TPS1_RICCO
ID TPS1_RICCO Reviewed; 558 AA.
AC B9S9Z3;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Alpha-copaene synthase;
DE EC=4.2.3.133;
DE AltName: Full=(+)-delta-cadinene synthase;
DE EC=4.2.3.13;
DE AltName: Full=Terpene synthase 1;
DE Short=RcSeTPS1;
GN Name=TPS1; ORFNames=RCOM_0179780;
OS Ricinus communis (Castor bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC Ricinus.
OX NCBI_TaxID=3988;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=22459969; DOI=10.1016/j.phytochem.2012.02.022;
RA Xie X., Kirby J., Keasling J.D.;
RT "Functional characterization of four sesquiterpene synthases from Ricinus
RT communis (castor bean).";
RL Phytochemistry 78:20-28(2012).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Hale;
RX PubMed=20729833; DOI=10.1038/nbt.1674;
RA Chan A.P., Crabtree J., Zhao Q., Lorenzi H., Orvis J., Puiu D.,
RA Melake-Berhan A., Jones K.M., Redman J., Chen G., Cahoon E.B., Gedil M.,
RA Stanke M., Haas B.J., Wortman J.R., Fraser-Liggett C.M., Ravel J.,
RA Rabinowicz P.D.;
RT "Draft genome sequence of the oilseed species Ricinus communis.";
RL Nat. Biotechnol. 28:951-956(2010).
CC -!- FUNCTION: Catalyzes the cyclization of farnesyl diphosphate to alpha-
CC copaene and (+)-delta cadinene. {ECO:0000269|PubMed:22459969}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = (1S,8aR)-delta-cadinene +
CC diphosphate; Xref=Rhea:RHEA:19525, ChEBI:CHEBI:15385,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:175763; EC=4.2.3.13;
CC Evidence={ECO:0000269|PubMed:22459969};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = alpha-copaene + diphosphate;
CC Xref=Rhea:RHEA:33991, ChEBI:CHEBI:10221, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:175763; EC=4.2.3.133;
CC Evidence={ECO:0000269|PubMed:22459969};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250};
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:0000250}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR EMBL; JN315864; AEQ27766.1; -; mRNA.
DR EMBL; EQ973900; EEF39510.1; -; Genomic_DNA.
DR RefSeq; NP_001310685.1; NM_001323756.1.
DR AlphaFoldDB; B9S9Z3; -.
DR SMR; B9S9Z3; -.
DR STRING; 3988.XP_002522812.1; -.
DR PRIDE; B9S9Z3; -.
DR GeneID; 8280754; -.
DR KEGG; rcu:8280754; -.
DR eggNOG; ENOG502QUCN; Eukaryota.
DR InParanoid; B9S9Z3; -.
DR OrthoDB; 360509at2759; -.
DR BRENDA; 4.2.3.13; 1204.
DR BRENDA; 4.2.3.133; 1204.
DR Proteomes; UP000008311; Unassembled WGS sequence.
DR GO; GO:0047461; F:(+)-delta-cadinene synthase activity; IDA:UniProtKB.
DR GO; GO:0102877; F:alpha-copaene synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:1901928; P:cadinene biosynthetic process; IDA:UniProtKB.
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 Lyase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..558
FT /note="Alpha-copaene synthase"
FT /id="PRO_0000422199"
FT MOTIF 310..314
FT /note="DDXXD motif"
FT BINDING 310
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 310
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 314
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 314
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 464
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
SQ SEQUENCE 558 AA; 64392 MW; 42DD0E888BB5FF6E CRC64;
MSLQVSAVPI KTSTQNATSA VKRHSSTYHP TIWGDHFLAN LSHSKIIDGS IEQQFEGLKQ
KVRKMIIDLN NEPCKKLGLI DAVQRLGVGY HFKSEIEDVL QKVYHDYSDD EDDLNTVALR
FRLLRQHGIK VSCAIFEKFK DSEGNFKTSL INDALGMLSL YEATHLSIRG EDVLDEALAF
TTTNLQSVLP QLNTHLAAQI SRALNRPIRK YLPRLEARNY IDIYATEESY NTTLLNFAKL
DFNMLQELHQ KELNVVTKWW KSLDVATKLP YARDRVVECY FWMVGVYFEP QYSFARIMMT
KIIAITSLLD DTYDNYATGE ELEILTEAIE RWDIKAKDAL PEYMKIIYTT LLDIYNEYEE
NIAKEEKSLL YSVYYAKEVM KRVVRAYLAE VRWRDNCYTP TMEEYMQSAL LTTCSPMLAI
ASFLGLKEIA TKEAYEWASE DPKIIRASSI VCRLMDDIVS HEFEQTRKHV ASGVECYIKQ
YGASEEEVIK LFRKEVTNAW KDLNEECLNP TPVPMPMLER VVNLTRAIDV IYKDDDGYTN
SHIMKDYVAS VLKDPVPV
