CPT1_SOLLC
ID CPT1_SOLLC Reviewed; 303 AA.
AC C1K5M2; R9R6P8;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=Dimethylallylcistransferase CPT1, chloroplastic {ECO:0000305};
DE EC=2.5.1.28 {ECO:0000269|PubMed:19487664, ECO:0000269|PubMed:23134568, ECO:0000269|PubMed:23757397};
DE AltName: Full=Cis-prenyltransferase 1 {ECO:0000303|PubMed:23134568};
DE Short=SlCPT1 {ECO:0000303|PubMed:23134568};
DE AltName: Full=Neryl-diphosphate synthase 1 {ECO:0000303|PubMed:19487664};
DE Flags: Precursor;
GN Name=CPT1 {ECO:0000303|PubMed:23134568};
GN Synonyms=NDPS1 {ECO:0000303|PubMed:19487664};
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, TISSUE SPECIFICITY, AND FUNCTION.
RC TISSUE=Trichome gland;
RX PubMed=19487664; DOI=10.1073/pnas.0904113106;
RA Schilmiller A.L., Schauvinhold I., Larson M., Xu R., Charbonneau A.L.,
RA Schmidt A., Wilkerson C., Last R.L., Pichersky E.;
RT "Monoterpenes in the glandular trichomes of tomato are synthesized from a
RT neryl diphosphate precursor rather than geranyl diphosphate.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:10865-10870(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=23757397; DOI=10.1105/tpc.113.111013;
RA Matsuba Y., Nguyen T.T., Wiegert K., Falara V., Gonzales-Vigil E.,
RA Leong B., Schafer P., Kudrna D., Wing R.A., Bolger A.M., Usadel B.,
RA Tissier A., Fernie A.R., Barry C.S., Pichersky E.;
RT "Evolution of a complex locus for terpene biosynthesis in Solanum.";
RL Plant Cell 25:2022-2036(2013).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=23134568; DOI=10.1111/tpj.12063;
RA Akhtar T.A., Matsuba Y., Schauvinhold I., Yu G., Lees H.A., Klein S.E.,
RA Pichersky E.;
RT "The tomato cis-prenyltransferase gene family.";
RL Plant J. 73:640-652(2013).
CC -!- FUNCTION: Uses dimethylallyl diphosphate and isopentenyl diphosphate to
CC catalyze the cis-prenyl chain elongation and produce the 10 carbon
CC product neryl diphosphate. {ECO:0000269|PubMed:19487664,
CC ECO:0000269|PubMed:23134568, ECO:0000269|PubMed:23757397}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dimethylallyl diphosphate + isopentenyl diphosphate =
CC diphosphate + neryl diphosphate; Xref=Rhea:RHEA:11328,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:57665,
CC ChEBI:CHEBI:128769; EC=2.5.1.28;
CC Evidence={ECO:0000269|PubMed:19487664, ECO:0000269|PubMed:23134568,
CC ECO:0000269|PubMed:23757397};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11329;
CC Evidence={ECO:0000269|PubMed:19487664, ECO:0000269|PubMed:23134568,
CC ECO:0000269|PubMed:23757397};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:23134568};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=152 uM for isopentenyl diphosphate {ECO:0000269|PubMed:19487664};
CC KM=177 uM for dimethylallyl diphosphate
CC {ECO:0000269|PubMed:19487664};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:23134568}.
CC -!- TISSUE SPECIFICITY: Expressed in leaf trichomes and stem trichomes.
CC {ECO:0000269|PubMed:19487664, ECO:0000269|PubMed:23134568}.
CC -!- SIMILARITY: Belongs to the UPP synthetase family. {ECO:0000305}.
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DR EMBL; FJ797956; ACO56895.1; -; mRNA.
DR EMBL; KC807995; AGK82810.1; -; Genomic_DNA.
DR RefSeq; NP_001234633.1; NM_001247704.1.
DR AlphaFoldDB; C1K5M2; -.
DR SMR; C1K5M2; -.
DR STRING; 4081.Solyc08g005680.2.1; -.
DR PaxDb; C1K5M2; -.
DR PRIDE; C1K5M2; -.
DR EnsemblPlants; Solyc08g005680.3.1; Solyc08g005680.3.1; Solyc08g005680.3.
DR GeneID; 100316884; -.
DR Gramene; Solyc08g005680.3.1; Solyc08g005680.3.1; Solyc08g005680.3.
DR KEGG; sly:100316884; -.
DR eggNOG; KOG1602; Eukaryota.
DR InParanoid; C1K5M2; -.
DR OMA; RRWAQKR; -.
DR OrthoDB; 1362420at2759; -.
DR BioCyc; MetaCyc:MON-15449; -.
DR BRENDA; 2.5.1.28; 3101.
DR Proteomes; UP000004994; Chromosome 8.
DR GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR GO; GO:0009570; C:chloroplast stroma; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0045547; F:dehydrodolichyl diphosphate synthase activity; IBA:GO_Central.
DR GO; GO:0047863; F:dimethylallylcistransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0002094; F:polyprenyltransferase activity; IBA:GO_Central.
DR GO; GO:0004659; F:prenyltransferase activity; IDA:UniProtKB.
DR GO; GO:0009668; P:plastid membrane organization; IBA:GO_Central.
DR GO; GO:0016094; P:polyprenol biosynthetic process; IBA:GO_Central.
DR GO; GO:0009409; P:response to cold; IBA:GO_Central.
DR CDD; cd00475; Cis_IPPS; 1.
DR Gene3D; 3.40.1180.10; -; 1.
DR HAMAP; MF_01139; ISPT; 1.
DR InterPro; IPR001441; UPP_synth-like.
DR InterPro; IPR018520; UPP_synth-like_CS.
DR InterPro; IPR036424; UPP_synth-like_sf.
DR PANTHER; PTHR10291; PTHR10291; 1.
DR Pfam; PF01255; Prenyltransf; 1.
DR SUPFAM; SSF64005; SSF64005; 1.
DR TIGRFAMs; TIGR00055; uppS; 1.
DR PROSITE; PS01066; UPP_SYNTHASE; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Magnesium; Metal-binding; Plastid; Reference proteome;
KW Transferase; Transit peptide.
FT TRANSIT 1..54
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 55..303
FT /note="Dimethylallylcistransferase CPT1, chloroplastic"
FT /id="PRO_0000405120"
FT ACT_SITE 86
FT /evidence="ECO:0000250|UniProtKB:P60472"
SQ SEQUENCE 303 AA; 34601 MW; 007D02C424C86A2A CRC64;
MSSLVLQCWK LSSPSLILQQ NTSISMGAFK GIHKLQIPNS PLTVSARGLN KISCSLNLQT
EKLCYEDNDN DLDEELMPKH IALIMDGNRR WAKDKGLEVY EGHKHIIPKL KEICDISSKL
GIQIITAFAF STENWKRSKE EVDFLLQMFE EIYDEFSRSG VRVSIIGCKS DLPMTLQKCI
ALTEETTKGN KGLHLVIALN YGGYYDILQA TKSIVNKAMN GLLDVEDINK NLFDQELESK
CPNPDLLIRT GGEQRVSNFL LWQLAYTEFY FTNTLFPDFG EEDLKEAIMN FQQRHRRFGG
HTY
