CAS2_BETPL
ID CAS2_BETPL Reviewed; 757 AA.
AC Q8W3Z3;
DT 16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 54.
DE RecName: Full=Cycloartenol synthase 2;
DE EC=5.4.99.8;
GN Name=CASBPX2;
OS Betula platyphylla (Asian white birch).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fagales; Betulaceae; Betula.
OX NCBI_TaxID=78630;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=12736505; DOI=10.1248/bpb.26.642;
RA Zhang H., Shibuya M., Yokota S., Ebizuka Y.;
RT "Oxidosqualene cyclases from cell suspension cultures of Betula platyphylla
RT var. japonica: molecular evolution of oxidosqualene cyclases in higher
RT plants.";
RL Biol. Pharm. Bull. 26:642-650(2003).
CC -!- FUNCTION: Oxidosqualene cyclase converting oxidosqualene to
CC cycloartenol. {ECO:0000269|PubMed:12736505}.
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:12736505};
CC -!- SIMILARITY: Belongs to the terpene cyclase/mutase family.
CC {ECO:0000305}.
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DR EMBL; AB055510; BAB83086.1; -; mRNA.
DR GO; GO:0005811; C:lipid droplet; IEA:InterPro.
DR GO; GO:0016871; F:cycloartenol synthase activity; IDA:UniProtKB.
DR GO; GO:0010686; P:tetracyclic triterpenoid biosynthetic process; IDA:UniProtKB.
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; Repeat.
FT CHAIN 1..757
FT /note="Cycloartenol synthase 2"
FT /id="PRO_0000413991"
FT REPEAT 147..188
FT /note="PFTB 1"
FT REPEAT 512..557
FT /note="PFTB 2"
FT REPEAT 589..629
FT /note="PFTB 3"
FT REPEAT 638..679
FT /note="PFTB 4"
FT REPEAT 700..741
FT /note="PFTB 5"
FT ACT_SITE 483
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P48449"
SQ SEQUENCE 757 AA; 86235 MW; 4D7464A55F588168 CRC64;
MWKLKIAEGG SPWLRTLNNH VGRQVWEFDP KLGSPEELAE IERARETSLK VRFEKKHSSD
LLMRIQFAKE NPRGAVLPQV KVNETEDVTE EMVTRMLRRA ISFHSTLQAH DGHWAGDYGG
PMFLMPGLVI TLSITGALNT VLSEEHKKEM CRYLYNHQNK DGGWGLHIEG PSTMFGTVLS
YVTLRLLGEG ANDGQGAIER GRKWILDHGS ATAIISWGKM WLSVLGAFEW SGNNPLPPEI
WLLPYMLPVH PGRMWCHCRM VYLPMSYLYG KRFVGPITPT VMSLRKELYS VPYHEIDWNQ
ARNLCAKEXL YYPHPLVQDI LWASLHKLVE PVLMRWPGKR LREKALRTVL EHIHYEDENT
RYICIGPVNK VLNMLCCWVE DPNSEAFKLH LPRINDYLWI AEDGMKMQGY NGSQLWDTAF
AVQAIISTNL FEEYGPTLEK AHMYIKKSQV REDCPGDLDF WYRHISKGAW PFSTADHGWP
ISDCTAEGLK AALLLSKIPP DVVGEPLVEE RLYDAVNVIL SLQNADGGFA TYELTRSYPW
LELINPAETF GDIVIDYNYV ECTSAAIQAL TSFKKSYPKH REEEVDVCIK RAAMFTEKIQ
ASDGSWYGSW GVCFTYGTWF GVKGLVAAGK NFNDCFGIRK ACDFLLSKQL PSGGWGESYL
SCQNKVYSHV EGNRSHVVNT GWAMLALIEA GQAERDPTPL HRAARVLINS QMENGDFPQE
EIMGVFNRNC MITYAAYRNI FPIWALGEYR CRVLQAP