BARS1_ARATH
ID BARS1_ARATH Reviewed; 759 AA.
AC O23390;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Baruol synthase;
DE Short=AtBARS1;
DE EC=5.4.99.57;
DE AltName: Full=Pentacyclic triterpene synthase 2;
DE Short=AtPEN2;
GN Name=BARS1; Synonyms=PEN2; OrderedLocusNames=At4g15370;
GN ORFNames=dl3730c, FCAALL.279;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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, 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 FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=17705488; DOI=10.1021/ja073133u;
RA Lodeiro S., Xiong Q., Wilson W.K., Kolesnikova M.D., Onak C.S.,
RA Matsuda S.P.T.;
RT "An oxidosqualene cyclase makes numerous products by diverse mechanisms: a
RT challenge to prevailing concepts of triterpene biosynthesis.";
RL J. Am. Chem. Soc. 129:11213-11222(2007).
CC -!- FUNCTION: Converts oxidosqualene to baruol (90%) and 22 minor products.
CC {ECO:0000269|PubMed:17705488}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-2,3-epoxysqualene = baruol; Xref=Rhea:RHEA:31987,
CC ChEBI:CHEBI:15441, ChEBI:CHEBI:63712; EC=5.4.99.57;
CC Evidence={ECO:0000269|PubMed:17705488};
CC -!- SIMILARITY: Belongs to the terpene cyclase/mutase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB10316.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB78579.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z97338; CAB10316.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161541; CAB78579.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE83589.1; -; Genomic_DNA.
DR PIR; B71418; B71418.
DR RefSeq; NP_193272.1; NM_117625.2.
DR AlphaFoldDB; O23390; -.
DR SMR; O23390; -.
DR STRING; 3702.AT4G15370.1; -.
DR PaxDb; O23390; -.
DR PRIDE; O23390; -.
DR ProteomicsDB; 240847; -.
DR EnsemblPlants; AT4G15370.1; AT4G15370.1; AT4G15370.
DR GeneID; 827203; -.
DR Gramene; AT4G15370.1; AT4G15370.1; AT4G15370.
DR KEGG; ath:AT4G15370; -.
DR Araport; AT4G15370; -.
DR TAIR; locus:2130040; AT4G15370.
DR eggNOG; KOG0497; Eukaryota.
DR HOGENOM; CLU_009074_2_0_1; -.
DR InParanoid; O23390; -.
DR OMA; FTHEHRI; -.
DR OrthoDB; 365003at2759; -.
DR PhylomeDB; O23390; -.
DR BioCyc; MetaCyc:AT4G15370-MON; -.
DR PRO; PR:O23390; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O23390; baseline and differential.
DR Genevisible; O23390; AT.
DR GO; GO:0005811; C:lipid droplet; IEA:InterPro.
DR GO; GO:0080011; F:baruol synthase activity; IDA:TAIR.
DR GO; GO:0042300; F:beta-amyrin synthase activity; IBA:GO_Central.
DR GO; GO:0010686; P:tetracyclic triterpenoid biosynthetic process; 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="Baruol synthase"
FT /id="PRO_0000366137"
FT REPEAT 149..190
FT /note="PFTB 1"
FT REPEAT 522..564
FT /note="PFTB 2"
FT REPEAT 641..682
FT /note="PFTB 3"
FT ACT_SITE 493
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P48449"
SQ SEQUENCE 759 AA; 87455 MW; 620E96D9085213C1 CRC64;
MWRLRIGAKA KDNTHLFTTN NYVGRQIWEF DANAGSPEEL AEVEEARRNF SNNRSRFKAS
ADLLWRMQFL REKKFEQKIP RVIVEDAEKI TYEDAKTALR RGLLYFTALQ ADDGHWPAEN
AGSIFFNAPF VICLYITGHL EKIFTHEHRV ELLRYMYNHQ NEDGGWGLHV ESPSNMFCSV
INYICLRILG VEAGHDDKGS ACARARKWIL DHGGATYSPL IGKAWLSVLG VYDWSGCKPI
PPEFWFLPSF FPVNGGTLWI YLRDIFMGLS YLYGKNFVAT STPLILQLRE EIYPEPYTNI
SWRQARNRCA KEDLYYPQSF LQDLFWKGVH VFSENILNRW PFNNLIRQRA LRTTMELVHY
HDEATRYITG GSVPKVIAVF HMLACWVEDP ESDYFKKHLA RVPDFIWIGE DGLKIQSFGS
QVWDTALSLH VFIDGFDDDV DEEIRSTLLK GYDYLEKSQV TENPPGDYMK MFRHMAKGGW
TFSDQDQGWP VSDCTAESLE CCLFFESMSS EFIGKKMDVE KLYDAVDFLL YLQSDNGGIT
AWQPADGKLV EFIEDAVVEH EYVECTGSAI VALAQFNKQF PGYKKEEVER FITKGVKYIE
DLQMVDGSWY GNWGVCFIYG TFFAVRGLVA AGKCYNNCEA IRRAVRFILD TQNTEGGWGE
SYLSCPRKKY IPLIGNKTNV VNTGQALMVL IMGNQMKRDP LPVHRAAKVL INSQMDNGDF
PQQEIMGVFK MNVMLHFPTY RNMFTLWALT HYTKALRGL
