BAMS2_PANGI
ID BAMS2_PANGI Reviewed; 761 AA.
AC O82146;
DT 16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 66.
DE RecName: Full=Beta-amyrin synthase 2 {ECO:0000303|Ref.1};
DE EC=5.4.99.39 {ECO:0000250|UniProtKB:O82140};
DE AltName: Full=Oxidosqualene cyclase 2 {ECO:0000303|PubMed:24198659};
GN Name=OSCPNY2 {ECO:0000303|Ref.1};
GN Synonyms=PNY2 {ECO:0000303|PubMed:24198659};
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].
RC TISSUE=Root;
RA Kushiro T., Shibuya M., Ebizuka Y.;
RT "Molecular cloning of oxidosqualene cyclase cDNA from Panax ginseng: the
RT isogene that encodes beta-amyrin synthase.";
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
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 [4]
RP REVIEW.
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).
CC -!- FUNCTION: Component of the oleanane-type triterpene saponins (e.g.
CC ginsenosides or panaxosides) biosynthetic pathway (PubMed:29378087).
CC Oxidosqualene cyclase converting oxidosqualene into beta-amyrin,
CC generating five rings and eight asymmetric centers in a single
CC transformation (By similarity). {ECO:0000250|UniProtKB:O82140,
CC 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:0000250|UniProtKB:O82140};
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 -!- SIMILARITY: Belongs to the terpene cyclase/mutase family.
CC {ECO:0000305}.
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DR EMBL; AB014057; BAA33722.1; -; mRNA.
DR AlphaFoldDB; O82146; -.
DR SMR; O82146; -.
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: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 2: Evidence at transcript level;
KW Endoplasmic reticulum; Isomerase; Isoprene biosynthesis; Membrane; Repeat.
FT CHAIN 1..761
FT /note="Beta-amyrin synthase 2"
FT /id="PRO_0000413966"
FT REPEAT 98..140
FT /note="PFTB 1"
FT /evidence="ECO:0000255"
FT REPEAT 148..189
FT /note="PFTB 2"
FT /evidence="ECO:0000255"
FT REPEAT 439..483
FT /note="PFTB 3"
FT /evidence="ECO:0000255"
FT REPEAT 513..558
FT /note="PFTB 4"
FT /evidence="ECO:0000255"
FT REPEAT 590..630
FT /note="PFTB 5"
FT /evidence="ECO:0000255"
FT REPEAT 639..680
FT /note="PFTB 6"
FT /evidence="ECO:0000255"
FT REPEAT 701..742
FT /note="PFTB 7"
FT /evidence="ECO:0000255"
FT ACT_SITE 484
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P48449"
FT SITE 417
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P48449"
FT SITE 473
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P48449"
FT SITE 611
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P48449"
SQ SEQUENCE 761 AA; 87875 MW; BDCFAD5E1C11E441 CRC64;
MWRLMTAKGG NDPYLYSTNN FIGRQTWEFD PDYGTPAERA EVEEARLHFW NNRYQVKPSS
DVLWRMQFLK EKNFKQIIPQ VKVEDGEEIT YEAATTTLRR AVHYFSALQA DDGHWPAENA
GPLFFLPPLV MCLYITGHLN TVFPAEHRIE ILRYIYCHQN DDGGWGLHIE GHSTMFCTAL
SYICMRILGE GRDGGENNAC ARARKWILDH GSVTAIPSWG KTWLSILGLF DWSGSNPMPP
EFWILPPFLP MHPAKMWCYC RMVYMPMSYL YGKRFVGPIT PLILQLREEL YAQAYDEINW
RKVRHNCAKE DLYYPHPLIQ DLMWDSLYIF TEPFLTRWPF NKLREKALQT TMKHIHYEDE
NSRYITIGCV EKVLCMLACW VEDPNGDYFK QHLARIPDYI WVAEDGMKMQ SFGSQEWDTG
FAIQALLASD LIDEIRPTLM KGHDFIKKSQ VKENPSGDFK SMHRHISKGS WTFSDQDHGW
QVSDCTAEAL KCCLLFSRMP TEIVGDKMED NQLFDAVNML LSLQSKNGGL AAWEPAGSSE
WLELLNPTEF FEDIVIEHEY VECTSSAIQA MVMFKKLYPG HRKKEIEVSI TNAVQYLEDI
QMPDGSWYGN WGVCFTYGTW FAMGGLTAAG KTYNNCQTLH KAVDFLIKSQ RSDGGWGESY
LSCPNKEYTP LEGNRSNLVH TSWAMMGLIH SRQAERDPTP LHRAAKLLIN SQMESGDFPQ
QEITGVFMKN CMLHYAASRN IYPLWALAEY RKNVRLPSKS V
