CUCS_CUCPE
ID CUCS_CUCPE Reviewed; 764 AA.
AC Q6BE24;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Cucurbitadienol synthase;
DE EC=5.4.99.33;
GN Name=CPQ;
OS Cucurbita pepo (Vegetable marrow) (Summer squash).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Cucurbiteae; Cucurbita.
OX NCBI_TaxID=3663;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS
RP OF 488-LEU-ILE-489.
RX DOI=10.1016/j.tet.2004.04.088;
RA Shibuya M., Adachi S., Ebizuka Y.;
RT "Cucurbitadienol synthase, the first committed enzyme for cucurbitacin
RT biosynthesis, is a distinct enzyme from cycloartenol synthase for
RT phytosterol biosynthesis.";
RL Tetrahedron 60:6995-7003(2004).
CC -!- FUNCTION: Oxidosqualene cyclase involved in the biosynthesis of the
CC highly oxygenated tetracyclic triterpenes cucurbitacins. Converts
CC oxidosqualene to cucurbitadienol and does not produce lanosterol.
CC {ECO:0000269|Ref.1}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-2,3-epoxysqualene = cucurbitadienol; Xref=Rhea:RHEA:30999,
CC ChEBI:CHEBI:15441, ChEBI:CHEBI:62456; EC=5.4.99.33;
CC Evidence={ECO:0000269|Ref.1};
CC -!- SIMILARITY: Belongs to the terpene cyclase/mutase family.
CC {ECO:0000305}.
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DR EMBL; AB116238; BAD34645.1; -; mRNA.
DR AlphaFoldDB; Q6BE24; -.
DR SMR; Q6BE24; -.
DR KEGG; ag:BAD34645; -.
DR BioCyc; MetaCyc:MON-16525; -.
DR BRENDA; 5.4.99.33; 1740.
DR GO; GO:0005811; C:lipid droplet; IEA:InterPro.
DR GO; GO:0034076; F:cucurbitadienol synthase activity; IDA:UniProtKB.
DR GO; GO:0016104; P:triterpenoid biosynthetic process; IEA:InterPro.
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 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..764
FT /note="Cucurbitadienol synthase"
FT /id="PRO_0000412984"
FT REPEAT 104..146
FT /note="PFTB 1"
FT REPEAT 154..195
FT /note="PFTB 2"
FT REPEAT 520..565
FT /note="PFTB 3"
FT REPEAT 597..637
FT /note="PFTB 4"
FT REPEAT 646..687
FT /note="PFTB 5"
FT ACT_SITE 491
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P48449"
FT MUTAGEN 488
FT /note="L->P: No change of product-specificity. No change of
FT product-specificity; when associated with V-489."
FT MUTAGEN 489
FT /note="I->V: No change of product-specificity. No change of
FT product-specificity; when associated with P-488."
SQ SEQUENCE 764 AA; 86517 MW; 27C59E3B5A6BEC05 CRC64;
MWRLKVGAES VGEEDEKWVK SVSNHLGRQV WEFCADAAAD TPHQLLQIQN ARNHFHHNRF
HRKQSSDLFL AIQYEKEIAK GAKGGAVKVK EGEEVGKEAV KSTLERALGF YSAVQTRDGN
WASDLGGPLF LLPGLVIALH VTGVLNSVLS KHHRVEMCRY LYNHQNEDGG WGLHIEGTST
MFGSALNYVA LRLLGEDADG GDGGAMTKAR AWILERGGAT AITSWGKLWL SVLGVYEWSG
NNPLPPEFWL LPYSLPFHPG RMWCHCRMVY LPMSYLYGKR FVGPITPKVL SLRQELYTIP
YHEIDWNKSR NTCAKEDLYY PHPKMQDILW GSIYHVYEPL FTRWPGKRLR EKALQAAMKH
IHYEDENSRY ICLGPVNKVL NMLCCWVEDP YSDAFKLHLQ RVHDYLWVAE DGMRMQGYNG
SQLWDTAFSI QAIVATKLVD SYAPTLRKAH DFVKDSQIQE DCPGDPNVWF RHIHKGAWPL
STRDHGWLIS DCTAEGLKAS LMLSKLPSTM VGEPLEKNRL CDAVNVLLSL QNDNGGFASY
ELTRSYPWLE LINPAETFGD IVIDYPYVEC TAATMEALTL FKKLHPGHRT KEIDTAIGKA
ANFLEKMQRA DGSWYGCWGV CFTYAGWFGI KGLVAAGRTY NSCLAIRKAC EFLLSKELPG
GGWGESYLSC QNKVYTNLEG NKPHLVNTAW VLMALIEAGQ GERDPAPLHR AARLLMNSQL
ENGDFVQQEI MGVFNKNCMI TYAAYRNIFP IWALGEYCHR VLTE