SPS2_ARATH
ID SPS2_ARATH Reviewed; 417 AA.
AC Q76FS5; Q84LG1; Q9SHG4;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Solanesyl diphosphate synthase 2, chloroplastic {ECO:0000305};
DE Short=AtSPS2 {ECO:0000303|PubMed:15653808};
DE EC=2.5.1.85 {ECO:0000269|PubMed:15784989};
DE AltName: Full=All-trans-nonaprenyl-diphosphate synthase 2 (geranylgeranyl-diphosphate specific) {ECO:0000305};
DE Flags: Precursor;
GN Name=SPS2 {ECO:0000303|PubMed:15653808}; Synonyms=SPPS {ECO:0000305};
GN OrderedLocusNames=At1g17050 {ECO:0000312|Araport:AT1G17050};
GN ORFNames=F20D23.25 {ECO:0000312|EMBL:AAD50025.1};
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, AND SUBCELLULAR LOCATION.
RX PubMed=15653808; DOI=10.1093/pcp/pch211;
RA Luo J., Saiki R., Tatsumi K., Nakagawa T., Kawamukai M.;
RT "Identification and subcellular localization of two solanesyl diphosphate
RT synthases from Arabidopsis thaliana.";
RL Plant Cell Physiol. 45:1882-1888(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=15784989; DOI=10.1271/bbb.69.592;
RA Hirooka K., Izumi Y., An C.I., Nakazawa Y., Fukusaki E., Kobayashi A.;
RT "Functional analysis of two solanesyl diphosphate synthases from
RT Arabidopsis thaliana.";
RL Biosci. Biotechnol. Biochem. 69:592-601(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF Clones.";
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 96-417.
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=23913686; DOI=10.1074/jbc.m113.492769;
RA Block A., Fristedt R., Rogers S., Kumar J., Barnes B., Barnes J.,
RA Elowsky C.G., Wamboldt Y., Mackenzie S.A., Redding K., Merchant S.S.,
RA Basset G.J.;
RT "Functional modeling identifies paralogous solanesyl-diphosphate synthases
RT that assemble the side chain of plastoquinone-9 in plastids.";
RL J. Biol. Chem. 288:27594-27606(2013).
RN [8]
RP INTERACTION WITH FBN5, AND SUBCELLULAR LOCATION.
RX PubMed=26432861; DOI=10.1105/tpc.15.00707;
RA Kim E.H., Lee Y., Kim H.U.;
RT "Fibrillin 5 is essential for plastoquinone-9 biosynthesis by binding to
RT solanesyl diphosphate synthases in Arabidopsis.";
RL Plant Cell 27:2956-2971(2015).
RN [9]
RP INDUCTION BY HIGH LIGHT.
RX PubMed=26039552; DOI=10.1038/srep10919;
RA Ksas B., Becuwe N., Chevalier A., Havaux M.;
RT "Plant tolerance to excess light energy and photooxidative damage relies on
RT plastoquinone biosynthesis.";
RL Sci. Rep. 5:10919-10919(2015).
CC -!- FUNCTION: Involved in providing solanesyl diphosphate for
CC plastoquinone-9 (PQ-9) formation in plastids (PubMed:15784989,
CC PubMed:23913686) (Probable). Catalyzes the elongation of the prenyl
CC side chain of PQ-9 in plastids (PubMed:23913686). Contributes to the
CC biosynthesis of plastochromanol-8 (PC-8) in plastids (PubMed:23913686).
