SPS1_ARATH
ID SPS1_ARATH Reviewed; 406 AA.
AC Q8S948; A8MQY5; Q0WMS5; Q9SYN0;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Solanesyl diphosphate synthase 1, chloroplastic {ECO:0000305};
DE Short=AtSPS1 {ECO:0000303|PubMed:15653808};
DE EC=2.5.1.85 {ECO:0000269|PubMed:12437513};
DE AltName: Full=All-trans-nonaprenyl-diphosphate synthase 1 (geranylgeranyl-diphosphate specific) {ECO:0000305};
DE AltName: Full=Geranylgeranyl diphosphate synthase {ECO:0000305};
DE EC=2.5.1.29 {ECO:0000269|PubMed:12437513};
DE Flags: Precursor;
GN Name=SPS1 {ECO:0000303|PubMed:15653808};
GN Synonyms=SPPS {ECO:0000305}, SPS {ECO:0000303|PubMed:12437513};
GN OrderedLocusNames=At1g78510 {ECO:0000312|Araport:AT1G78510};
GN ORFNames=T30F21.15 {ECO:0000312|EMBL:AAD30584.1};
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] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=12437513; DOI=10.1042/bj20021311;
RA Hirooka K., Bamba T., Fukusaki E., Kobayashi A.;
RT "Cloning and kinetic characterization of Arabidopsis thaliana solanesyl
RT diphosphate synthase.";
RL Biochem. J. 370:679-686(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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 [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] (ISOFORM 1).
RA Shinn P., Chen H., Kim C.J., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP TISSUE SPECIFICITY.
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 [8]
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 [9]
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 [10]
RP FUNCTION, AND 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).
RN [11]
RP FUNCTION.
RX PubMed=29901834; DOI=10.1111/tpj.13993;
RA Ferretti U., Ciura J., Ksas B., Rac M., Sedlarova M., Kruk J., Havaux M.,
RA Pospisil P.;
RT "Chemical quenching of singlet oxygen by plastoquinols and their oxidation
RT products in Arabidopsis.";
RL Plant J. 0:0-0(2018).
CC -!- FUNCTION: Involved in providing solanesyl diphosphate for
CC plastoquinone-9 (PQ-9) formation in plastids (PubMed:12437513,
CC PubMed:23913686, PubMed:26039552). Catalyzes the elongation of the
CC prenyl side chain of PQ-9 in plastids (PubMed:23913686,
CC PubMed:26039552). Contributes to the biosynthesis of plastochromanol-8
CC (PC-8) in plastids (PubMed:23913686, PubMed:26039552). Does not
CC 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, PubMed:26039552, PubMed:29901834). Prefers
CC geranylgeranyl diphosphate to farnesyl diphosphate as substrate
CC (PubMed:12437513). No activity with geranyl diphosphate or
CC dimethylallyl diphosphate as substrate (PubMed:12437513).
CC {ECO:0000269|PubMed:12437513, ECO:0000269|PubMed:23913686,
CC ECO:0000269|PubMed:26039552, ECO:0000269|PubMed:29901834}.
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:12437513};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27595;
CC Evidence={ECO:0000269|PubMed:12437513};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate + isopentenyl diphosphate =
CC (2E,6E,10E)-geranylgeranyl diphosphate + diphosphate;
CC Xref=Rhea:RHEA:17653, ChEBI:CHEBI:33019, ChEBI:CHEBI:58756,
CC ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; EC=2.5.1.29;
CC Evidence={ECO:0000269|PubMed:12437513};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17654;
CC Evidence={ECO:0000269|PubMed:12437513};
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=5.73 uM for farnesyl diphosphate (in the presence of 500 uM of
CC isopentenyl diphosphate) {ECO:0000269|PubMed:12437513};
CC KM=1.61 uM for geranylgeranyl diphosphate (in the presence of 100 uM
CC of isopentenyl diphosphate) {ECO:0000269|PubMed:12437513};
CC KM=151 uM for isopentenyl diphosphate (in the presence of 20 uM of
CC farnesyl diphosphate) {ECO:0000269|PubMed:12437513};
CC KM=20 uM for isopentenyl diphosphate (in the presence of 4 uM of
CC geranylgeranyl diphosphate) {ECO:0000269|PubMed:12437513};
CC Note=kcat is 29.7 sec(-1) with farnesyl diphosphate as substrate (in
CC the presence of 500 uM of isopentenyl diphosphate). kcat is 21.0
CC sec(-1) with geranylgeranyl diphosphate as substrate (in the presence
CC of 100 uM of isopentenyl diphosphate). kcat is 14.7 sec(-1) with
CC isopentenyl diphosphate as substrate (in the presence of 20 uM of
CC farnesyl diphosphate). kcat is 15.0 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:12437513};
CC -!- SUBUNIT: Homodimer (PubMed:12437513). Interacts with FBN5
CC (PubMed:26432861). {ECO:0000269|PubMed:12437513,
CC ECO:0000269|PubMed:26432861}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:23913686, ECO:0000269|PubMed:26432861}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8S948-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8S948-2; Sequence=VSP_042134;
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: Decreased levels of plastoquinone-9 (PQ-9) and
CC plastochromanol-8 (PC-8) in leaves (PubMed:23913686). The double
CC mutants sps1 and sps2 exhibit an albino phenotype and are devoided of
CC both PQ-9 and PC-8 in cotyledons (PubMed:23913686).
CC {ECO:0000269|PubMed:23913686}.
