PubMed:9746369};
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC       {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the terpene cyclase/mutase family.
CC       {ECO:0000305}.
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DR   EMBL; AB009029; BAA33460.1; -; mRNA.
DR   AlphaFoldDB; O82139; -.
DR   SMR; O82139; -.
DR   PRIDE; O82139; -.
DR   BioCyc; MetaCyc:MON-13453; -.
DR   BRENDA; 5.4.99.8; 7895.
DR   UniPathway; UPA00213; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005811; C:lipid droplet; IEA:InterPro.
DR   GO; GO:0016871; F:cycloartenol synthase activity; IDA:UniProtKB.
DR   GO; GO:0019745; P:pentacyclic triterpenoid biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0016126; P:sterol biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd02892; SQCY_1; 1.
DR   InterPro; IPR032696; SQ_cyclase_C.
DR   InterPro; IPR032697; SQ_cyclase_N.
DR   InterPro; IPR018333; Squalene_cyclase.
DR   InterPro; IPR002365; Terpene_synthase_CS.
DR   InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR   PANTHER; PTHR11764; PTHR11764; 1.
DR   Pfam; PF13243; SQHop_cyclase_C; 1.
DR   Pfam; PF13249; SQHop_cyclase_N; 1.
DR   SFLD; SFLDG01016; Prenyltransferase_Like_2; 1.
DR   SUPFAM; SSF48239; SSF48239; 2.
DR   TIGRFAMs; TIGR01787; squalene_cyclas; 1.
DR   PROSITE; PS01074; TERPENE_SYNTHASES; 1.
PE   1: Evidence at protein level;
KW   Isomerase; Lipid biosynthesis; Lipid metabolism; Membrane; Repeat;
KW   Steroid biosynthesis; Steroid metabolism; Sterol biosynthesis;
KW   Sterol metabolism; Transmembrane; Transmembrane helix.
FT   CHAIN           1..758
FT                   /note="Cycloartenol Synthase"
FT                   /id="PRO_0000413964"
FT   TRANSMEM        122..142
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REPEAT          147..188
FT                   /note="PFTB 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          512..557
FT                   /note="PFTB 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          589..629
FT                   /note="PFTB 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          638..679
FT                   /note="PFTB 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          700..747
FT                   /note="PFTB 5"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        483
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P48449"
SQ   SEQUENCE   758 AA;  86109 MW;  C690792053C786E6 CRC64;
     MWKLKIAEGG NPWLRTLNDH VGRQIWEFDP NIGSPEELAE VEKVRENFRN HRFEKKHSAD
     LLMRIQFANE NPGSVVLPQV KVNDGEDISE DKVTVTLKRA MSFYSTLQAH DGHWPGDYGG
     PMFLMPGLVI TLSITGVLNV VLSKEHKREI CRYLYNHQNR DGGWGLHIEG PSTMFGTVLN
     YVTLRLLGEG ANDGQGAMEK GRQWILDHGS ATAITSWGKM WLSVLGVFEW SGNNPLPPET
     WLLPYILPIH PGRMWCHRRM VYLPMSYLYG KRFVGPITPT VLSLRKEVFS VPYHEIDWNQ
     ARNLCAKEDL YYPHPLIQDI LWASLDKVWE PIFMHWPAKK LREKSLRTVM EHIHYEDENT
     RYICIGPVNK VLNMLCCWVE DPNSEAFKLH LPRLHDFLWL AEDGMKMQGY NGSQLWDTAF
     AVQAIISTNL AEEYGPTLRK AHTFMKNSQV LDDCPGDLDA WYRHVSKGAW PFSTADHGWP
     ISDCTAEGFK AVLQLSKLPS ELVGEPLDAK RLYDAVNVIL SLQNSDGGYA TYELTRSYSW
     LELVNPAETF GDIVIDYPYV ECTSAAIQAL TAFKKLFPGH RREEIQHSIE KAALFIEKIQ
     SSDGSWYGSW GVCFTYGTWF GIKGLVTAGR TFSSCASIRK ACDFLLSKQV ASGGWGESYL
     SCQNKVYTNL EGNRSHVVNT GWAMLALIDA GQAERDATPL HRAAKLLINS QMENGDFPQE
     EIMGVFDKNC MITYAAYRNI FPIWALGEYR CRVLQGPS