DDPS1_ARATH
ID DDPS1_ARATH Reviewed; 303 AA.
AC O80458; Q9SEB8;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Dehydrodolichyl diphosphate synthase 1;
DE Short=Dedol-PP synthase 1;
DE EC=2.5.1.87;
DE AltName: Full=Ditrans,polycis-polyprenyl diphosphate synthase ((2E,6E)-farnesyl diphosphate specific) 1;
GN Name=DPS; Synonyms=ACPT; OrderedLocusNames=At2g23410; ORFNames=F26B6.6;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=10764783; DOI=10.1074/jbc.m002000200;
RA Oh S.K., Han K.H., Ryu S.B., Kang H.;
RT "Molecular cloning, expression, and functional analysis of a cis-
RT prenyltransferase from Arabidopsis thaliana. Implications in rubber
RT biosynthesis.";
RL J. Biol. Chem. 275:18482-18488(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia; TISSUE=Seedling;
RX PubMed=10908715; DOI=10.1016/s0014-5793(00)01798-1;
RA Cunillera N., Arro M., Fores O., Manzano D., Ferrer A.;
RT "Characterization of dehydrodolichyl diphosphate synthase of Arabidopsis
RT thaliana, a key enzyme in dolichol biosynthesis.";
RL FEBS Lett. 477:170-174(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
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:10764783, ECO:0000269|PubMed:10908715}.
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:10764783,
CC ECO:0000269|PubMed:10908715};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.13 uM for farnesyl diphosphate (FPP);
CC KM=3.62 uM for geranylgeranyl diphosphate (GGPP);
CC KM=23 uM for isopentenyl diphosphate (IPP);
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:10764783, ECO:0000269|PubMed:10908715}; Single-pass
CC membrane protein {ECO:0000269|PubMed:10764783,
CC ECO:0000269|PubMed:10908715}.
CC -!- TISSUE SPECIFICITY: Expressed in low levels in the whole plant.
CC Preferentially expressed in roots. {ECO:0000269|PubMed:10764783,
CC ECO:0000269|PubMed:10908715}.
CC -!- SIMILARITY: Belongs to the UPP synthase family. {ECO:0000305}.
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DR EMBL; AF162441; AAF22257.1; -; mRNA.
DR EMBL; AJ277136; CAB91841.1; -; mRNA.
DR EMBL; AC003040; AAC23756.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC07452.1; -; Genomic_DNA.
DR PIR; T01130; T01130.
DR PIR; T52648; T52648.
DR RefSeq; NP_565551.1; NM_127905.4.
DR AlphaFoldDB; O80458; -.
DR SMR; O80458; -.
DR STRING; 3702.AT2G23410.1; -.
DR PaxDb; O80458; -.
DR PRIDE; O80458; -.
DR ProteomicsDB; 224609; -.
DR EnsemblPlants; AT2G23410.1; AT2G23410.1; AT2G23410.
DR GeneID; 816873; -.
DR Gramene; AT2G23410.1; AT2G23410.1; AT2G23410.
DR KEGG; ath:AT2G23410; -.
DR Araport; AT2G23410; -.
DR TAIR; locus:2046867; AT2G23410.
DR eggNOG; KOG1602; Eukaryota.
DR HOGENOM; CLU_038505_1_0_1; -.
DR InParanoid; O80458; -.
DR OMA; KSEMPNL; -.
DR OrthoDB; 1362420at2759; -.
DR PhylomeDB; O80458; -.
DR BioCyc; ARA:AT2G23410-MON; -.
DR BRENDA; 2.5.1.87; 399.
DR UniPathway; UPA00378; -.
DR PRO; PR:O80458; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O80458; baseline and differential.
DR Genevisible; O80458; AT.
DR GO; GO:0009570; C:chloroplast stroma; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045547; F:dehydrodolichyl diphosphate synthase activity; IGI:TAIR.
DR GO; GO:0002094; F:polyprenyltransferase activity; IBA:GO_Central.
DR GO; GO:0019408; P:dolichol biosynthetic process; IMP:TAIR.
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:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
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 Endoplasmic reticulum; Membrane; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..303
FT /note="Dehydrodolichyl diphosphate synthase 1"
FT /id="PRO_0000123751"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 303 AA; 34975 MW; 8446DF3C8BE5A81E CRC64;
MLSLLSSDSS LLSLLFLFLI PCLFITSYIG FPVFLLKLIG LIKIKAARDN EKRDEGTYVV
REDGLQRELM PRHVAFILDG NRRWAKRAGL TTSQGHEAGA KRLIDIAELC FELGVHTVSA
FAFSTENWGR DKIEIDNLMS LIQHYRNKSN IKFFHRSEVR VSVIGNKTKI PESLLKEIHE
IEEATKGYKN KHLIMAVDYS GKFDIMHACK SLVKKSEKGL IREEDVDEAL IERELLTNCS
DFPSPDLMIR TSGEQRISNF FLWQLAYSEL FFSPVFWPDF DKDKLLEALA SYQRRERRFG
CRV
