TPS1_CITSI
ID TPS1_CITSI Reviewed; 548 AA.
AC D0UZK2; A0A067E424; Q71MJ3;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2009, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Terpene synthase 1 {ECO:0000303|PubMed:14617067, ECO:0000303|Ref.2};
DE Short=CsTPS1 {ECO:0000303|PubMed:14617067, ECO:0000303|PubMed:23072391};
DE AltName: Full=Valencene synthase TPS1 {ECO:0000303|PubMed:14617067, ECO:0000303|PubMed:21818683, ECO:0000303|PubMed:23072391};
DE Short=CsVS {ECO:0000303|PubMed:23072391};
DE EC=4.2.3.73 {ECO:0000269|PubMed:14617067, ECO:0000269|PubMed:21818683};
GN Name=TPS1 {ECO:0000303|PubMed:14617067, ECO:0000303|Ref.2};
GN Synonyms=CSVS {ECO:0000303|PubMed:23072391};
GN ORFNames=CISIN_1g045533mg {ECO:0000312|EMBL:KDO49808.1};
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY,
RP DEVELOPMENTAL STAGE, AND INDUCTION BY ETHYLENE.
RC STRAIN=cv. Valencia;
RX PubMed=14617067; DOI=10.1046/j.1365-313x.2003.01910.x;
RA Sharon-Asa L., Shalit M., Frydman A., Bar E., Holland D., Or E., Lavi U.,
RA Lewinsohn E., Eyal Y.;
RT "Citrus fruit flavor and aroma biosynthesis: isolation, functional
RT characterization, and developmental regulation of Cstps1, a key gene in the
RT production of the sesquiterpene aroma compound valencene.";
RL Plant J. 36:664-674(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Liu C.H., Deng X.X., Ye J.L., Xu J.;
RT "Isolation of the genes-encoding 1,2 rhamnosyltransferase and valencene
RT synthase from Citrus grandis and C. sinensis.";
RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG International Citrus Genome Consortium;
RA Gmitter F., Chen C., Farmerie W., Harkins T., Desany B., Mohiuddin M.,
RA Kodira C., Borodovsky M., Lomsadze A., Burns P., Jenkins J., Prochnik S.,
RA Shu S., Chapman J., Pitluck S., Schmutz J., Rokhsar D.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND GENE FAMILY.
RX PubMed=21818683; DOI=10.1007/s11103-011-9813-x;
RA Bleeker P.M., Spyropoulou E.A., Diergaarde P.J., Volpin H., De Both M.T.J.,
RA Zerbe P., Bohlmann J., Falara V., Matsuba Y., Pichersky E., Haring M.A.,
RA Schuurink R.C.;
RT "RNA-seq discovery, functional characterization, and comparison of
RT sesquiterpene synthases from Solanum lycopersicum and Solanum habrochaites
RT trichomes.";
RL Plant Mol. Biol. 77:323-336(2011).
RN [5]
RP GENE FAMILY.
RX PubMed=23072391; DOI=10.2174/138920112804724864;
RA Hsu C.-Y., Huang P.-L., Chen C.-M., Mao C.-T., Chaw S.-M.;
RT "Tangy scent in Toona sinensis (Meliaceae) leaflets: isolation, functional
RT characterization, and regulation of TsTPS1 and TsTPS2, two key terpene
RT synthase genes in the biosynthesis of the scent compound.";
RL Curr. Pharm. Biotechnol. 13:2721-2732(2012).
CC -!- FUNCTION: Sesquiterpene synthase involved in the biosynthesis of
CC volatile compounds which contribute to fruit flavor and aroma
CC (PubMed:21818683, PubMed:14617067). Mediates the conversion of (2E,6E)-
CC farnesyl diphosphate (FPP) into (+)-valencene (PubMed:21818683,
CC PubMed:14617067). No activity detected with geranyl diphosphate (GPP)
CC (PubMed:14617067). {ECO:0000269|PubMed:14617067,
CC ECO:0000269|PubMed:21818683}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = (+)-valencene + diphosphate;
CC Xref=Rhea:RHEA:29511, ChEBI:CHEBI:33019, ChEBI:CHEBI:61700,
CC ChEBI:CHEBI:175763; EC=4.2.3.73;
CC Evidence={ECO:0000269|PubMed:14617067, ECO:0000269|PubMed:21818683};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29512;
CC Evidence={ECO:0000269|PubMed:14617067, ECO:0000269|PubMed:21818683};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7};
CC Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit.
