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CPT6_SOLLC
ID   CPT6_SOLLC              Reviewed;         285 AA.
AC   K7W9N9; A0A3Q7GTN3;
DT   07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT   07-OCT-2020, sequence version 2.
DT   03-AUG-2022, entry version 32.
DE   RecName: Full=(2Z,6Z)-farnesyl diphosphate synthase CPT6, chloroplastic {ECO:0000305};
DE            EC=2.5.1.92 {ECO:0000305};
DE   AltName: Full=Cis-prenyltransferase 6 {ECO:0000303|PubMed:23134568};
DE            Short=SlCPT6 {ECO:0000303|PubMed:23134568};
DE   Flags: Precursor;
GN   Name=CPT6 {ECO:0000303|PubMed:23134568};
GN   OrderedLocusNames=Solyc06g059990 {ECO:0000305};
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 [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP   SUBCELLULAR LOCATION, AND TISSUE 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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Heinz 1706;
RX   PubMed=22660326; DOI=10.1038/nature11119;
RG   Tomato Genome Consortium;
RT   "The tomato genome sequence provides insights into fleshy fruit
RT   evolution.";
RL   Nature 485:635-641(2012).
CC   -!- FUNCTION: Uses neryl diphosphate to catalyze the cis-prenyl chain
CC       elongation and produce the 15 carbon product (2Z,6Z)-farnesyl
CC       diphosphate. {ECO:0000269|PubMed:23134568}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dimethylallyl diphosphate + 2 isopentenyl diphosphate =
CC         (2Z,6Z)-farnesyl diphosphate + 2 diphosphate; Xref=Rhea:RHEA:27810,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:60374,
CC         ChEBI:CHEBI:128769; EC=2.5.1.92;
CC         Evidence={ECO:0000269|PubMed:23134568};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27811;
CC         Evidence={ECO:0000269|PubMed:23134568};
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; Evidence={ECO:0000269|PubMed:23134568};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11329;
CC         Evidence={ECO:0000269|PubMed:23134568};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=isopentenyl diphosphate + neryl diphosphate = (2Z,6Z)-farnesyl
CC         diphosphate + diphosphate; Xref=Rhea:RHEA:64572, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57665, ChEBI:CHEBI:60374, ChEBI:CHEBI:128769;
CC         Evidence={ECO:0000269|PubMed:23134568};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64573;
CC         Evidence={ECO:0000269|PubMed:23134568};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:23134568};
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC       {ECO:0000269|PubMed:23134568}. Note=Localizes in punctuate patterns
CC       inside the chloroplasts. {ECO:0000269|PubMed:23134568}.
CC   -!- TISSUE SPECIFICITY: Expressed in roots and red fruits.
CC       {ECO:0000269|PubMed:23134568}.
CC   -!- SIMILARITY: Belongs to the UPP synthase family. {ECO:0000305}.
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DR   EMBL; JX943888; AFW98430.1; -; Genomic_DNA.
DR   EMBL; CM001069; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; K7W9N9; -.
DR   SMR; K7W9N9; -.
DR   STRING; 4081.Solyc06g059990.2.1; -.
DR   BRENDA; 2.5.1.92; 3101.
DR   Proteomes; UP000004994; Chromosome 6.
DR   ExpressionAtlas; K7W9N9; baseline.
DR   GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR   GO; GO:0102059; F:2-cis,6-cis-farnesyl pyrophosphate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0047863; F:dimethylallylcistransferase activity; IEA:RHEA.
DR   GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR   GO; GO:0004659; F:prenyltransferase activity; IDA:UniProtKB.
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..30
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..285
FT                   /note="(2Z,6Z)-farnesyl diphosphate synthase CPT6,
FT                   chloroplastic"
FT                   /id="PRO_0000450937"
FT   ACT_SITE        65
FT                   /evidence="ECO:0000250|UniProtKB:P60472"
FT   CONFLICT        118
FT                   /note="Missing (in Ref. 1; AFW98430)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   285 AA;  32797 MW;  483490FB380801B9 CRC64;
     MNSLFVGRPI VKSSYNVYTL PSSICGGHFF KVSNSLSLYD DHRRTRIEII RNSELIPKHV
     AIIMDGNRRW AKARGLPVQE GHKFLAPNLK NICNISSKLG IQVITAFAFS TENWNRSSEE
     VDFLMRLFEE FFEEFMRLGV RVSLIGGKSK LPTKLQQVIE LTEEVTKSNE GLHLMMALNY
     GGQYDMLQAT KNIASKVKDG LIKLEDIDYT LFEQELTTKC AKFPKPDLLI RTGGEQRISN
     FLLWQLAYSE LYFTNTLFPD FGEEALMDAI FSFQRRHRRF GGHTY
 
 
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