位置:首页 > 蛋白库 > RLC1_CITSI
RLC1_CITSI
ID   RLC1_CITSI              Reviewed;         607 AA.
AC   A0A1C9J6A7;
DT   07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2017, sequence version 2.
DT   03-AUG-2022, entry version 24.
DE   RecName: Full=(R)-limonene synthase 1, chloroplastic {ECO:0000303|PubMed:28272875};
DE            EC=4.2.3.20 {ECO:0000269|PubMed:28272875, ECO:0000269|PubMed:28272876};
DE   AltName: Full=(+)-limonene synthase 1;
DE   Flags: Precursor;
OS   Citrus sinensis (Sweet orange) (Citrus aurantium var. sinensis).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX   NCBI_TaxID=2711 {ECO:0000312|EMBL:AOP12358.2};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF
RP   APOPROTEIN, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF TYR-565.
RC   STRAIN=cv. Washington Navel; TISSUE=Flavedo;
RX   PubMed=28272875; DOI=10.1021/acs.biochem.7b00143;
RA   Morehouse B.R., Kumar R.P., Matos J.O., Olsen S.N., Entova S., Oprian D.D.;
RT   "Functional and Structural Characterization of a (+)-Limonene Synthase from
RT   Citrus sinensis.";
RL   Biochemistry 56:1706-1715(2017).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH MANGANESE AND
RP   SUBSTRATE ANALOGS, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP   SUBSTRATE SPECIFICITY, AND ACTIVITY REGULATION.
RX   PubMed=28272876; DOI=10.1021/acs.biochem.7b00144;
RA   Kumar R.P., Morehouse B.R., Matos J.O., Malik K., Lin H., Krauss I.J.,
RA   Oprian D.D.;
RT   "Structural Characterization of early michaelis complexes in the reaction
RT   catalyzed by (+)-limonene synthase from Citrus sinensis using fluorinated
RT   substrate analogues.";
RL   Biochemistry 56:1716-1725(2017).
CC   -!- FUNCTION: Catalyzes the conversion of geranyl diphosphate to (+)-(4R)-
CC       limonene (PubMed:28272875, PubMed:28272876). Produces exclusively the
CC       (+)-enantiomer (PubMed:28272875). Can use neryl diphosphate as
CC       substrate (PubMed:28272876). Has no activity with farnesyl diphosphate
CC       (PubMed:28272875). {ECO:0000269|PubMed:28272875,
CC       ECO:0000269|PubMed:28272876}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-geranyl diphosphate = (4R)-limonene + diphosphate;
CC         Xref=Rhea:RHEA:10940, ChEBI:CHEBI:15382, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:58057; EC=4.2.3.20;
CC         Evidence={ECO:0000269|PubMed:28272875, ECO:0000269|PubMed:28272876};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:28272875};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000269|PubMed:28272875};
CC       Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit (PubMed:28272876). The
CC       best cofactor is Mn(2+) (PubMed:28272875). No effect with monovalent
CC       cations (PubMed:28272875). {ECO:0000269|PubMed:28272875,
CC       ECO:0000269|PubMed:28272876};
CC   -!- ACTIVITY REGULATION: Inhibited by 2-fluorogeranyl diphosphate (FGPP)
CC       and 2-fluoroneryl diphosphate (FNPP). {ECO:0000269|PubMed:28272876}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=13.1 uM for geranyl diphosphate in presence of manganese
CC         {ECO:0000269|PubMed:28272875};
CC         KM=35 uM for geranyl diphosphate in presence of magnesium
CC         {ECO:0000269|PubMed:28272875};
CC         KM=9 uM for neryl diphosphate {ECO:0000269|PubMed:28272876};
CC         Note=kcat is 0.186 sec(-1) for geranyl diphosphate in presence of
CC         manganese. kcat is 0.118 sec(-1) for geranyl diphosphate in presence
CC         of magnesium. kcat is 0.43 sec(-1) for neryl diphosphate.
CC         {ECO:0000269|PubMed:28272875, ECO:0000269|PubMed:28272876};
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
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   -!- SIMILARITY: Belongs to the terpene synthase family. {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; KU746814; AOP12358.2; -; mRNA.
DR   PDB; 5UV0; X-ray; 2.30 A; A=1-607.
DR   PDB; 5UV1; X-ray; 2.40 A; A=1-607.
DR   PDB; 5UV2; X-ray; 2.20 A; A=1-607.
DR   PDB; 6ONM; X-ray; 2.70 A; A=1-607.
DR   PDBsum; 5UV0; -.
DR   PDBsum; 5UV1; -.
DR   PDBsum; 5UV2; -.
DR   PDBsum; 6ONM; -.
DR   AlphaFoldDB; A0A1C9J6A7; -.
DR   SMR; A0A1C9J6A7; -.
DR   eggNOG; ENOG502QUH3; Eukaryota.
DR   BRENDA; 4.2.3.20; 1426.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0034002; F:(R)-limonene synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
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   3D-structure; Chloroplast; Lyase; Magnesium; Manganese; Metal-binding;
KW   Plastid; Transit peptide.
