SPS3_ORYSJ
ID SPS3_ORYSJ Reviewed; 414 AA.
AC Q0INZ4; A0A0P0Y8W6; Q2QU65;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 08-MAY-2019, sequence version 2.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Probable solanesyl-diphosphate synthase 3, chloroplastic {ECO:0000305};
DE Short=OsSPS3 {ECO:0000305};
DE EC=2.5.1.84 {ECO:0000250|UniProtKB:Q75HZ9};
DE AltName: Full=Probable all-trans-nonaprenyl-diphosphate synthase 3 (geranyl-diphosphate specific) {ECO:0000305};
DE Flags: Precursor;
GN Name=SPS3 {ECO:0000305};
GN OrderedLocusNames=Os12g0271700 {ECO:0000312|EMBL:BAT16653.1},
GN LOC_Os12g17320 {ECO:0000312|EMBL:ABA97399.2};
GN ORFNames=OsJ_1767i3 {ECO:0000312|EMBL:ABA97399.2};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16188032; DOI=10.1186/1741-7007-3-20;
RG The rice chromosomes 11 and 12 sequencing consortia;
RT "The sequence of rice chromosomes 11 and 12, rich in disease resistance
RT genes and recent gene duplications.";
RL BMC Biol. 3:20-20(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
CC -!- FUNCTION: Involved in providing solanesyl diphosphate for
CC plastoquinone-9 (PQ-9) formation. {ECO:0000250|UniProtKB:Q75HZ9}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate + 7 isopentenyl diphosphate = all-
CC trans-nonaprenyl diphosphate + 7 diphosphate; Xref=Rhea:RHEA:27563,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58057, ChEBI:CHEBI:58391,
CC ChEBI:CHEBI:128769; EC=2.5.1.84;
CC Evidence={ECO:0000250|UniProtKB:Q75HZ9};
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 -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q5HZ00}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABA97399.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAF29571.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAT16653.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=EEE62870.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DP000011; ABA97399.2; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008218; BAF29571.1; ALT_INIT; Genomic_DNA.
DR EMBL; AP014968; BAT16653.1; ALT_INIT; Genomic_DNA.
DR EMBL; CM000142; EEE62870.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_015620200.1; XM_015764714.1.
DR AlphaFoldDB; Q0INZ4; -.
DR SMR; Q0INZ4; -.
DR STRING; 4530.OS12T0271700-02; -.
DR PaxDb; Q0INZ4; -.
DR PRIDE; Q0INZ4; -.
DR EnsemblPlants; Os12t0271700-02; Os12t0271700-02; Os12g0271700.
DR GeneID; 4351957; -.
DR Gramene; Os12t0271700-02; Os12t0271700-02; Os12g0271700.
DR KEGG; osa:4351957; -.
DR eggNOG; KOG0776; Eukaryota.
DR HOGENOM; CLU_014015_2_2_1; -.
DR PlantReactome; R-OSA-1119367; Polyisoprenoid biosynthesis.
DR Proteomes; UP000000763; Chromosome 12.
DR Proteomes; UP000007752; Chromosome 5.
DR Proteomes; UP000059680; Chromosome 12.
DR ExpressionAtlas; Q0INZ4; baseline and differential.
DR Genevisible; Q0INZ4; OS.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0052923; F:all-trans-nonaprenyl-diphosphate synthase (geranyl-diphosphate specific) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW Chloroplast; Isoprene biosynthesis; Magnesium; Metal-binding; Plastid;
KW Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..72
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 73..414
FT /note="Probable solanesyl-diphosphate synthase 3,
FT chloroplastic"
FT /evidence="ECO:0000250"
FT /id="PRO_0000414853"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 134
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 137
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 172
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 179
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 179
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 183
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 183
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 188
FT /ligand="an all-trans-polyprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58914"
FT /evidence="ECO:0000250"
FT BINDING 189
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 265
FT /ligand="an all-trans-polyprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58914"
FT /evidence="ECO:0000250"
FT BINDING 266
FT /ligand="an all-trans-polyprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58914"
FT /evidence="ECO:0000250"
FT BINDING 303
FT /ligand="an all-trans-polyprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58914"
FT /evidence="ECO:0000250"
FT BINDING 320
FT /ligand="an all-trans-polyprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58914"
FT /evidence="ECO:0000250"
SQ SEQUENCE 414 AA; 44374 MW; 64A3D0B7FF591E6B CRC64;
MAAPSSLASS SHLSRRATAA ASPSIPPPSP PPPPQRLRCG WVGRAAPPTR RAPGVCSVVS
PSKPGVAAVD VPAATIPDAA ATGVGVAERI SVSSLLEVVA DDLLKLNNNL KSLVGAENPV
LVSAAEQIFG AGGKRLRPAL VFLVSRATAE LAGLLELTTE HQRLAEIIEM IHTASLIHDD
VIDDSGMRRG KETIHQLYGT RVAVLAGDFM FAQSSWFLAN LENIEVIKLI SQVIKDFASG
EIKQASTLFD CDITLDDYLL KSYYKTASLI AASTRSAAIF SGVSTAICEQ MYEYGRNLGL
SFQVVDDILD FTQSAEQLGK PAGSDLAKGN LTAPVIFALQ DEPQLREIID SEFSETNSLA
TAIELVHRSG GIKRAHELAR EKGEIAIQSL QCLPRSEFRS TLENMVKYNL ERID
