ID   BAS_BRUGY               Reviewed;         759 AA.
AC   A8CDT2;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   03-AUG-2022, entry version 47.
DE   RecName: Full=Beta-amyrin synthase;
DE            Short=BgbAS;
DE            EC=5.4.99.39;
GN   Name=BAS;
OS   Bruguiera gymnorhiza (Burma mangrove) (Rhizophora gymnorhiza).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Rhizophoraceae; Bruguiera.
OX   NCBI_TaxID=39984;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC   TISSUE=Leaf;
RX   PubMed=17803686; DOI=10.1111/j.1742-4658.2007.06025.x;
RA   Basyuni M., Oku H., Tsujimoto E., Kinjo K., Baba S., Takara K.;
RT   "Triterpene synthases from the Okinawan mangrove tribe, Rhizophoraceae.";
RL   FEBS J. 274:5028-5042(2007).
CC   -!- FUNCTION: Oxidosqualene cyclase involved in the biosynthesis of beta-
CC       amyrin. {ECO:0000269|PubMed:17803686}.
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:17803686};
CC   -!- SIMILARITY: Belongs to the terpene cyclase/mutase family.
CC       {ECO:0000305}.
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DR   EMBL; AB289585; BAF80443.1; -; mRNA.
DR   AlphaFoldDB; A8CDT2; -.
DR   SMR; A8CDT2; -.
DR   KEGG; ag:BAF80443; -.
DR   BioCyc; MetaCyc:MON-14451; -.
DR   BRENDA; 5.4.99.39; 1002.
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; 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.
PE   1: Evidence at protein level;
KW   Isomerase; Repeat.
FT   CHAIN           1..759
FT                   /note="Beta-amyrin synthase"
FT                   /id="PRO_0000412989"
FT   REPEAT          148..189
FT                   /note="PFTB 1"
FT   REPEAT          514..559
FT                   /note="PFTB 2"
FT   REPEAT          591..631
FT                   /note="PFTB 3"
FT   REPEAT          640..681
FT                   /note="PFTB 4"
FT   ACT_SITE        485
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P48449"
SQ   SEQUENCE   759 AA;  87665 MW;  9335B3C84943318B CRC64;
     MWRIKIAEGG KDPYLYSTNN YVGRQTWEFD PDAGTPEERA EVEEARQNFY KNRYQVKPCG
     DLLWRLQFLG EKNFEQTIPQ VRIEEGEGIT YEKATRALRR TVQFFSALQA SDGHWPAEIA
     GPLFFLPPLV MCVYITGHLD AVFPAEHRKE ILRYIYYHQN EDGGWGLHIE GHSTMFCTAL
     NYICMRIIGE GPNGGQDDAC ARARKWIHDH GSVTNIPSWG KTWLSILGVY DWSGSNPMPP
     EFWMLPSFLP MHPAKMWCYC RMVYMPMSYL YGKRFVGPIT PLIQQLREEL FTQPYDQINW
     KKTRHQCAPE DLYYPHPFVQ DLIWDCLYIF TEPLLTRWPL NEIIRKKALE VTMKHIHYED
     ESSRYITIGC VEKVLCMLAC WVEDPNGDYF KKHLARIPDY IWVAEDGMKM QSFGSQEWDT
     GFAIQALLAT NLTDEIGDVL RRGHDFIKKS QVRDNPSGDF KSMYRHISKG SWTFSDQDHG
     WQVSDCTAEG LKCCLLFSMM PPEIVGEHMV PERLYDSVNV LLSLQSKNGG LSAWEPAGAQ
     EWLELLNPTE FFADIVIEHE YVECTSSAIH ALVLFKKLYP GHRKKEIDNF IVNAVRYLES
     IQTSDGGWYG NWGVCFTYGT WFALGGLAAA GKTYNNCLAM RKAVDFLLRI QRDNGGWGES
     YLSCPEKRYV PLEGNRSNLV HTAWALMALI HAGQMDRDPT PLHRAARLMI NSQLEDGDFP
     QQEITGVFMK NCMLHYAAYR NIYPLWALAE YRRRVPLPS