ID   BAMS_SOLLC              Reviewed;         761 AA.
AC   E7DN63;
DT   16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-MAR-2011, sequence version 1.
DT   24-JAN-2024, entry version 54.
DE   RecName: Full=Beta-amyrin synthase;
DE            EC=5.4.99.39;
DE   AltName: Full=Triterpenoid synthase 1;
DE            Short=SlTTS1;
GN   Name=TTS1;
OS   Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC   Solanum subgen. Lycopersicon.
OX   NCBI_TaxID=4081;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP   SPECIFICITY.
RC   STRAIN=cv. MicroTom;
RX   PubMed=21059824; DOI=10.1104/pp.110.162883;
RA   Wang Z., Guhling O., Yao R., Li F., Yeats T., Rose J., Jetter R.;
RT   "Two oxidosqualene cyclases responsible for biosynthesis of tomato fruit
RT   cuticular triterpenoids.";
RL   Plant Physiol. 155:540-552(2011).
CC   -!- FUNCTION: Oxidosqualene cyclase converting oxidosqualene into beta-
CC       amyrin, generating five rings and eight asymmetric centers in a single
CC       transformation. {ECO:0000269|PubMed:21059824}.
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:21059824};
CC   -!- TISSUE SPECIFICITY: Expressed in the leaves and in the epidermal cells
CC       but not in the inner tissues of the fruit.
CC       {ECO:0000269|PubMed:21059824}.
CC   -!- SIMILARITY: Belongs to the terpene cyclase/mutase family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; HQ266579; ADU52574.1; -; mRNA.
DR   RefSeq; NP_001234604.1; NM_001247675.1.
DR   AlphaFoldDB; E7DN63; -.
DR   SMR; E7DN63; -.
DR   STRING; 4081.E7DN63; -.
DR   PaxDb; 4081-Solyc12g006530-1-1; -.
DR   GeneID; 100529102; -.
DR   KEGG; sly:100529102; -.
DR   eggNOG; KOG0497; Eukaryota.
DR   InParanoid; E7DN63; -.
DR   OrthoDB; 608at2759; -.
DR   BioCyc; MetaCyc:MONOMER-17974; -.
DR   BRENDA; 5.4.99.39; 3101.
DR   Proteomes; UP000004994; Unplaced.
DR   ExpressionAtlas; E7DN63; baseline and differential.
DR   GO; GO:0005811; C:lipid droplet; IEA:InterPro.
DR   GO; GO:0042300; F:beta-amyrin synthase activity; IBA:GO_Central.
DR   GO; GO:0016104; P:triterpenoid biosynthetic process; IBA:GO_Central.
DR   CDD; cd02892; SQCY_1; 1.
DR   Gene3D; 1.50.10.20; -; 2.
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   NCBIfam; TIGR01787; squalene_cyclas; 1.
DR   PANTHER; PTHR11764:SF58; BETA-AMYRIN SYNTHASE-RELATED; 1.
DR   PANTHER; PTHR11764; TERPENE CYCLASE/MUTASE FAMILY MEMBER; 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; Terpenoid cyclases/Protein prenyltransferases; 2.
DR   PROSITE; PS01074; TERPENE_SYNTHASES; 1.
PE   1: Evidence at protein level;
KW   Isomerase; Reference proteome; Repeat.
FT   CHAIN           1..761
FT                   /note="Beta-amyrin synthase"
FT                   /id="PRO_0000413967"
FT   REPEAT          148..189
FT                   /note="PFTB 1"
FT   REPEAT          513..558
FT                   /note="PFTB 2"
FT   REPEAT          590..630
FT                   /note="PFTB 3"
FT   REPEAT          639..680
FT                   /note="PFTB 4"
FT   REPEAT          701..742
FT                   /note="PFTB 5"
FT   ACT_SITE        484
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P48449"
SQ   SEQUENCE   761 AA;  87248 MW;  313628BF40BA5428 CRC64;
     MWKLKIAEGQ NGPYLYSTNN YVGRQTWEFD PNGGTIEERA KIEEARQQFW NNRYKVKPSS
     DLLWRIQFLG EKNFKQKIPA VKVEEGEEIS HEVATIALHR AVNFFSALQA TDGHWPAENA
     GPLFFLPPLV MCMYITGHLN TVFPAEHRKE ILRYIYCHQN EDGGWGLHIE GHSTMFCTAL
     SYICMRILGE GPDGGVNNAC ARARKWILDH GSVTAIPSWG KTWLSILGVF EWIGTNPMPP
     EFWILPSFLP VHPAKMWCYC RMVYMPMSYL YGKRFVGPIT PLILQLREEL YDRPYDEINW
     KKVRHVCAKE DLYYPHPLVQ DLMWDSLYIC TEPLLTRWPF NKLRNKALEV TMKHIHYEDE
     NSRYITIGCV EKVLCMLACW VEDPNGDYFK KHLARIPDYL WVAEDGMKMQ SFGSQEWDTG
     FAIQALLASE MNDEIADTLR KGHDFIKQSQ VTNNPSGDFK GMYRHISKGS WTFSDQDHGW
     QVSDCTAEAL KCCLLLSTMP RELVGQAMEP GRLYDSVNVV LSLQSKNGGL AAWEPAGASE
     YLELLNPTEF FADIVIEHEY VECTASSIQA LVLFKKLYPG HRTKEINIFI DNAVKYLEDV
     QMPDGSWYGN WGVCFTYGSW FALGGLVAAG KSYNNSAAVR KGVEFLLRTQ RSDGGWGESY
     RSCPDKVYRE LETNDSNLVQ TAWALMGLIH SGQADRDPKP LHRAAKLLIN SQMEDGDFPQ
     QEITGVFMKN CMLHYAAYRN IYPLWGLAEY RKNVLLPLEN N
//