CC Does not contribute to the synthesis of tocopherol or ubiquinone
CC (PubMed:23913686). PQ-9 and PC-8 are lipophilic antioxidants that act
CC as protectant against photooxidative stress under high light stress
CC conditions (PubMed:23913686). Prefers geranylgeranyl diphosphate to
CC farnesyl diphosphate as substrate (PubMed:15784989). No activity with
CC geranyl diphosphate or dimethylallyl diphosphate as substrate
CC (PubMed:15784989). {ECO:0000269|PubMed:15784989,
CC ECO:0000269|PubMed:23913686, ECO:0000305|PubMed:15653808}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E,10E)-geranylgeranyl diphosphate + 5 isopentenyl
CC diphosphate = all-trans-nonaprenyl diphosphate + 5 diphosphate;
CC Xref=Rhea:RHEA:27594, ChEBI:CHEBI:33019, ChEBI:CHEBI:58391,
CC ChEBI:CHEBI:58756, ChEBI:CHEBI:128769; EC=2.5.1.85;
CC Evidence={ECO:0000269|PubMed:15784989};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6.89 uM for farnesyl diphosphate (in the presence of 500 uM of
CC isopentenyl diphosphate) {ECO:0000269|PubMed:15784989};
CC KM=0.843 uM for geranylgeranyl diphosphate (in the presence of 100 uM
CC of isopentenyl diphosphate) {ECO:0000269|PubMed:15784989};
CC KM=182 uM for isopentenyl diphosphate (in the presence of 20 uM of
CC farnesyl diphosphate) {ECO:0000269|PubMed:15784989};
CC KM=28.9 uM for isopentenyl diphosphate (in the presence of 4 uM of
CC geranylgeranyl diphosphate) {ECO:0000269|PubMed:15784989};
CC Note=kcat is 3.77 sec(-1) with farnesyl diphosphate as substrate (in
CC the presence of 500 uM of isopentenyl diphosphate). kcat is 2.33
CC sec(-1) with geranylgeranyl diphosphate as substrate (in the presence
CC of 100 uM of isopentenyl diphosphate). kcat is 2.83 sec(-1) with
CC isopentenyl diphosphate as substrate (in the presence of 20 uM of
CC farnesyl diphosphate). kcat is 1.72 sec(-1) with isopentenyl
CC diphosphate as substrate (in the presence of 4 uM of geranylgeranyl
CC diphosphate).;
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:15784989};
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with FBN5
CC (PubMed:26432861). {ECO:0000250|UniProtKB:Q5HZ00,
CC ECO:0000269|PubMed:26432861}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:15653808, ECO:0000269|PubMed:15784989,
CC ECO:0000269|PubMed:23913686, ECO:0000269|PubMed:26432861}.
CC -!- TISSUE SPECIFICITY: Higher expression in leaves than in roots.
CC {ECO:0000269|PubMed:15784989}.
CC -!- INDUCTION: Induced by high light conditions.
CC {ECO:0000269|PubMed:26039552}.
CC -!- DISRUPTION PHENOTYPE: Reduced growth (PubMed:23913686). Decreased
CC levels of plastoquinone-9 (PQ-9) and complete loss of plastochromanol-8
CC (PC-8) in leaves (PubMed:23913686). Severe increase of photoinhibition
CC at high light intensity (PubMed:23913686). The double mutants sps1 and
CC sps2 exhibit an albino phenotype and are devoided of both PQ-9 and PC-8
CC in cotyledons (PubMed:23913686). {ECO:0000269|PubMed:23913686}.
CC -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD50025.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB104727; BAC82428.1; -; mRNA.
DR EMBL; AB188498; BAD88534.1; -; mRNA.
DR EMBL; AC007651; AAD50025.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002684; AEE29535.1; -; Genomic_DNA.
DR EMBL; BT028962; ABI54337.1; -; mRNA.
DR EMBL; BT004246; AAO42250.1; -; mRNA.
DR PIR; C86306; C86306.
DR RefSeq; NP_173148.2; NM_101565.6.
DR AlphaFoldDB; Q76FS5; -.
DR SMR; Q76FS5; -.
DR BioGRID; 23515; 1.
DR STRING; 3702.AT1G17050.1; -.
DR PaxDb; Q76FS5; -.
DR PRIDE; Q76FS5; -.