CC {ECO:0000250|UniProtKB:A0A1C9J6A7};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000269|PubMed:14617067}.
CC -!- DEVELOPMENTAL STAGE: Accumulates during fruit maturation and ripening.
CC {ECO:0000269|PubMed:14617067}.
CC -!- INDUCTION: Induced by ethylene. {ECO:0000269|PubMed:14617067}.
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|UniProtKB:Q40577}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. Tpsa subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=KDO49808.1; Type=Erroneous gene model prediction; Evidence={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; AF441124; AAQ04608.1; -; mRNA.
DR EMBL; GQ988384; ACX70155.1; -; mRNA.
DR EMBL; KK785100; KDO49808.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; NP_001275785.1; NM_001288856.1.
DR SMR; D0UZK2; -.
DR STRING; 2711.XP_006477783.1; -.
DR GeneID; 102577959; -.
DR KEGG; cit:102577959; -.
DR eggNOG; ENOG502QUCN; Eukaryota.
DR OrthoDB; 360509at2759; -.
DR BioCyc; MetaCyc:MON-14951; -.
DR BRENDA; 4.2.3.128; 1426.
DR BRENDA; 4.2.3.133; 1426.
DR BRENDA; 4.2.3.73; 1426.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000027120; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0010333; F:terpene synthase activity; IEA:InterPro.
DR GO; GO:0102905; F:valencene synthase activity; IDA:UniProtKB.
DR GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR GO; GO:0009835; P:fruit ripening; IEP:UniProtKB.
DR GO; GO:0009723; P:response to ethylene; IEP:UniProtKB.
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..548
FT /note="Terpene synthase 1"
FT /id="PRO_0000454681"
FT MOTIF 301..305
FT /note="DDXXD motif"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 301
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 301
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 305
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 305
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 445
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 453
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT CONFLICT 83
FT /note="E -> G (in Ref. 1; AAQ04608)"
FT /evidence="ECO:0000305"
FT CONFLICT 221
FT /note="Y -> C (in Ref. 1; AAQ04608)"
FT /evidence="ECO:0000305"
FT CONFLICT 221
FT /note="Y -> H (in Ref. 3; KDO49808)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 548 AA; 63677 MW; BC2105AF8C3BB17C CRC64;
MSSGETFRPT ADFHPSLWRN HFLKGASDFK TVDHTATQER HEALKEEVRR MITDAEDKPV
QKLRLIDEVQ RLGVAYHFEK EIEDAIQKLC PIYIDSNRAD LHTVSLHFRL LRQQGIKISC
DVFEKFKDDE GRFKSSLIND VQGMLSLYEA AYMAVRGEHI LDEAIAFTTT HLKSLVAQDH
VTPKLAEQIN HALYRPLRKT LPRLEARYFM SMINSTSDHL YNKTLLNFAK LDFNILLELH
KEELNELTKW WKDLDFTTKL PYARDRLVEL YFWDLGTYFE PQYAFGRKIM TQLNYILSII
DDTYDAYGTL EELSLFTEAV QRWNIEAVDM LPEYMKLIYR TLLDAFNEIE EDMAKQGRSH
CVRYAKEENQ KVIGAYSVQA KWFSEGYVPT IEEYMPIALT SCAYTFVITN SFLGMGDFAT
KEVFEWISNN PKVVKAASVI CRLMDDMQGH EFEQKRGHVA SAIECYTKQH GVSKEEAIKM
FEEEVANAWK DINEELMMKP TVVARPLLGT ILNLARAIDF IYKEDDGYTH SYLIKDQIAS
VLGDHVPF