ABAMS_PEA
ID ABAMS_PEA Reviewed; 764 AA.
AC Q9LRH7;
DT 16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=Mixed-amyrin synthase;
DE EC=5.4.99.39;
DE EC=5.4.99.40;
GN Name=OSCPSM;
OS Pisum sativum (Garden pea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX NCBI_TaxID=3888;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=10848960; DOI=10.1046/j.1432-1327.2000.01357.x;
RA Morita M., Shibuya M., Kushiro T., Masuda K., Ebizuka Y.;
RT "Molecular cloning and functional expression of triterpene synthases from
RT pea (Pisum sativum) new alpha-amyrin-producing enzyme is a multifunctional
RT triterpene synthase.";
RL Eur. J. Biochem. 267:3453-3460(2000).
CC -!- FUNCTION: Multifunctional oxidosqualene cyclase producing alpha- and
CC beta-amyrin and several other minor triterpenes.
CC {ECO:0000269|PubMed:10848960}.
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:10848960};
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:10848960};
CC -!- SIMILARITY: Belongs to the terpene cyclase/mutase family.
CC {ECO:0000305}.
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DR EMBL; AB034803; BAA97559.1; -; mRNA.
DR AlphaFoldDB; Q9LRH7; -.
DR SMR; Q9LRH7; -.
DR PRIDE; Q9LRH7; -.
DR KEGG; ag:BAA97559; -.
DR BRENDA; 5.4.99.40; 4872.
DR GO; GO:0005811; C:lipid droplet; IEA:InterPro.
DR GO; GO:0042561; F:alpha-amyrin synthase activity; IDA:UniProtKB.
DR GO; GO:0042300; F:beta-amyrin synthase activity; IDA:UniProtKB.
DR GO; GO:0019745; P:pentacyclic 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; Repeat.
FT CHAIN 1..764
FT /note="Mixed-amyrin synthase"
FT /id="PRO_0000413970"
FT REPEAT 148..189
FT /note="PFTB 1"
FT REPEAT 514..556
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 764 AA; 88277 MW; DED4CAE6CB822197 CRC64;
MWKLKIGDGG KDRNIFSTNN FVGRQTWEFD PDAGTSQEKA QVEAARQHFY DNRFEVKACS
DLLWRFQILK EKNFKQTIES VKIKDEEEIS EENVAITLRR AVHHLSTLQS NDGHWPALNA
GPLFYFPPLV FCMYVTGHLD SIFPYEYRKE ILRYIYCHQN EDGGWGLHVE GHSIMFCTVL
NYICMRILGE GPNGGKEDAC ARARKWIHDH GSVTHVSSWG KIWLSVLGIF DWCASNPMPP
EFWMLPSFLL KHPAKMLCYC RLVYMPMSYL YGKRFVGPIT PLILMLREEL LTQPYEKVNW
KKTRHLCAKE DLYYPHPLIQ DLIWDSLYIF VEPLLTHWPF NKLLREKALQ TVMKHIHYED
ENSRYITIGC VEKVLCILAC WVEDPNGDAF KKHLARLPDY LWVSEDGMTL HSFGSQTWDA
SLIIQALLAT NLIEDVGPIL TKAHEFIKKS QVRDNPSGDF KSMYRHISKG SWTFSDKDHG
WQVSDCTAES LKCCLLLSML PPEIVGEKME PEMLYDSVNI LLSLQGKKGG LPAWEPSEAV
EWLELFNPIE FLEEIVVERE YVECTSSAIQ ALVLFKKLYP EHRKKEVENF IANAVRFLEY
KQTSDGSWYG NWGICFTYGS WFALNGLVAA GKTYDNCAAI RKGVEFLLTT QREDGGWGES
HLSSSKKIYV PLERSQSNIV QTSWAIMGLI HAGQMERDPT PLHRAVKLII NFQQEEGDWP
QQELTGVFMK NCMLQYAMYR DIFPTWALAE YRRRILLASP AVAI