DR ProteomicsDB; 232487; -.
DR EnsemblPlants; AT1G17050.1; AT1G17050.1; AT1G17050.
DR GeneID; 838275; -.
DR Gramene; AT1G17050.1; AT1G17050.1; AT1G17050.
DR KEGG; ath:AT1G17050; -.
DR Araport; AT1G17050; -.
DR TAIR; locus:2020362; AT1G17050.
DR eggNOG; KOG0776; Eukaryota.
DR HOGENOM; CLU_014015_2_2_1; -.
DR OMA; LEMCACK; -.
DR OrthoDB; 381154at2759; -.
DR PhylomeDB; Q76FS5; -.
DR BioCyc; ARA:AT1G17050-MON; -.
DR BioCyc; MetaCyc:AT1G17050-MON; -.
DR BRENDA; 2.5.1.85; 399.
DR PRO; PR:Q76FS5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q76FS5; baseline and differential.
DR Genevisible; Q76FS5; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0009536; C:plastid; IDA:TAIR.
DR GO; GO:0052924; F:all-trans-nonaprenyl-diphosphate synthase (geranylgeranyl-diphosphate specific) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004659; F:prenyltransferase activity; IBA:GO_Central.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; IBA:GO_Central.
DR GO; GO:0010236; P:plastoquinone biosynthetic process; IMP:TAIR.
DR CDD; cd00685; Trans_IPPS_HT; 1.
DR Gene3D; 1.10.600.10; -; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR000092; Polyprenyl_synt.
DR InterPro; IPR033749; Polyprenyl_synt_CS.
DR Pfam; PF00348; polyprenyl_synt; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
DR PROSITE; PS00723; POLYPRENYL_SYNTHASE_1; 1.
DR PROSITE; PS00444; POLYPRENYL_SYNTHASE_2; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Isoprene biosynthesis; Magnesium; Metal-binding; Plastid;
KW Reference proteome; Stress response; Transferase; Transit peptide.
FT TRANSIT 1..60
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 61..417
FT /note="Solanesyl diphosphate synthase 2, chloroplastic"
FT /id="PRO_0000414849"
FT BINDING 137
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 140
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 175
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 182
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 182
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 186
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 186
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 191
FT /ligand="an all-trans-polyprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58914"
FT /evidence="ECO:0000250"
FT BINDING 192
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 268
FT /ligand="an all-trans-polyprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58914"
FT /evidence="ECO:0000250"
FT BINDING 269
FT /ligand="an all-trans-polyprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58914"
FT /evidence="ECO:0000250"
FT BINDING 306
FT /ligand="an all-trans-polyprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58914"
FT /evidence="ECO:0000250"
FT BINDING 323
FT /ligand="an all-trans-polyprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58914"
FT /evidence="ECO:0000250"
SQ SEQUENCE 417 AA; 46045 MW; E62BA8786A2548BB CRC64;
MMMSCRNIDL GTSVLDHSCS SSSTSRRFLF GNSSKTVCMI GGRSCVGNLV FLRRDLATCR
AVPAKSKENS LVNGIGQDQT VMLNLRQESR KPISLETLFE VVADDLQRLN DNLLSIVGAE
NPVLISAAEQ IFSAGGKRMR PGLVFLVSRA TAELAGLKEL TVEHRRLGEI IEMIHTASLI
HDDVLDESDM RRGRETVHEL FGTRVAVLAG DFMFAQASWY LANLENLEVI KLISQVIKDF
ASGEIKQASS LFDCDVKLDD YMLKSYYKTA SLVAASTKGA AIFSKVESKV AEQMYQFGKN
LGLSFQVVDD ILDFTQSTEQ LGKPAANDLA KGNITAPVIF ALENEPRLRE IIESEFCEPG
SLEEAIEIVR NRGGIKKAQE LAKEKAELAL KNLNCLPRSG FRSALEDMVM FNLERID
