BAMS1_PANGI
ID BAMS1_PANGI Reviewed; 763 AA.
AC O82140; A0A0N7AWI6;
DT 16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Beta-amyrin synthase 1 {ECO:0000303|PubMed:9746369};
DE Short=Pgb-AS {ECO:0000303|PubMed:23232757};
DE EC=5.4.99.39 {ECO:0000269|PubMed:9746369};
DE AltName: Full=Oxidosqualene cyclase 1 {ECO:0000303|PubMed:24198659};
GN Name=OSCPNY1 {ECO:0000303|PubMed:9746369};
GN Synonyms=bAS {ECO:0000303|Ref.2}, beta-AS {ECO:0000303|PubMed:30577538,
GN ECO:0000303|Ref.2}, PNY1 {ECO:0000303|PubMed:24198659,
GN ECO:0000303|PubMed:29509695};
OS Panax ginseng (Korean ginseng).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Apiales; Araliaceae; Panax.
OX NCBI_TaxID=4054;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC TISSUE=Root;
RX PubMed=9746369; DOI=10.1046/j.1432-1327.1998.2560238.x;
RA Kushiro T., Shibuya M., Ebizuka Y.;
RT "Beta-amyrin synthase--cloning of oxidosqualene cyclase that catalyzes the
RT formation of the most popular triterpene among higher plants.";
RL Eur. J. Biochem. 256:238-244(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Hou S., Han M., Liu C., Yang L.;
RT "Cloning and expression analysis of HMGR, SS, SE, DS, and bAS genes in
RT Panax ginseng.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP INDUCTION BY METHYL JASMONATE.
RC STRAIN=cv. Chunpoong; TISSUE=Leaf;
RX PubMed=15356323; DOI=10.1093/pcp/pch126;
RA Lee M.-H., Jeong J.-H., Seo J.-W., Shin C.-G., Kim Y.-S., In J.-G.,
RA Yang D.-C., Yi J.-S., Choi Y.-E.;
RT "Enhanced triterpene and phytosterol biosynthesis in Panax ginseng
RT overexpressing squalene synthase gene.";
RL Plant Cell Physiol. 45:976-984(2004).
RN [4]
RP INDUCTION BY CLE; ETHYLENE; ROSE BENGAL; NITRIC OXIDE AND HYDROGEN
RP PEROXIDE.
RX PubMed=15821288; DOI=10.1093/pcp/pci103;
RA Xu X., Hu X., Neill S.J., Fang J., Cai W.;
RT "Fungal elicitor induces singlet oxygen generation, ethylene release and
RT saponin synthesis in cultured cells of Panax ginseng C. A. Meyer.";
RL Plant Cell Physiol. 46:947-954(2005).
RN [5]
RP INDUCTION BY METHYL JASMONATE.
RX PubMed=15538577; DOI=10.1007/s00299-004-0845-4;
RA Choi D.-W., Jung J., Ha Y.I., Park H.-W., In D.S., Chung H.-J., Liu J.R.;
RT "Analysis of transcripts in methyl jasmonate-treated ginseng hairy roots to
RT identify genes involved in the biosynthesis of ginsenosides and other
RT secondary metabolites.";
RL Plant Cell Rep. 23:557-566(2005).
RN [6]
RP INDUCED BY HEAVY METAL STRESS.
RX PubMed=23232757; DOI=10.1007/s00128-012-0891-5;
RA Balusamy S.R.D., Kim Y.-J., Rahimi S., Senthil K.S., Lee O.R., Lee S.,
RA Yang D.-C.;
RT "Transcript pattern of cytochrome P450, antioxidant and ginsenoside
RT biosynthetic pathway genes under heavy metal stress in Panax ginseng
RT Meyer.";
RL Bull. Environ. Contam. Toxicol. 90:194-202(2013).
RN [7]
RP GENE FAMILY.
RX PubMed=24198659; DOI=10.5142/jgr.2013.37.332;
RA Kim D.S., Song M., Kim S.-H., Jang D.-S., Kim J.-B., Ha B.-K., Kim S.H.,
RA Lee K.J., Kang S.-Y., Jeong I.Y.;
RT "The improvement of ginsenoside accumulation in Panax ginseng as a result
RT of gamma-irradiation.";
RL J. Ginseng Res. 37:332-340(2013).
RN [8]
RP REVIEW.
RX PubMed=29378087; DOI=10.1002/bab.1649;
RA Lu J., Li J., Wang S., Yao L., Liang W., Wang J., Gao W.;
RT "Advances in ginsenoside biosynthesis and metabolic regulation.";
RL Biotechnol. Appl. Biochem. 65:514-522(2018).
RN [9]
RP REVIEW, AND NOMENCLATURE.
RX PubMed=29509695; DOI=10.3390/molecules23030589;
RA Yang J.-L., Hu Z.-F., Zhang T.-T., Gu A.-D., Gong T., Zhu P.;
RT "Progress on the studies of the key enzymes of ginsenoside biosynthesis.";
RL Molecules 23:0-0(2018).
RN [10]
RP DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, AND INDUCTION BY ABIOTIC FACTORS.
RX PubMed=30577538; DOI=10.3390/molecules24010014;
RA Zhang T., Han M., Yang L., Han Z., Cheng L., Sun Z., Yang L.;
RT "The effects of environmental factors on ginsenoside biosynthetic enzyme
RT gene expression and saponin abundance.";
RL Molecules 24:0-0(2018).
