ID   CPT5_SOLLC              Reviewed;         313 AA.
AC   K7X479; A0A494GA08;
DT   07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2013, sequence version 1.
DT   25-MAY-2022, entry version 29.
DE   RecName: Full=Dehydrodolichyl diphosphate synthase CPT5, chloroplastic {ECO:0000305};
DE            EC=2.5.1.87 {ECO:0000269|PubMed:23134568};
DE   AltName: Full=Cis-prenyltransferase 5 {ECO:0000303|PubMed:23134568};
DE            Short=SlCPT5 {ECO:0000303|PubMed:23134568};
DE   Flags: Precursor;
GN   Name=CPT5 {ECO:0000303|PubMed:23134568};
GN   OrderedLocusNames=Solyc00g136560 {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: Catalyzes cis-prenyl chain elongation to produce the
CC       polyprenyl backbone of dolichol, a glycosyl carrier-lipid required for
CC       the biosynthesis of several classes of glycoprotein.
CC       {ECO:0000269|PubMed:23134568}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E)-farnesyl diphosphate + n isopentenyl diphosphate = di-
CC         trans,poly-cis-polyprenyl diphosphate + n diphosphate;
CC         Xref=Rhea:RHEA:53008, Rhea:RHEA-COMP:13431, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:128769, ChEBI:CHEBI:136960, ChEBI:CHEBI:175763;
CC         EC=2.5.1.87; Evidence={ECO:0000269|PubMed:23134568};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53009;
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}.
CC   -!- TISSUE SPECIFICITY: Expressed in leaf trichomes, stem trichomes and old
CC       leaves (PubMed:23134568). Expressed at low levels in young leaves and
CC       flowers (PubMed:23134568). {ECO:0000269|PubMed:23134568}.
CC   -!- SIMILARITY: Belongs to the UPP synthase family. {ECO:0000305}.
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DR   EMBL; JX943887; AFW98429.1; -; Genomic_DNA.
DR   EMBL; CM001076; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; K7X479; -.
DR   SMR; K7X479; -.
DR   STRING; 4081.Solyc00g136560.2.1; -.
DR   Proteomes; UP000004994; Unplaced.
DR   ExpressionAtlas; K7X479; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
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..42
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           43..313
FT                   /note="Dehydrodolichyl diphosphate synthase CPT5,
FT                   chloroplastic"
FT                   /id="PRO_0000450936"
FT   ACT_SITE        89
FT                   /evidence="ECO:0000250|UniProtKB:P60472"
SQ   SEQUENCE   313 AA;  35540 MW;  F868381114A024A2 CRC64;
     MAFSFQLQQV FPFPVKFCSQ PKSIKLQIFP NLTKRLPIHP LASAQNNATS NIDHNYIAMD
     ESSINEEEVP LPTELSRELM PKHIAVIMDG NRRWAKRRGL PVALGYAAGI RVLRNFVKLS
     YNWGISALTL FAFSSENWFR PKAEVDLLMG LFDKVLKDEL ENLARTGIRL SIIGDASQLP
     KSLQDLIDKA VMATKANSRL HILVAINYSG QYDVVQACQT IAQRVKDGNI EPEDINSLLV
     EQELQTKCTE FPSPDLLIRT SGELRLSNFL LWQLAYTELF FSHSQWPDFG EAEFLEALCS
     FQQRQRRYGG QSS