LUP4_ARATH
ID LUP4_ARATH Reviewed; 759 AA.
AC B6EXY6; O64553; Q3ECA8;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 2.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=Beta-amyrin synthase {ECO:0000303|PubMed:18977664};
DE Short=AtBAS {ECO:0000303|PubMed:18977664};
DE EC=5.4.99.39 {ECO:0000269|PubMed:11247608};
DE AltName: Full=Lupeol synthase 4 {ECO:0000303|PubMed:11247608};
DE Short=AtLUP4 {ECO:0000303|PubMed:11247608};
GN Name=BAS {ECO:0000303|PubMed:18977664};
GN Synonyms=LUP4 {ECO:0000303|PubMed:11247608};
GN OrderedLocusNames=At1g78950 {ECO:0000312|Araport:AT1G78950};
GN ORFNames=YUP8H12R.44 {ECO:0000312|EMBL:AAC17080.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=18977664; DOI=10.1016/j.plaphy.2008.09.007;
RA Shibuya M., Katsube Y., Otsuka M., Zhang H., Tansakul P., Xiang T.,
RA Ebizuka Y.;
RT "Identification of a product specific beta-amyrin synthase from Arabidopsis
RT thaliana.";
RL Plant Physiol. Biochem. 47:26-30(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP IDENTIFICATION, CATALYTIC ACTIVITY, AND NOMENCLATURE.
RX PubMed=11247608; DOI=10.1023/a:1006476123930;
RA Husselstein-Muller T., Schaller H., Benveniste P.;
RT "Molecular cloning and expression in yeast of 2,3-oxidosqualene-
RT triterpenoid cyclases from Arabidopsis thaliana.";
RL Plant Mol. Biol. 45:75-92(2001).
RN [5]
RP BIOTECHNOLOGY, AND REVIEW.
RX PubMed=31138208; DOI=10.1186/s12934-019-1138-5;
RA Wang C., Su X., Sun M., Zhang M., Wu J., Xing J., Wang Y., Xue J., Liu X.,
RA Sun W., Chen S.;
RT "Efficient production of glycyrrhetinic acid in metabolically engineered
RT Saccharomyces cerevisiae via an integrated strategy.";
RL Microb. Cell Fact. 18:95-95(2019).
CC -!- FUNCTION: Converts oxidosqualene to beta-amyrin.
CC {ECO:0000269|PubMed:18977664}.
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:11247608};
CC -!- BIOTECHNOLOGY: Saccharomyces cerevisiae expressing Glycyrrhiza
CC uralensis CYP88D6 and CYP72A154, combined with the expression of
CC Arabidopsis thaliana beta-amyrin synthase (beta-AS) and NADPH-
CC cytochrome P450 reductase 1 (ATR1), accumulates glycyrrhetinic acid
CC (GA) and, to lower levels, beta-amyrin; these GA production was
CC increased in the presence of G.uralensis cytochrome b5 (CYB5).
CC {ECO:0000269|PubMed:31138208}.
CC -!- SIMILARITY: Belongs to the terpene cyclase/mutase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC17080.1; Type=Erroneous gene model prediction; Note=The predicted gene At1g78950 has been split into 2 genes: At1g78950 and At1g78955.; Evidence={ECO:0000305};
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DR EMBL; AB374428; BAG82628.1; -; mRNA.
DR EMBL; AC002986; AAC17080.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE36183.1; -; Genomic_DNA.
DR PIR; T01060; T01060.
DR RefSeq; NP_178016.2; NM_106544.5.
DR AlphaFoldDB; B6EXY6; -.
DR SMR; B6EXY6; -.
DR STRING; 3702.AT1G78950.1; -.
DR PaxDb; B6EXY6; -.
DR ProteomicsDB; 238809; -.
DR EnsemblPlants; AT1G78950.1; AT1G78950.1; AT1G78950.
DR GeneID; 844234; -.
DR Gramene; AT1G78950.1; AT1G78950.1; AT1G78950.
DR KEGG; ath:AT1G78950; -.
DR Araport; AT1G78950; -.
DR TAIR; locus:2207315; AT1G78950.
DR eggNOG; KOG0497; Eukaryota.
DR HOGENOM; CLU_009074_2_0_1; -.
DR OMA; YINCEAM; -.
DR PhylomeDB; B6EXY6; -.
DR BRENDA; 5.4.99.39; 399.
DR PRO; PR:B6EXY6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; B6EXY6; baseline and differential.
DR Genevisible; B6EXY6; AT.
DR GO; GO:0005811; C:lipid droplet; IEA:InterPro.
DR GO; GO:0042300; F:beta-amyrin synthase activity; IDA:TAIR.
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..759
FT /note="Beta-amyrin synthase"
FT /id="PRO_0000366134"
FT REPEAT 149..190
FT /note="PFTB 1"
FT REPEAT 592..632
FT /note="PFTB 2"
FT REPEAT 641..682
FT /note="PFTB 3"
FT ACT_SITE 486
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P48449"
FT CONFLICT 334
FT /note="P -> L (in Ref. 1; BAG82628)"
FT /evidence="ECO:0000305"
FT CONFLICT 544
FT /note="L -> S (in Ref. 1; BAG82628)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 759 AA; 86953 MW; E8677A08B251C33D CRC64;
MWRLKIGEGN GDDPYLFTTN NFAGRQTWEF DPDGGSPEER HSVVEARRIF YDNRFHVKAS
SDLLWRMQFL REKKFEQRIA PVKVEDSEKV TFETATSALR RGIHFFSALQ ASDGHWPAEN
AGPLFFLPPL VFCLYITGHL DEVFTSEHRK EILRYIYCHQ KEDGGWGLHI EGHSTMFCTT
LNYICMRILG ESPDGGHDNA CGRAREWILS HGGVTYIPSW GKTWLSILGV FDWSGSNPMP
PEFWILPSFF PVHPAKMWSY CRMVYLPMSY LYGKRFVGPI TSLILQLRKE LYLQPYEEIN
WMKVRHLCAK EDTYYPRPLV QELVWDSLYI FAEPFLARWP FNKLLREKAL QLAMKHIHYE
DENSRYITIG CVEKVLCMLA CWVEDPNGDY FKKHLSRISD YLWMAEDGMK MQSFGSQLWD
TGFAMQALLA SNLSSEISDV LRRGHEFIKN SQVGENPSGD YKSMYRHISK GAWTFSDRDH
GWQVSDCTAH GLKCCLLFSM LAPDIVGPKQ DPERLHDSVN ILLSLQSKNG GMTAWEPAGA
PKWLELLNPT EMFSDIVIEH EYSECTSSAI QALSLFKQLY PDHRTTEITA FIKKAAEYLE
NMQTRDGSWY GNWGICFTYG TWFALAGLAA AGKTFNDCEA IRKGVQFLLA AQKDNGGWGE
SYLSCSKKIY IAQVGEISNV VQTAWALMGL IHSGQAERDP IPLHRAAKLI INSQLESGDF
PQQQATGVFL KNCTLHYAAY RNIHPLWALA EYRARVSLP