CC -!- FUNCTION: Component of the oleanane-type triterpene saponins
CC biosynthetic pathway (PubMed:15821288, PubMed:29378087). Oxidosqualene
CC cyclase converting oxidosqualene into beta-amyrin, generating five
CC rings and eight asymmetric centers in a single transformation
CC (PubMed:9746369). {ECO:0000269|PubMed:9746369,
CC ECO:0000303|PubMed:15821288, ECO:0000303|PubMed:29378087}.
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:9746369};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31008;
CC Evidence={ECO:0000303|PubMed:29509695};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000305}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P48449}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P48449}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P48449}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in roots, and, to a lower extent,
CC in stems and leaves. {ECO:0000269|PubMed:30577538}.
CC -!- DEVELOPMENTAL STAGE: Progressive decrease in roots from the leaf opened
CC stage to the green fruit, red fruit and root growth stages,
CC respectively. {ECO:0000269|PubMed:30577538}.
CC -!- INDUCTION: Induced methyl jasmonate (MeJA) in adventitious roots
CC (PubMed:15356323, PubMed:15538577). Accumulates upon Cle-mediated
CC signaling, an elicitor derived from fungal cell walls of C.lagenarium,
CC thus inducing the accumulation of saponins. Triggered by ethylene
CC (ACC), rose bengal (RB), nitric oxide (NO) and hydrogen peroxide
CC (H(2)O(2)) (PubMed:15821288). Accumulates under heavy metal stress in
CC the presence of NiCl(2) and CdCl(2) (PubMed:23232757). Influenced in
CC roots and leaves by relative humidity, and in roots by soil water
CC potential (PubMed:30577538). {ECO:0000269|PubMed:15356323,
CC ECO:0000269|PubMed:15538577, ECO:0000269|PubMed:15821288,
CC ECO:0000269|PubMed:23232757, ECO:0000269|PubMed:30577538}.
CC -!- SIMILARITY: Belongs to the terpene cyclase/mutase family.
CC {ECO:0000305}.
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DR EMBL; AB009030; BAA33461.1; -; mRNA.
DR EMBL; KJ939267; AJV26448.1; -; mRNA.
DR AlphaFoldDB; O82140; -.
DR SMR; O82140; -.
DR KEGG; ag:BAA33461; -.
DR BioCyc; MetaCyc:MON-12195; -.
DR BRENDA; 5.4.99.39; 7895.
DR UniPathway; UPA00213; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005811; C:lipid droplet; IEA:InterPro.
DR GO; GO:0016866; F:intramolecular transferase activity; IEA:InterPro.
DR GO; GO:0009723; P:response to ethylene; IEP:UniProtKB.
DR GO; GO:0042542; P:response to hydrogen peroxide; IEP:UniProtKB.
DR GO; GO:0009753; P:response to jasmonic acid; IEP:UniProtKB.
DR GO; GO:0010038; P:response to metal ion; IEP:UniProtKB.
DR GO; GO:0002238; P:response to molecule of fungal origin; IEP:UniProtKB.
DR GO; GO:0071731; P:response to nitric oxide; IEP:UniProtKB.
DR GO; GO:0016104; P:triterpenoid biosynthetic process; IEA:InterPro.
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 Endoplasmic reticulum; Isomerase; Isoprene biosynthesis; Membrane; Repeat.
FT CHAIN 1..763
FT /note="Beta-amyrin synthase 1"
FT /id="PRO_0000413965"
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; 87994 MW; F41CC99BA0E372F6 CRC64;
MWKLKIAEGN KNDPYLYSTN NFVGRQTWEF DPDYVASPGE LEEVEQVRRQ FWDNRYQVKP
SGDLLWRMQF LREKNFRQTI PQVKVGDDEA VTYEAATTTL RRAVHFFSAL QASDGHWPAE
NSGPLFFLPP LVMCVYITGH LDTVFPAEHR KEILRYIYCH QNEDGGWGLH IEGHSTMFCT
TLSYICMRIL GEGPDGGVNN ACARGRKWIL DHGSVTAIPS WGKTWLSILG VYEWIGSNPM
PPEFWILPSF LPMHPAKMWC YCRMVYMPMS YLYGKRFVGP ITPLILQLRE ELYGQPYNEI
NWRKTRRVCA KEDIYYPHPL IQDLLWDSLY VLTEPLLTRW PFNKLREKAL QTTMKHIHYE
DENSRYITIG CVEKVLCMLV CWVEDPNGDY FRKHLARIPD YIWVAEDGMK MQSFGSQEWD
TGFSIQALLD SDLTHEIGPT LMKGHDFIKK SQVKDNPSGD FKSMYRHISK GSWTFSDQDH
GWQVSDCTAE GLKCCLIFST MPEEIVGKKI KPERLYDSVN VLLSLQRKNG GLSAWEPAGA
QEWLELLNPT EFFADIVIEH EYVECTSSAI QALVLFKKLY PGHRKKEIDN FITNAVRYLE
DTQMPDGSWY GNWGVCFTYG SWFALGGLAA AGKTYYNCAA VRKAVEFLLK SQMDDGGWGE
SYLSCPKKVY VPLEGNRSNL VHTGWALMGL IHSEQAERDP TPLHRAAKLL INSQMEDGDF
PQQEISGVFM KNCMLHYAAY RNIYPLWALA EYRRRVPLPS LGT
