BAMS1_BARVU
ID BAMS1_BARVU Reviewed; 762 AA.
AC A0A0U2U4F3; H9NAL5;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 16-MAR-2016, sequence version 1.
DT 03-AUG-2022, entry version 22.
DE RecName: Full=Beta-amyrin synthase 1 {ECO:0000305};
DE EC=5.4.99.39 {ECO:0000269|PubMed:26333142, ECO:0000269|PubMed:29603041};
DE AltName: Full=Protein LUP5 homolog {ECO:0000303|PubMed:26333142};
GN Name=LUP5 {ECO:0000303|PubMed:26333142}; Synonyms=BAS1 {ECO:0000305};
OS Barbarea vulgaris (Yellow rocket) (Erysimum barbarea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Cardamineae; Barbarea.
OX NCBI_TaxID=50459;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=26333142; DOI=10.1111/tpj.13012;
RA Khakimov B., Kuzina V., Erthmann P.O., Fukushima E.O., Augustin J.M.,
RA Olsen C.E., Scholtalbers J., Volpin H., Andersen S.B., Hauser T.P.,
RA Muranaka T., Bak S.;
RT "Identification and genome organization of saponin pathway genes from a
RT wild crucifer, and their use for transient production of saponins in
RT Nicotiana benthamiana.";
RL Plant J. 84:478-490(2015).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RA Wei X., Li X.;
RT "Cloning and characterization of beta-amyrin synthase gene in Barbarea
RT vulgaris.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=29603041; DOI=10.1007/s11103-018-0723-z;
RA Erthmann P.O., Agerbirk N., Bak S.;
RT "A tandem array of UDP-glycosyltransferases from the UGT73C subfamily
RT glycosylate sapogenins, forming a spectrum of mono- and bisdesmosidic
RT saponins.";
RL Plant Mol. Biol. 97:37-55(2018).
CC -!- FUNCTION: Component of the oleanane-type triterpene saponins
CC biosynthetic pathway (PubMed:26333142, PubMed:29603041). Oxidosqualene
CC cyclase converting oxidosqualene into beta-amyrin, generating five
CC rings and eight asymmetric centers in a single transformation
CC (PubMed:26333142, PubMed:29603041). {ECO:0000269|PubMed:26333142,
CC ECO:0000269|PubMed:29603041}.
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:26333142, ECO:0000269|PubMed:29603041};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31008;
CC Evidence={ECO:0000269|PubMed:26333142, ECO:0000269|PubMed:29603041};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the terpene cyclase/mutase family.
CC {ECO:0000305}.
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DR EMBL; KP784690; ALR73780.1; -; mRNA.
DR EMBL; JQ172795; AFF27505.1; -; mRNA.
DR EMBL; JQ172796; AFF27506.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0U2U4F3; -.
DR SMR; A0A0U2U4F3; -.
DR BRENDA; 5.4.99.39; 16171.
DR UniPathway; UPA00213; -.
DR GO; GO:0005811; C:lipid droplet; IEA:InterPro.
DR GO; GO:0042300; F:beta-amyrin synthase activity; IDA:UniProtKB.
DR GO; GO:0016104; P: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 SUPFAM; SSF48239; SSF48239; 2.
DR TIGRFAMs; TIGR01787; squalene_cyclas; 1.
DR PROSITE; PS01074; TERPENE_SYNTHASES; 1.
PE 1: Evidence at protein level;
KW Isomerase; Isoprene biosynthesis; Repeat.
FT CHAIN 1..762
FT /note="Beta-amyrin synthase 1"
FT /id="PRO_0000452137"
FT REPEAT 99..141
FT /note="PFTB 1"
FT /evidence="ECO:0000255"
FT REPEAT 149..190
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 613
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P48449"
SQ SEQUENCE 762 AA; 87503 MW; 4FFFE2BF615EDAD8 CRC64;
MWRLKLGEGN GDDPYLFSSN NFVGRQTWEF DPKAGTLEER AAVEEARRSF LVNRSRVKAC
SDLLWRMQFL KEAKFEQVIP PVKIEDAKDI TYENATDSLR RGVSFFSALQ ASDGHWPGEI
AGPLFFLPPL VFCLYITGHL EEIFDEEHRK EMLRHVYCHQ NEDGGWGLHV ESKSIMFCTV
LNYICLRMLG EGPNGGRDNA CKRARQWILD RGGVTYIPSW GKIWLSILGI YDWSGTNPMP
PEIWLLPSFV PIHLAKTLCY CRMVYMPMSY LYGKRFVGPI TPLILQLREE LHLQPYEAIN
WNKTRRLYAK EDMYFPHPLV QDLIWDTLHI FVEPLLTHWP LNKLVREKAL RLAMKHIHYE
DENSHYITIG CVEKVLCMLA CWIDDPNGDY FKKHLARIPD YMWVAEDGMK MQSFGSQQWD
TGFAVQAIIA SDLSSETGDV LKRGHDYIKK SQIRENPSGD FKSMYRHISK GAWTLSDRDH
GWQVSDCTAE ALKCCLLLSM MPAEVVGHKM DPEQLYDSVN LLLSLQSANG GVTAWEPVRA
YAWTELLNPT EFLANLVAER EYVECTSSVV QALVLFQQLY PDHKTKKISR AIEKAVQFLE
NEQKPDGSWY GNWGVCFIYA TWFALGGLAA AGKTYKTSQA MRKGVEFLLT TQKDDGGWGE
SYLSCPEQRY IPLEGNRSNL VQTAWAIMGL IHAGQAERDP IPLHRAAKLI INSQMENGDF
PQQEIVGVFM RNCLLHYATF RNTFPLWALA EYRKAAFVTH KH
