ID   DAMS_SOLLC              Reviewed;         763 AA.
AC   E7DN64;
DT   16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-MAR-2011, sequence version 1.
DT   03-AUG-2022, entry version 48.
DE   RecName: Full=Delta-amyrin synthase;
DE            EC=5.4.99.55;
DE   AltName: Full=Alpha-amyrin synthase;
DE            EC=5.4.99.40;
DE   AltName: Full=Beta-amyrin synthase;
DE            EC=5.4.99.39;
DE   AltName: Full=Triterpenoid synthase 2;
DE            Short=SlTTS2;
GN   Name=TTS2;
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: Multifunctional oxidosqualene cyclase producing delta-amyrin
CC       (48%), alpha-amyrin (18%), beta-amyrin (13%) and 4 other minor
CC       triterpenes. {ECO:0000269|PubMed:21059824}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-2,3-epoxysqualene = delta-amyrin; Xref=Rhea:RHEA:31883,
CC         ChEBI:CHEBI:15441, ChEBI:CHEBI:63467; EC=5.4.99.55;
CC         Evidence={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   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-2,3-epoxysqualene = alpha-amyrin; Xref=Rhea:RHEA:31387,
CC         ChEBI:CHEBI:10213, ChEBI:CHEBI:15441; EC=5.4.99.40;
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}.
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DR   EMBL; HQ266580; ADU52575.1; -; mRNA.
DR   RefSeq; NP_001234597.1; NM_001247668.2.
DR   AlphaFoldDB; E7DN64; -.
DR   SMR; E7DN64; -.
DR   STRING; 4081.Solyc12g006520.1.1; -.
DR   PaxDb; E7DN64; -.
DR   PRIDE; E7DN64; -.
DR   GeneID; 100529100; -.
DR   KEGG; sly:100529100; -.
DR   eggNOG; KOG0497; Eukaryota.
DR   InParanoid; E7DN64; -.
DR   OrthoDB; 365003at2759; -.
DR   BioCyc; MetaCyc:MON-17972; -.
DR   Proteomes; UP000004994; Unplaced.
DR   ExpressionAtlas; E7DN64; 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   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; Reference proteome; Repeat.
FT   CHAIN           1..763
FT                   /note="Delta-amyrin synthase"
FT                   /id="PRO_0000413971"
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   763 AA;  88036 MW;  0CD81BBC15F49BEC CRC64;
     MWKLKIAKGQ DDRYLYSTNN YIGRQIWEFD PNAGTIEEQA KIEEARQHYW NNRYKVKPNS
     DLLWRMQFLR EKNFKQRIRA VKVEEGEEIS HEIATVALHR AVHFFSALQA TDGHWPAESA
     GPLFFLPPLV MCMYITGHLN TVFPAEHRKE ILRYIYCHQN EDGGWGLHIE GHSTMFCTAM
     SYICMRILGE GPEGGVNNAC ARARKWILDH GSVIAIPSWG KTWLSILGAF EWIGTNPMPP
     EFWILPSFLP VHPAKMWCYC RTVYMPMSYL YGKRFVGPIT PLILKLREEL YDQTYDEINW
     KKVRHVCAKE DLYYPHPFVQ DLMWDSLYIC TEPLLTRWPF NKLRNKALEV TMKHIHYEDE
     NSRYITMGCV EKVLSMLACW VEDPNGDHFK KHLARIPDFL WVAEDGMKMQ GCGSQSWDAS
     LAIQALLASE MNDEISDTLK NGHDFIKQSQ VKDNPSGDFK VMYRHISKGS WAFADQDLGW
     QVSDCTAEAL KCCLLFSTMP PEIVGEAMDP VRLYDSVNVI LSLQSKNGGL SAWEPAGAPE
     YLELLNPTEF FEDIVIEHEH VECTSSAIQA LVRFKKLYPG HRTTEVDNFI NNGVKYIEDV
     QEPDGSWYGN WGVCFIYASW FALGGLAAVG LSYSNCAAVR KSVEFLLRTQ RSDGGWGESY
     RSCPDKVYRE LETEHSNLVQ TAWALMGLIH SGQVERDPRP LHRAAKLLIN FQMEDGDFPQ
     QEITGVFLRN CMMHYALYRN IFPLWGLAEY RRNVLVPLKH NYI