CC -!- MISCELLANEOUS: Plants over-expressing SPS1 exhibit increased resistance
CC to photooxidative stress, decreases in leaf bleaching, lipid
CC peroxidation and PSII photoinhibition under excess light due to their
CC increased capacities for plastoquinone-9 (PQ-9) biosynthesis
CC (PubMed:26039552). Plants over-expressing SPS1 exhibit decreased
CC singlet oxygen production in response to photooxidative stress due to
CC increased levels of PQ-9, which acts as chemical quencher of singlet
CC oxygen (PubMed:29901834). {ECO:0000269|PubMed:26039552,
CC ECO:0000269|PubMed:29901834}.
CC -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD30584.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB071514; BAB86941.1; -; mRNA.
DR EMBL; AB188497; BAD88533.1; -; mRNA.
DR EMBL; AC007260; AAD30584.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE36114.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE36115.1; -; Genomic_DNA.
DR EMBL; BT025550; ABF58968.1; -; mRNA.
DR EMBL; AK229738; BAF01575.1; -; mRNA.
DR PIR; F96813; F96813.
DR RefSeq; NP_001077840.1; NM_001084371.1. [Q8S948-2]
DR RefSeq; NP_177972.2; NM_106498.4. [Q8S948-1]
DR AlphaFoldDB; Q8S948; -.
DR SMR; Q8S948; -.
DR BioGRID; 29406; 2.
DR STRING; 3702.AT1G78510.1; -.
DR SwissLipids; SLP:000001502; -. [Q8S948-1]
DR iPTMnet; Q8S948; -.
DR PaxDb; Q8S948; -.
DR PRIDE; Q8S948; -.
DR ProteomicsDB; 245348; -. [Q8S948-1]
DR EnsemblPlants; AT1G78510.1; AT1G78510.1; AT1G78510. [Q8S948-1]
DR EnsemblPlants; AT1G78510.2; AT1G78510.2; AT1G78510. [Q8S948-2]
DR GeneID; 844187; -.
DR Gramene; AT1G78510.1; AT1G78510.1; AT1G78510. [Q8S948-1]
DR Gramene; AT1G78510.2; AT1G78510.2; AT1G78510. [Q8S948-2]
DR KEGG; ath:AT1G78510; -.
DR Araport; AT1G78510; -.
DR TAIR; locus:2202940; AT1G78510.
DR eggNOG; KOG0776; Eukaryota.
DR HOGENOM; CLU_014015_2_2_1; -.
DR OMA; GKQMRPM; -.
DR OrthoDB; 381154at2759; -.
DR PhylomeDB; Q8S948; -.
DR BioCyc; ARA:AT1G78510-MON; -.
DR BioCyc; MetaCyc:AT1G78510-MON; -.
DR BRENDA; 2.5.1.85; 399.
DR PRO; PR:Q8S948; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8S948; baseline and differential.
DR Genevisible; Q8S948; AT.
DR GO; GO:0009507; C:chloroplast; IBA:GO_Central.
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:0004311; F:farnesyltranstransferase 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:0050347; F:trans-octaprenyltranstransferase activity; IDA:TAIR.
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 Alternative splicing; Chloroplast; Isoprene biosynthesis; Magnesium;
KW Metal-binding; Plastid; Reference proteome; Stress response; Transferase;
KW Transit peptide.
FT TRANSIT 1..71
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 72..406
FT /note="Solanesyl diphosphate synthase 1, chloroplastic"
FT /id="PRO_0000414848"
FT BINDING 126
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 129
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 164
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 171
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 171
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 175
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 175
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 180
FT /ligand="an all-trans-polyprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58914"
FT /evidence="ECO:0000250"
FT BINDING 181
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 257
FT /ligand="an all-trans-polyprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58914"
FT /evidence="ECO:0000250"
FT BINDING 258
FT /ligand="an all-trans-polyprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58914"
FT /evidence="ECO:0000250"
FT BINDING 295
FT /ligand="an all-trans-polyprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58914"
FT /evidence="ECO:0000250"
FT BINDING 312
FT /ligand="an all-trans-polyprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58914"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..63
FT /note="MMTSCRNIDLGTMMMACGCGRRQFPSLAKTVCKFTSSNRSYGGLVGSCKAVP
FT TKSKEISLLNG -> MAVWWGVAKRCQRNQRRSLCSMVC (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_042134"
FT CONFLICT 388
FT /note="S -> G (in Ref. 6; BAF01575)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 406 AA; 44468 MW; 2FDDD1877A569411 CRC64;
MMTSCRNIDL GTMMMACGCG RRQFPSLAKT VCKFTSSNRS YGGLVGSCKA VPTKSKEISL
LNGIGQSQTV SFDLKQESKQ PISLVTLFEL VAVDLQTLND NLLSIVGAEN PVLISAAEQI
FGAGGKRMRP GLVFLVSHAT AELAGLKELT TEHRRLAEII EMIHTASLIH DDVLDESDMR
RGKETVHELF GTRVAVLAGD FMFAQASWYL ANLENLEVIK LISQVIKDFA SGEIKQASSL
FDCDTKLDEY LLKSFYKTAS LVAASTKGAA IFSRVEPDVT EQMYEFGKNL GLSFQIVDDI
LDFTQSTEQL GKPAGSDLAK GNLTAPVIFA LEREPRLREI IESEFCEAGS LEEAIEAVTK
GGGIKRAQEL AREKADDAIK NLQCLPRSGF RSALEDMVLY NLERID