FT   TRANSIT         1..52
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000305|PubMed:28272875"
FT   CHAIN           53..607
FT                   /note="(R)-limonene synthase 1, chloroplastic"
FT                   /id="PRO_0000440244"
FT   MOTIF           343..347
FT                   /note="DDXXD motif"
FT                   /evidence="ECO:0000305"
FT   BINDING         343
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:28272876"
FT   BINDING         343
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:28272876"
FT   BINDING         343
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:28272876"
FT   BINDING         347
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:28272876"
FT   BINDING         347
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:28272876"
FT   BINDING         347
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:28272876"
FT   BINDING         485
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:28272876"
FT   BINDING         488
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000269|PubMed:28272876"
FT   BINDING         488
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:28272876"
FT   BINDING         504
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:28272876"
FT   MUTAGEN         565
FT                   /note="Y->F: 50-fold decreased catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:28272875"
FT   HELIX           65..70
FT                   /evidence="ECO:0007829|PDB:5UV2"
FT   HELIX           74..76
FT                   /evidence="ECO:0007829|PDB:5UV2"
FT   HELIX           78..96
FT                   /evidence="ECO:0007829|PDB:5UV2"
FT   HELIX           101..113
FT                   /evidence="ECO:0007829|PDB:5UV2"
FT   HELIX           117..119
FT                   /evidence="ECO:0007829|PDB:5UV2"
FT   HELIX           121..134
FT                   /evidence="ECO:0007829|PDB:5UV2"
FT   TURN            138..140
FT                   /evidence="ECO:0007829|PDB:5UV1"
FT   HELIX           145..157
FT                   /evidence="ECO:0007829|PDB:5UV2"
FT   HELIX           164..170
FT                   /evidence="ECO:0007829|PDB:5UV2"
FT   TURN            173..175
FT                   /evidence="ECO:0007829|PDB:5UV2"
FT   HELIX           182..192
FT                   /evidence="ECO:0007829|PDB:5UV2"
FT   HELIX           200..215
FT                   /evidence="ECO:0007829|PDB:5UV2"
FT   HELIX           227..238
FT                   /evidence="ECO:0007829|PDB:5UV2"
FT   HELIX           241..243
FT                   /evidence="ECO:0007829|PDB:5UV2"
FT   HELIX           247..249
FT                   /evidence="ECO:0007829|PDB:5UV2"
FT   HELIX           250..258
FT                   /evidence="ECO:0007829|PDB:5UV2"
FT   HELIX           265..296
FT                   /evidence="ECO:0007829|PDB:5UV2"
FT   HELIX           298..301
FT                   /evidence="ECO:0007829|PDB:5UV2"
FT   HELIX           309..319
FT                   /evidence="ECO:0007829|PDB:5UV2"
FT   HELIX           323..325
FT                   /evidence="ECO:0007829|PDB:5UV2"
FT   HELIX           326..347
FT                   /evidence="ECO:0007829|PDB:5UV2"
FT   HELIX           352..364
FT                   /evidence="ECO:0007829|PDB:5UV2"
FT   HELIX           367..373
FT                   /evidence="ECO:0007829|PDB:5UV2"
FT   HELIX           376..400
FT                   /evidence="ECO:0007829|PDB:5UV2"
FT   HELIX           405..427
FT                   /evidence="ECO:0007829|PDB:5UV2"
FT   HELIX           434..444
FT                   /evidence="ECO:0007829|PDB:5UV2"
FT   HELIX           447..458
FT                   /evidence="ECO:0007829|PDB:5UV2"
FT   HELIX           464..471
FT                   /evidence="ECO:0007829|PDB:5UV2"
FT   HELIX           475..490
FT                   /evidence="ECO:0007829|PDB:5UV2"
FT   HELIX           494..499
FT                   /evidence="ECO:0007829|PDB:5UV2"
FT   HELIX           505..513
FT                   /evidence="ECO:0007829|PDB:5UV2"
FT   HELIX           517..540
FT                   /evidence="ECO:0007829|PDB:5UV2"
FT   STRAND          544..546
FT                   /evidence="ECO:0007829|PDB:5UV2"
FT   HELIX           548..566
FT                   /evidence="ECO:0007829|PDB:5UV2"
FT   STRAND          567..570
FT                   /evidence="ECO:0007829|PDB:5UV0"
FT   HELIX           581..586
FT                   /evidence="ECO:0007829|PDB:5UV2"
SQ   SEQUENCE   607 AA;  70354 MW;  F1A481732DDE2B95 CRC64;
     MSSCINPSTL ATSVNGFKCL PLATNRAAIR IMAKNKPVQC LVSTKYDNLT VDRRSANYQP
     SIWDHDFLQS LNSNYTDETY KRRAEELKGK VKTAIKDVTE PLDQLELIDN LQRLGLAYHF
     EPEIRNILRN IHNHNKDYNW RKENLYATSL EFRLLRQHGY PVSQEVFSGF KDDKVGFICD
     DFKGILSLHE ASYYSLEGES IMEEAWQFTS KHLKEMMITS NSKEEDVFVA EQAKRALELP
     LHWKAPMLEA RWFIHVYEKR EDKNHLLLEL AKLEFNTLQA IYQEELKDIS GWWKDTGLGE
     KLSFARNRLV ASFLWSMGIA FEPQFAYCRR VLTISIALIT VIDDIYDVYG TLDELEIFTD
     AVARWDINYA LKHLPGYMKM CFLALYNFVN EFAYYVLKQQ DFDMLLSIKH AWLGLIQAYL
     VEAKWYHSKY TPKLEEYLEN GLVSITGPLI ITISYLSGTN PIIKKELEFL ESNPDIVHWS
     SKIFRLQDDL GTSSDEIQRG DVPKSIQCYM HETGASEEVA REHIKDMMRQ MWKKVNAYTA
     DKDSPLTRTT AEFLLNLVRM SHFMYLHGDG HGVQNQETID VGFTLLFQPI PLEDKDMAFT
     ASPGTKG
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024