PEN6_ARATH
ID PEN6_ARATH Reviewed; 767 AA.
AC Q9SYN1;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Seco-amyrin synthase;
DE EC=5.4.99.52;
DE EC=5.4.99.54;
DE AltName: Full=Alpha-seco-amyrin synthase;
DE AltName: Full=Beta-seco-amyrin synthase;
DE AltName: Full=Pentacyclic triterpene synthase 6;
DE Short=AtPEN6;
GN Name=PEN6; OrderedLocusNames=At1g78500; ORFNames=T30F21.16;
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=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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=17263431; DOI=10.1021/ja066873w;
RA Shibuya M., Xiang T., Katsube Y., Otsuka M., Zhang H., Ebizuka Y.;
RT "Origin of structural diversity in natural triterpenes: direct synthesis of
RT seco-triterpene skeletons by oxidosqualene cyclase.";
RL J. Am. Chem. Soc. 129:1450-1455(2007).
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.
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).
CC -!- FUNCTION: Multifunctional enzyme that converts oxidosqualene to lupeol,
CC bauerenol, alpha-amyrin, taraxasterol, psi-taraxasterol, multiflorenol,
CC alpha-seco-amyrin and beta-seco-amyrin. {ECO:0000269|PubMed:17263431,
CC ECO:0000269|Ref.5}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-2,3-epoxysqualene = alpha-seco-amyrin;
CC Xref=Rhea:RHEA:31871, ChEBI:CHEBI:15441, ChEBI:CHEBI:63464;
CC EC=5.4.99.52; Evidence={ECO:0000269|PubMed:17263431};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-2,3-epoxysqualene = beta-seco-amyrin;
CC Xref=Rhea:RHEA:31879, ChEBI:CHEBI:15441, ChEBI:CHEBI:63466;
CC EC=5.4.99.54; Evidence={ECO:0000269|PubMed:17263431};
CC -!- SIMILARITY: Belongs to the terpene cyclase/mutase family.
CC {ECO:0000305}.
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DR EMBL; AC007260; AAD30585.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE36113.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60176.1; -; Genomic_DNA.
DR EMBL; AB274959; BAF80447.1; -; mRNA.
DR PIR; E96813; E96813.
DR RefSeq; NP_001322480.1; NM_001334828.1.
DR RefSeq; NP_177971.1; NM_106497.1.
DR AlphaFoldDB; Q9SYN1; -.
DR SMR; Q9SYN1; -.
DR STRING; 3702.AT1G78500.1; -.
DR PaxDb; Q9SYN1; -.
DR PRIDE; Q9SYN1; -.
DR ProteomicsDB; 236408; -.
DR EnsemblPlants; AT1G78500.1; AT1G78500.1; AT1G78500.
DR EnsemblPlants; AT1G78500.2; AT1G78500.2; AT1G78500.
DR GeneID; 844186; -.
DR Gramene; AT1G78500.1; AT1G78500.1; AT1G78500.
DR Gramene; AT1G78500.2; AT1G78500.2; AT1G78500.
DR KEGG; ath:AT1G78500; -.
DR Araport; AT1G78500; -.
DR TAIR; locus:2202950; AT1G78500.
DR eggNOG; KOG0497; Eukaryota.
DR HOGENOM; CLU_009074_2_0_1; -.
DR InParanoid; Q9SYN1; -.
DR OMA; ISADLLW; -.
DR OrthoDB; 365003at2759; -.
DR PhylomeDB; Q9SYN1; -.
DR BioCyc; ARA:AT1G78500-MON; -.
DR PRO; PR:Q9SYN1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SYN1; baseline and differential.
DR Genevisible; Q9SYN1; AT.
DR GO; GO:0005811; C:lipid droplet; IEA:InterPro.
DR GO; GO:0042300; F:beta-amyrin synthase activity; IBA:GO_Central.
DR GO; GO:0042299; F:lupeol synthase activity; TAS:TAIR.
DR GO; GO:0031559; F:oxidosqualene cyclase 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..767
FT /note="Seco-amyrin synthase"
FT /id="PRO_0000366141"
FT REPEAT 149..190
FT /note="PFTB 1"
FT REPEAT 598..638
FT /note="PFTB 2"
FT REPEAT 647..688
FT /note="PFTB 3"
FT ACT_SITE 492
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P48449"
SQ SEQUENCE 767 AA; 88447 MW; A7CBB9FA961A3050 CRC64;
MWRLKIGAKG GDETHLFTTN NYTGRQTWEF DADACSPEEL AEVDEARQNF SINRSRFKIS
ADLLWRMQFL REKKFEQKIP RVEIGDAENI TYKDAKTALR RGILYFKALQ AEDGHWPAEN
SGCLFFEAPF VICLYITGHL EKILTLEHRK ELLRYMYNHQ NEDGGWGIHV EGQSAMFCTV
INYICLRILG VEADLDDIKG SGCARARKWI LDHGGATYTP LIGKAWLSIL GVYDWSGCKP
IPPEVWMLPT FSPFNGGTLW IYFRDIFMGV SYLYGKKFVA TPTPLILQLR EELYPQPYDK
ILWSQARNQC AKEDLYYPQS FLQEMFWKCV HILSENILNR WPCNKLIRQK ALRTTMELLH
YQDEASRYFT GGCVPKPFHM LACWVEDPDG DYFKKHLARV PDYIWIGEDG LKIQSFGSQL
WDTAFSLQVM LAYQDVDDDD DEIRSTLIKG YSFLNKSQLT QNPPGDHRKM LKDIAKGGWT
FSDQDQGWPV SDCTAESLEC CLVFGSMPSE LIGEKMDVER LYDAVNLLLY FQSKNGGITV
WEAARGRTWL EWLSPVEFME DTIVEHEYVE CTGSAIVALA RFLKEFPEHR REEVEKFIKN
AVKYIESFQM PDGSWYGNWG VCFMYGTFFA VRGLVAAGKT YQNCEPIRKA VQFILETQNV
EGGWGESYLS CPNKKYTLLE GNRTNVVNTG QALMVLIMGG QMERDPLPVH RAAKVLINSQ
LDNGDFPQEE IMGVFKMNVM VHYATYRNIF TLWALTYYTK ALRVPLC
