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MYRS2_ARATH
ID   MYRS2_ARATH             Reviewed;         598 AA.
AC   Q9LRZ6; B7ZWS1; Q84UV1;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=Beta-myrcene/(E)-beta-ocimene synthase 2, chloroplastic;
DE            EC=4.2.3.15 {ECO:0000269|PubMed:12566586};
DE   AltName: Full=Terpenoid synthase 24;
DE            Short=AtTPS24;
DE   Flags: Precursor;
GN   Name=TPS24; OrderedLocusNames=At3g25810; ORFNames=K13N2.7;
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, BIOPHYSICOCHEMICAL PROPERTIES,
RP   CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Landsberg erecta;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA   Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT   features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT   clones.";
RL   DNA Res. 7:131-135(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].
RC   STRAIN=cv. Columbia;
RA   De Los Reyes C., Quan R., Chen H., Bautista V.R., Kim C.J., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (JAN-2009) 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   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).
CC   -!- FUNCTION: Involved in monoterpene (C10) biosynthesis. The major
CC       products are alpha- and beta-pinene, sabinene, beta-myrcene, (E)-beta-
CC       ocimene and limonene. {ECO:0000269|PubMed:12566586}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-geranyl diphosphate = beta-myrcene + diphosphate;
CC         Xref=Rhea:RHEA:16965, ChEBI:CHEBI:17221, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:58057; EC=4.2.3.15;
CC         Evidence={ECO:0000269|PubMed:12566586};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         Vmax=1.7 pmol/sec/mg enzyme toward geranyl diphosphate
CC         {ECO:0000269|PubMed:12566586};
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC       {ECO:0000305|PubMed:12566586}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed exclusively in mature flowers, but not in
CC       inmmature buds. {ECO:0000269|PubMed:12566586}.
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   -!- SIMILARITY: Belongs to the terpene synthase family. Tpsb subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AF497484; AAO85532.1; -; mRNA.
DR   EMBL; AB028607; BAA95770.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE77072.1; -; Genomic_DNA.
DR   EMBL; BT053763; ACL13990.1; -; mRNA.
DR   RefSeq; NP_189209.2; NM_113482.5.
DR   AlphaFoldDB; Q9LRZ6; -.
DR   SMR; Q9LRZ6; -.
DR   BioGRID; 7504; 1.
DR   IntAct; Q9LRZ6; 1.
DR   STRING; 3702.AT3G25810.1; -.
DR   PaxDb; Q9LRZ6; -.
DR   PRIDE; Q9LRZ6; -.
DR   ProteomicsDB; 251358; -.
DR   EnsemblPlants; AT3G25810.1; AT3G25810.1; AT3G25810.
DR   GeneID; 822173; -.
DR   Gramene; AT3G25810.1; AT3G25810.1; AT3G25810.
DR   KEGG; ath:AT3G25810; -.
DR   Araport; AT3G25810; -.
DR   TAIR; locus:2086004; AT3G25810.
DR   eggNOG; ENOG502QUH3; Eukaryota.
DR   HOGENOM; CLU_003125_7_1_1; -.
DR   InParanoid; Q9LRZ6; -.
DR   OMA; TMLIHFY; -.
DR   OrthoDB; 401091at2759; -.
DR   PhylomeDB; Q9LRZ6; -.
DR   BioCyc; ARA:AT3G25810-MON; -.
DR   BioCyc; MetaCyc:AT3G25810-MON; -.
DR   UniPathway; UPA00213; -.
DR   PRO; PR:Q9LRZ6; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9LRZ6; baseline and differential.
DR   Genevisible; Q9LRZ6; AT.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0050552; F:(4S)-limonene synthase activity; IDA:TAIR.
DR   GO; GO:0034768; F:(E)-beta-ocimene synthase activity; IDA:TAIR.
DR   GO; GO:0034002; F:(R)-limonene synthase activity; IDA:TAIR.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0050551; F:myrcene synthase activity; IDA:TAIR.
DR   GO; GO:0050550; F:pinene synthase activity; IDA:TAIR.
DR   GO; GO:0080015; F:sabinene synthase activity; IDA:TAIR.
DR   GO; GO:0010334; F:sesquiterpene synthase activity; IDA:TAIR.
DR   GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR   GO; GO:0043693; P:monoterpene 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; IPR034741; Terpene_cyclase-like_1_C.
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   SFLD; SFLDG01019; Terpene_Cyclase_Like_1_C_Termi; 1.
DR   SUPFAM; SSF48239; SSF48239; 1.
DR   SUPFAM; SSF48576; SSF48576; 1.
PE   1: Evidence at protein level;
KW   Chloroplast; Lyase; Magnesium; Manganese; Metal-binding; Plastid;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         1..30
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..598
FT                   /note="Beta-myrcene/(E)-beta-ocimene synthase 2,
FT                   chloroplastic"
FT                   /id="PRO_0000348418"
FT   MOTIF           344..348
FT                   /note="DDXXD motif"
FT   BINDING         344
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         344
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         348
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         348
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         489
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         493
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         497
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        32
FT                   /note="S -> A (in Ref. 2; AAO85532)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        37
FT                   /note="M -> I (in Ref. 2; AAO85532)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        41
FT                   /note="N -> Y (in Ref. 2; AAO85532)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        65
FT                   /note="I -> T (in Ref. 2; AAO85532)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        460
FT                   /note="G -> D (in Ref. 2; AAO85532)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        543
FT                   /note="A -> V (in Ref. 2; AAO85532)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        546
FT                   /note="S -> I (in Ref. 2; AAO85532)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        553
FT                   /note="R -> G (in Ref. 2; AAO85532)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   598 AA;  69812 MW;  8BC02555898C5C60 CRC64;
     MATLCIGSAP IYQNACIHNF RLQRPRRFIS KSMTKTMPDA NPLDLRRRSG NYQPSSWDHS
     YLLSIENKYV NEKEVITRHV LKKKVKKMLE EVETKSRLEK LELIDDLQKL GVSYHFEQEI
     NNILTNFHLE NGKNIWKCDK EEDLHATALE FRLLRQHGFG VSEDIFDVII DKIESNTFKS
     DNITSIITLY EASYLSTKSD TKLHKVIRPF ATEQIRNFVD DESETYNIML REMAIHALEI
     PYHWRMRRLE TRWYIDAYEK KHDMNLFLAE FAKIDFNIVQ TAHQEDVKYV SCWWKETGLG
     SQLHFVRDRI VENYFWTVGM IYEPQFGYIR RIVAIVAALI TVIDDIYDIY GTPEELELFT
     AMVQNWDINR LDELPEYMKL CFLTLFNEIN AMGCDVLKCK NIDVIPYFKK SWADLCKAYL
     VEAKWYKGGY KPSVEEYMQN AWISISAPTM LIHFYCAFSG QISVQILESL VQQQQDVVRC
     SATVLRLAND LATSPDELAR GDVLKSVQCY MHETGVSEEE ARTHVQQMIS HTWDEMNYEA
     RTAARSSSLL SRRFVETAMN LARMSQCMYQ HGDGHGCPDK AKIVDRVQTL LVDPIPLD
 
 
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