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KSB_ARATH
ID   KSB_ARATH               Reviewed;         785 AA.
AC   Q9SAK2; O64952; Q67ZQ6;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 144.
DE   RecName: Full=Ent-kaur-16-ene synthase, chloroplastic {ECO:0000305};
DE            EC=4.2.3.19 {ECO:0000269|PubMed:17456599, ECO:0000269|PubMed:9536043};
DE   AltName: Full=Ent-kaurene synthase {ECO:0000303|PubMed:17456599};
DE            Short=AtKS {ECO:0000303|PubMed:17456599};
DE   AltName: Full=Ent-kaurene synthase B;
DE            Short=KSB;
DE   AltName: Full=Protein GA REQUIRING 2 {ECO:0000303|PubMed:9536043};
DE   Flags: Precursor;
GN   Name=GA2 {ECO:0000303|PubMed:9536043};
GN   Synonyms=KS {ECO:0000303|PubMed:17456599}, KS1,
GN   TPSGA2 {ECO:0000303|PubMed:12207221};
GN   OrderedLocusNames=At1g79460 {ECO:0000312|Araport:AT1G79460};
GN   ORFNames=T8K14.12 {ECO:0000312|EMBL:AAD30231.1};
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], FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC
RP   ACTIVITY, PATHWAY, AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=9536043; DOI=10.1104/pp.116.4.1271;
RA   Yamaguchi S., Sun T.-P., Kawaide H., Kamiya Y.;
RT   "The GA2 locus of Arabidopsis thaliana encodes ent-kaurene synthase of
RT   gibberellin biosynthesis.";
RL   Plant Physiol. 116:1271-1278(1998).
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 12-785.
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=12207221; DOI=10.1007/s00438-002-0709-y;
RA   Aubourg S., Lecharny A., Bohlmann J.;
RT   "Genomic analysis of the terpenoid synthase (AtTPS) gene family of
RT   Arabidopsis thaliana.";
RL   Mol. Genet. Genomics 267:730-745(2002).
RN   [6]
RP   TISSUE SPECIFICITY.
RX   PubMed=12566586; DOI=10.1105/tpc.007989;
RA   Chen F., Tholl D., D'Auria J.C., Farooq A., Pichersky E., Gershenzon J.;
RT   "Biosynthesis and emission of terpenoid volatiles from Arabidopsis
RT   flowers.";
RL   Plant Cell 15:481-494(2003).
RN   [7]
RP   GENE FAMILY.
RX   PubMed=12777052; DOI=10.1023/a:1023005504702;
RA   Lange B.M., Ghassemian M.;
RT   "Genome organization in Arabidopsis thaliana: a survey for genes involved
RT   in isoprenoid and chlorophyll metabolism.";
RL   Plant Mol. Biol. 51:925-948(2003).
RN   [8]
RP   FUNCTION, MUTAGENESIS OF ILE-638, CATALYTIC ACTIVITY, PATHWAY, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=17456599; DOI=10.1073/pnas.0611454104;
RA   Xu M., Wilderman P.R., Peters R.J.;
RT   "Following evolution's lead to a single residue switch for diterpene
RT   synthase product outcome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:7397-7401(2007).
CC   -!- FUNCTION: Involved in the biosynthesis of ent-kaurene diterpenoids
CC       natural products and in the production of gibberellins phytohormones
CC       (PubMed:17456599, PubMed:9536043). Catalyzes the conversion of ent-
CC       copalyl diphosphate to the gibberellin precursor ent-kaur-16-ene
CC       (PubMed:17456599, PubMed:9536043). {ECO:0000269|PubMed:17456599,
CC       ECO:0000269|PubMed:9536043}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ent-copalyl diphosphate = diphosphate + ent-kaur-16-ene;
CC         Xref=Rhea:RHEA:22220, ChEBI:CHEBI:15415, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:58553; EC=4.2.3.19;
CC         Evidence={ECO:0000269|PubMed:17456599, ECO:0000269|PubMed:9536043};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22221;
CC         Evidence={ECO:0000269|PubMed:17456599, ECO:0000269|PubMed:9536043};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q40577};
CC       Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q40577};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.3 uM for ent-copalyl diphosphate {ECO:0000269|PubMed:17456599};
CC         Note=kcat is 0.06 sec(-1) with ent-copalyl diphosphate as substrate.
CC         {ECO:0000269|PubMed:17456599};
CC   -!- PATHWAY: Plant hormone biosynthesis; gibberellin biosynthesis.
CC       {ECO:0000269|PubMed:17456599, ECO:0000269|PubMed:9536043}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC       {ECO:0000269|PubMed:17456599}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Expressed ubiquitously in roots, stems, leaves,
CC       flowers and siliques. {ECO:0000269|PubMed:12566586,
CC       ECO:0000269|PubMed:9536043}.
CC   -!- DOMAIN: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for
CC       the catalytic activity, presumably through binding to Mg(2+).
CC       {ECO:0000305}.
CC   -!- DISRUPTION PHENOTYPE: Gibberellin-deficient dwarf plants.
CC       {ECO:0000269|PubMed:9536043}.
CC   -!- SIMILARITY: Belongs to the terpene synthase family. Tpse subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AF034774; AAC39443.1; -; mRNA.
DR   EMBL; AC007202; AAD30231.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE36246.1; -; Genomic_DNA.
DR   EMBL; AK176061; BAD43824.1; -; mRNA.
DR   PIR; G96825; G96825.
DR   PIR; T52059; T52059.
DR   RefSeq; NP_178064.1; NM_106594.4.
DR   AlphaFoldDB; Q9SAK2; -.
