ID   BASM1_KALSE             Reviewed;         763 AA.
AC   A0A0S2IHL6;
DT   07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT   17-FEB-2016, sequence version 1.
DT   25-MAY-2022, entry version 19.
DE   RecName: Full=Beta-amyrin synthase 1 {ECO:0000303|PubMed:29186583};
DE            Short=KsBAS1 {ECO:0000303|PubMed:29186583};
DE            EC=5.4.99.39 {ECO:0000269|PubMed:29186583};
GN   Name=BAS1 {ECO:0000303|PubMed:29186583};
GN   Synonyms=BAS {ECO:0000303|PubMed:29186583};
OS   Kalopanax septemlobus (Castor aralia) (Acanthopanax septemlobus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Apiales; Araliaceae; Kalopanax.
OX   NCBI_TaxID=228393;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=29186583; DOI=10.1093/pcp/pcx188;
RA   Han J.Y., Chun J.H., Oh S.A., Park S.B., Hwang H.S., Lee H., Choi Y.E.;
RT   "Transcriptomic analysis of Kalopanax septemlobus and characterization of
RT   KsBAS, CYP716A94 and CYP72A397 genes involved in hederagenin saponin
RT   biosynthesis.";
RL   Plant Cell Physiol. 59:319-330(2018).
CC   -!- FUNCTION: Component of the oleanane-type triterpene saponins
CC       biosynthetic pathway (PubMed:29186583). Oxidosqualene cyclase
CC       converting oxidosqualene into beta-amyrin, generating five rings and
CC       eight asymmetric centers in a single transformation (PubMed:29186583).
CC       {ECO:0000269|PubMed:29186583}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-2,3-epoxysqualene = beta-amyrin; Xref=Rhea:RHEA:31007,
CC         ChEBI:CHEBI:10352, ChEBI:CHEBI:15441; EC=5.4.99.39;
CC         Evidence={ECO:0000269|PubMed:29186583};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31008;
CC         Evidence={ECO:0000269|PubMed:29186583};
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the terpene cyclase/mutase family.
CC       {ECO:0000305}.
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DR   EMBL; KT150523; ALO23119.1; -; mRNA.
DR   AlphaFoldDB; A0A0S2IHL6; -.
DR   SMR; A0A0S2IHL6; -.
DR   UniPathway; UPA00213; -.
DR   GO; GO:0005811; C:lipid droplet; IEA:InterPro.
DR   GO; GO:0042300; F:beta-amyrin synthase activity; IDA:UniProtKB.
DR   GO; GO:0016104; P: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; Isoprene biosynthesis; Repeat.
FT   CHAIN           1..763
FT                   /note="Beta-amyrin synthase 1"
FT                   /id="PRO_0000452138"
FT   REPEAT          100..142
FT                   /note="PFTB 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          150..191
FT                   /note="PFTB 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          441..485
FT                   /note="PFTB 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          515..560
FT                   /note="PFTB 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          592..632
FT                   /note="PFTB 5"
FT                   /evidence="ECO:0000255"
FT   REPEAT          641..682
FT                   /note="PFTB 6"
FT                   /evidence="ECO:0000255"
FT   REPEAT          703..744
FT                   /note="PFTB 7"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        486
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P48449"
FT   SITE            419
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:P48449"
FT   SITE            475
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:P48449"
FT   SITE            613
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:P48449"
SQ   SEQUENCE   763 AA;  87385 MW;  BA333A8D580C0ECE CRC64;
     MWKLKIAEGD KNDPYLYSTN NFVGRQTWEF DPDYVGSPGE LEEVEEARRQ FGENRYKVKP
     CGDLLWRLQF LREKNFKQTI PQVKVGDDEA VTYEAATTTL RRAVHFFSAL QASDGHWPAE
     IAGPLYFLPP LVMCLYITGH LDTVFPAEHR KEILRYIYCH QNEDGGWGFH IEGHSTMFCT
     TLSYICMRIL GEGPDGGVNN ACARGRKWIL DHGSATAVPS WGKTWLSILG VYEWMGSNPM
     PPEFWILPSF LPMHPAKMWC YCRMVYMPMS YLYGKRFVGP ITPLILQLRE ELYAQPYNEI
     KWGKVRHVCA KEDIYYPHPL IQDLLWDSLY VLTEPLLTRW PFNKLREKAL QTTMKHVHYE
     DENSRYITIG CVEKVLCMLA CWVEDPNGDY FKKHLARIPD YIWVGEDGMK MQSFGSQEWD
     TGFGIQALLA SDLTHELGPT LMKGHDFIKK SQVKDNPSGD FKSMYRHISK GSWTFSDQDH
     GWQVSDCTAE GLKCCLIFST MPEEIVGKKM EPELLYNSVN ILLSLQSKNG GLAAWEPVTA
     QDWLELLNPT EFFADIVIEH EYVECTASAI QALVLFKKLY PGHRKKEIDN FITNAIRFLE
     DVQMPDGSWY GNWGVCFTYG SWFALGGLAA AGKTYDNCAA VRKAVNFLLE SQLDDGGWGE
     SYLSCPKKVY VPLEGNRSNL VHTGWALMGL IHSGQAERDP TPLHRAAKLL INSQMEDGDF
     PQQEITGVFM KNCMLHYATY RNIYPLWALA EYRRRVPLPS LGA