LUP1_ARATH
ID LUP1_ARATH Reviewed; 757 AA.
AC Q9C5M3; O49985; O64551; P92977;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Lupeol synthase 1 {ECO:0000303|PubMed:11247608, ECO:0000303|PubMed:9883589};
DE Short=AtLUP1 {ECO:0000303|PubMed:11247608, ECO:0000303|PubMed:9883589};
DE EC=5.4.99.41 {ECO:0000269|PubMed:10930257, ECO:0000269|PubMed:11247608, ECO:0000269|PubMed:17107079};
DE AltName: Full=(S)-2,3-epoxysqualene synthase {ECO:0000303|PubMed:11247608, ECO:0000303|PubMed:9883589};
DE EC=4.2.1.128 {ECO:0000269|PubMed:10930257, ECO:0000269|PubMed:11247608};
DE AltName: Full=Beta-amyrin synthase {ECO:0000303|PubMed:11247608, ECO:0000303|PubMed:9883589};
DE EC=5.4.99.39 {ECO:0000269|PubMed:10930257, ECO:0000269|PubMed:11247608};
DE AltName: Full=Germanicol synthase {ECO:0000303|PubMed:10930257};
DE EC=5.4.99.34 {ECO:0000269|PubMed:10930257};
DE AltName: Full=Lupan-3-beta,20-diol synthase;
GN Name=LUP1 {ECO:0000303|PubMed:11247608, ECO:0000303|PubMed:9883589};
GN OrderedLocusNames=At1g78970 {ECO:0000312|Araport:AT1G78970};
GN ORFNames=YUP8H12R.28 {ECO:0000312|EMBL:AAC17055.1},
GN YUP8H12R.42 {ECO:0000312|EMBL:AAC17055.1};
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].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=9883589; DOI=10.1016/s0031-9422(98)00366-5;
RA Herrera J.B.R., Bartel B., Wilson W.K., Matsuda S.P.T.;
RT "Cloning and characterization of the Arabidopsis thaliana lupeol synthase
RT gene.";
RL Phytochemistry 49:1905-1911(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia; TISSUE=Hypocotyl;
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 [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=10930257; DOI=10.1021/ol006016b;
RA Segura M.J.R., Meyer M.M., Matsuda S.P.T.;
RT "Arabidopsis thaliana LUP1 converts oxidosqualene to multiple triterpene
RT alcohols and a triterpene diol.";
RL Org. Lett. 2:2257-2259(2000).
RN [7]
RP CHARACTERIZATION.
RX DOI=10.1351/pac200375020369;
RA Ebizuka Y., Katsube Y., Tsutsumi T., Kushiro T., Shibuya M.;
RT "Functional genomics approach to the study of triterpene biosynthesis.";
RL Pure Appl. Chem. 75:369-374(2003).
RN [8]
RP CATALYTIC ACTIVITY, AND REACTION MECHANISM.
RX PubMed=17107079; DOI=10.1021/ol062310d;
RA Kushiro T., Hoshino M., Tsutsumi T., Kawai K., Shiro M., Shibuya M.,
RA Ebizuka Y.;
RT "Stereochemical course in water addition during LUP1-catalyzed triterpene
RT cyclization.";
RL Org. Lett. 8:5589-5592(2006).
CC -!- FUNCTION: Multifunctional enzyme that converts oxidosqualene to lupeol
CC and 3,20-dihydroxylupane. Minor production of beta-amyrin, germanicol,
CC taraxasterol and psi-taraxasterol. {ECO:0000269|PubMed:10930257,
CC ECO:0000269|PubMed:11247608}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=lupan-3beta,20-diol = (S)-2,3-epoxysqualene + H2O;
CC Xref=Rhea:RHEA:31351, ChEBI:CHEBI:15377, ChEBI:CHEBI:15441,
CC ChEBI:CHEBI:62735; EC=4.2.1.128;
CC Evidence={ECO:0000269|PubMed:10930257, ECO:0000269|PubMed:11247608};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-2,3-epoxysqualene = lupeol; Xref=Rhea:RHEA:31383,
CC ChEBI:CHEBI:6570, ChEBI:CHEBI:15441; EC=5.4.99.41;
CC Evidence={ECO:0000269|PubMed:10930257, ECO:0000269|PubMed:11247608,
CC ECO:0000269|PubMed:17107079};
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:10930257, ECO:0000269|PubMed:11247608};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-2,3-epoxysqualene = germanicol; Xref=Rhea:RHEA:31003,
CC ChEBI:CHEBI:15441, ChEBI:CHEBI:62455; EC=5.4.99.34;
CC Evidence={ECO:0000269|PubMed:10930257};
CC -!- SIMILARITY: Belongs to the terpene cyclase/mutase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC17055.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; U49919; AAD05032.1; -; mRNA.
DR EMBL; U87266; AAB94341.1; -; mRNA.
DR EMBL; AC002986; AAC17055.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE36186.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE36187.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM58606.1; -; Genomic_DNA.
DR EMBL; AF360147; AAK25857.1; -; mRNA.
DR EMBL; AY052358; AAK96549.1; -; mRNA.