DR   SMR; Q9SAK2; -.
DR   STRING; 3702.AT1G79460.1; -.
DR   PaxDb; Q9SAK2; -.
DR   PRIDE; Q9SAK2; -.
DR   ProteomicsDB; 250704; -.
DR   EnsemblPlants; AT1G79460.1; AT1G79460.1; AT1G79460.
DR   GeneID; 844284; -.
DR   Gramene; AT1G79460.1; AT1G79460.1; AT1G79460.
DR   KEGG; ath:AT1G79460; -.
DR   Araport; AT1G79460; -.
DR   TAIR; locus:2206390; AT1G79460.
DR   eggNOG; ENOG502QVGX; Eukaryota.
DR   HOGENOM; CLU_003125_2_0_1; -.
DR   InParanoid; Q9SAK2; -.
DR   OMA; HMKHERD; -.
DR   OrthoDB; 318477at2759; -.
DR   PhylomeDB; Q9SAK2; -.
DR   BioCyc; ARA:AT1G79460-MON; -.
DR   BioCyc; MetaCyc:AT1G79460-MON; -.
DR   BRENDA; 4.2.3.19; 399.
DR   UniPathway; UPA00213; -.
DR   UniPathway; UPA00390; -.
DR   PRO; PR:Q9SAK2; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9SAK2; baseline and differential.
DR   Genevisible; Q9SAK2; AT.
DR   GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR   GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
DR   GO; GO:0009899; F:ent-kaurene synthase activity; IDA:TAIR.
DR   GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central.
DR   GO; GO:0010333; F:terpene synthase activity; IBA:GO_Central.
DR   GO; GO:0016102; P:diterpenoid biosynthetic process; IBA:GO_Central.
DR   GO; GO:0009740; P:gibberellic acid mediated signaling pathway; TAS:TAIR.
DR   GO; GO:0009686; P:gibberellin biosynthetic process; IDA:TAIR.
DR   CDD; cd00684; Terpene_cyclase_plant_C1; 1.
DR   Gene3D; 1.10.600.10; -; 1.
DR   Gene3D; 1.50.10.130; -; 1.
DR   InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR   InterPro; IPR044814; Terpene_cyclase_plant_C1.
DR   InterPro; IPR001906; Terpene_synth_N.
DR   InterPro; IPR036965; Terpene_synth_N_sf.
DR   InterPro; IPR005630; Terpene_synthase_metal-bd.
DR   InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR   Pfam; PF01397; Terpene_synth; 1.
DR   Pfam; PF03936; Terpene_synth_C; 1.
DR   SUPFAM; SSF48239; SSF48239; 2.
DR   SUPFAM; SSF48576; SSF48576; 1.
PE   1: Evidence at protein level;
KW   Chloroplast; Lyase; Magnesium; Metal-binding; Plastid; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         1..29
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..785
FT                   /note="Ent-kaur-16-ene synthase, chloroplastic"
FT                   /id="PRO_0000033625"
FT   MOTIF           531..535
FT                   /note="DDXXD motif"
FT                   /evidence="ECO:0000305"
FT   BINDING         531
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         531
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         535
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         535
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         675
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         683
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   MUTAGEN         638
FT                   /note="I->T: Changes catalytic activity. Converts ent-
FT                   copalyl diphosphate to ent-pimara-8(14),15-diene and
FT                   diphosphate."
FT                   /evidence="ECO:0000269|PubMed:17456599"
FT   CONFLICT        21
FT                   /note="R -> G (in Ref. 1; AAC39443)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        781
FT                   /note="E -> K (in Ref. 1; AAC39443)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   785 AA;  89622 MW;  E44C271E9D2BDDD7 CRC64;
     MSINLRSSGC SSPISATLER RLDSEVQTRA NNVSFEQTKE KIRKMLEKVE LSVSAYDTSW
     VAMVPSPSSQ NAPLFPQCVK WLLDNQHEDG SWGLDNHDHQ SLKKDVLSST LASILALKKW
     GIGERQINKG LQFIELNSAL VTDETIQKPT GFDIIFPGMI KYARDLNLTI PLGSEVVDDM
     IRKRDLDLKC DSEKFSKGRE AYLAYVLEGT RNLKDWDLIV KYQRKNGSLF DSPATTAAAF
     TQFGNDGCLR YLCSLLQKFE AAVPSVYPFD QYARLSIIVT LESLGIDRDF KTEIKSILDE
     TYRYWLRGDE EICLDLATCA LAFRLLLAHG YDVSYDPLKP FAEESGFSDT LEGYVKNTFS
     VLELFKAAQS YPHESALKKQ CCWTKQYLEM ELSSWVKTSV RDKYLKKEVE DALAFPSYAS
     LERSDHRRKI LNGSAVENTR VTKTSYRLHN ICTSDILKLA VDDFNFCQSI HREEMERLDR
     WIVENRLQEL KFARQKLAYC YFSGAATLFS PELSDARISW AKGGVLTTVV DDFFDVGGSK
     EELENLIHLV EKWDLNGVPE YSSEHVEIIF SVLRDTILET GDKAFTYQGR NVTHHIVKIW
     LDLLKSMLRE AEWSSDKSTP SLEDYMENAY ISFALGPIVL PATYLIGPPL PEKTVDSHQY
     NQLYKLVSTM GRLLNDIQGF KRESAEGKLN AVSLHMKHER DNRSKEVIIE SMKGLAERKR
     EELHKLVLEE KGSVVPRECK EAFLKMSKVL NLFYRKDDGF TSNDLMSLVK SVIYEPVSLQ
     EESLT
 
 
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