DR EMBL; AY142678; AAN13216.1; -; mRNA.
DR PIR; T01058; T01058.
DR RefSeq; NP_001321029.1; NM_001334865.1.
DR RefSeq; NP_178018.1; NM_106546.3.
DR RefSeq; NP_849903.1; NM_179572.2.
DR AlphaFoldDB; Q9C5M3; -.
DR SMR; Q9C5M3; -.
DR BioGRID; 29456; 2.
DR IntAct; Q9C5M3; 1.
DR STRING; 3702.AT1G78970.1; -.
DR PaxDb; Q9C5M3; -.
DR PRIDE; Q9C5M3; -.
DR ProteomicsDB; 238808; -.
DR EnsemblPlants; AT1G78970.1; AT1G78970.1; AT1G78970.
DR EnsemblPlants; AT1G78970.2; AT1G78970.2; AT1G78970.
DR EnsemblPlants; AT1G78970.3; AT1G78970.3; AT1G78970.
DR GeneID; 844237; -.
DR Gramene; AT1G78970.1; AT1G78970.1; AT1G78970.
DR Gramene; AT1G78970.2; AT1G78970.2; AT1G78970.
DR Gramene; AT1G78970.3; AT1G78970.3; AT1G78970.
DR KEGG; ath:AT1G78970; -.
DR Araport; AT1G78970; -.
DR TAIR; locus:2207310; AT1G78970.
DR eggNOG; KOG0497; Eukaryota.
DR HOGENOM; CLU_009074_2_1_1; -.
DR InParanoid; Q9C5M3; -.
DR OMA; EFMANTM; -.
DR OrthoDB; 365003at2759; -.
DR PhylomeDB; Q9C5M3; -.
DR BioCyc; ARA:AT1G78970-MON; -.
DR BRENDA; 4.2.1.128; 399.
DR BRENDA; 5.4.99.41; 399.
DR PRO; PR:Q9C5M3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C5M3; baseline and differential.
DR Genevisible; Q9C5M3; AT.
DR GO; GO:0005811; C:lipid droplet; IEA:InterPro.
DR GO; GO:0042300; F:beta-amyrin synthase activity; IDA:TAIR.
DR GO; GO:0102245; F:lupan-3beta,20-diol synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0042299; F:lupeol 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; Lyase; Reference proteome; Repeat.
FT CHAIN 1..757
FT /note="Lupeol synthase 1"
FT /id="PRO_0000366131"
FT REPEAT 149..190
FT /note="PFTB 1"
FT /evidence="ECO:0000255"
FT REPEAT 589..629
FT /note="PFTB 2"
FT /evidence="ECO:0000255"
FT REPEAT 638..679
FT /note="PFTB 3"
FT /evidence="ECO:0000255"
FT ACT_SITE 483
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P48449"
FT CONFLICT 466
FT /note="S -> W (in Ref. 2; AAB94341)"
FT /evidence="ECO:0000305"
FT CONFLICT 503
FT /note="V -> G (in Ref. 1; AAD05032)"
FT /evidence="ECO:0000305"
FT CONFLICT 698
FT /note="I -> T (in Ref. 1; AAD05032)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 757 AA; 87352 MW; 98C1C0C30D7975D5 CRC64;
MWKLKIGKGN GEDPHLFSSN NFVGRQTWKF DHKAGSPEER AAVEEARRGF LDNRFRVKGC
SDLLWRMQFL REKKFEQGIP QLKATNIEEI TYETTTNALR RGVRYFTALQ ASDGHWPGEI
TGPLFFLPPL IFCLYITGHL EEVFDAEHRK EMLRHIYCHQ NEDGGWGLHI ESKSVMFCTV
LNYICLRMLG ENPEQDACKR ARQWILDRGG VIFIPSWGKF WLSILGVYDW SGTNPTPPEL
LMLPSFLPIH PGKILCYSRM VSIPMSYLYG KRFVGPITPL ILLLREELYL EPYEEINWKK
SRRLYAKEDM YYAHPLVQDL LSDTLQNFVE PLLTRWPLNK LVREKALQLT MKHIHYEDEN
SHYITIGCVE KVLCMLACWV ENPNGDYFKK HLARIPDYMW VAEDGMKMQS FGCQLWDTGF
AIQALLASNL PDETDDALKR GHNYIKASQV RENPSGDFRS MYRHISKGAW TFSDRDHGWQ
VSDCTAEALK CCLLLSMMSA DIVGQKIDDE QLYDSVNLLL SLQSGNGGVN AWEPSRAYKW
LELLNPTEFM ANTMVEREFV ECTSSVIQAL DLFRKLYPDH RKKEINRSIE KAVQFIQDNQ
TPDGSWYGNW GVCFIYATWF ALGGLAAAGE TYNDCLAMRN GVHFLLTTQR DDGGWGESYL
SCSEQRYIPS EGERSNLVQT SWAMMALIHT GQAERDLIPL HRAAKLIINS QLENGDFPQQ
EIVGAFMNTC MLHYATYRNT FPLWALAEYR KVVFIVN
