SPS1_ORYSJ
ID SPS1_ORYSJ Reviewed; 430 AA.
AC Q653T6; A0A0N7KML1; B9FQH5;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Solanesyl-diphosphate synthase 1, mitochondrial {ECO:0000303|PubMed:20421194};
DE Short=OsSPS1 {ECO:0000303|PubMed:20421194};
DE EC=2.5.1.84 {ECO:0000269|PubMed:20421194};
DE AltName: Full=All-trans-nonaprenyl-diphosphate synthase 1 (geranyl-diphosphate specific) {ECO:0000305};
DE Flags: Precursor;
GN Name=SPS1 {ECO:0000303|PubMed:20421194};
GN OrderedLocusNames=Os06g0678200 {ECO:0000312|EMBL:BAS99121.1},
GN LOC_Os06g46450 {ECO:0000305};
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=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 [2]
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 [3]
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 [4]
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).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=20421194; DOI=10.1093/jxb/erq103;
RA Ohara K., Sasaki K., Yazaki K.;
RT "Two solanesyl diphosphate synthases with different subcellular
RT localizations and their respective physiological roles in Oryza sativa.";
RL J. Exp. Bot. 61:2683-2692(2010).
CC -!- FUNCTION: Involved in the supply of solanesyl diphosphate for
CC ubiquinone-9 (UQ-9) biosynthesis in mitochondria. Farnesyl diphosphate
CC is the preferred substrate. {ECO:0000269|PubMed:20421194}.
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:0000269|PubMed:20421194};
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 -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q5HZ00}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:20421194}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, stems and roots. Highest
CC expression in roots. {ECO:0000269|PubMed:20421194}.
CC -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EEE66217.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP003728; BAD45534.1; -; Genomic_DNA.
DR EMBL; AP004989; BAD45931.1; -; Genomic_DNA.
DR EMBL; AP008212; BAF20276.1; -; Genomic_DNA.
DR EMBL; AP014962; BAS99121.1; -; Genomic_DNA.
DR EMBL; CM000143; EEE66217.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AK059456; BAG87000.1; -; mRNA.
DR RefSeq; XP_015644451.1; XM_015788965.1.
DR AlphaFoldDB; Q653T6; -.
DR SMR; Q653T6; -.
DR STRING; 4530.OS06T0678200-01; -.
DR PaxDb; Q653T6; -.
DR PRIDE; Q653T6; -.
DR EnsemblPlants; Os06t0678200-01; Os06t0678200-01; Os06g0678200.
DR GeneID; 4341844; -.
DR Gramene; Os06t0678200-01; Os06t0678200-01; Os06g0678200.
DR KEGG; osa:4341844; -.
DR eggNOG; KOG0776; Eukaryota.
DR HOGENOM; CLU_014015_1_2_1; -.
DR OMA; RVAKYYT; -.
DR OrthoDB; 381154at2759; -.
DR BRENDA; 2.5.1.84; 4460.
DR BRENDA; 2.5.1.B14; 4460.
DR PlantReactome; R-OSA-1119367; Polyisoprenoid biosynthesis.
DR PlantReactome; R-OSA-1119457; Geranyldiphosphate biosynthesis.
DR PlantReactome; R-OSA-1119526; Trans,trans-farnesyl diphosphate biosynthesis.
DR PlantReactome; R-OSA-1119545; Geranylgeranyldiphosphate biosynthesis II (plastidic).
DR UniPathway; UPA00232; -.
DR Proteomes; UP000000763; Chromosome 6.
DR Proteomes; UP000007752; Chromosome 6.
DR Proteomes; UP000059680; Chromosome 6.
DR Genevisible; Q653T6; OS.
DR GO; GO:0005739; C:mitochondrion; IDA:CACAO.
DR GO; GO:1990234; C:transferase complex; IBA:GO_Central.
DR GO; GO:0052923; F:all-trans-nonaprenyl-diphosphate synthase (geranyl-diphosphate specific) activity; IEA:UniProtKB-EC.
DR GO; GO:0004311; F:farnesyltranstransferase activity; IDA:UniProtKB.
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; IDA:UniProtKB.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; IBA:GO_Central.
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 Isoprene biosynthesis; Magnesium; Metal-binding; Mitochondrion;
KW Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..31
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 32..430
FT /note="Solanesyl-diphosphate synthase 1, mitochondrial"
FT /id="PRO_0000414851"
FT BINDING 133
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 136
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 182
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 189
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 189
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 193
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 193
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 198
FT /ligand="an all-trans-polyprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58914"
FT /evidence="ECO:0000250"
FT BINDING 199
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 275
FT /ligand="an all-trans-polyprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58914"
FT /evidence="ECO:0000250"
FT BINDING 276
FT /ligand="an all-trans-polyprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58914"
FT /evidence="ECO:0000250"
FT BINDING 313
FT /ligand="an all-trans-polyprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58914"
FT /evidence="ECO:0000250"
FT BINDING 330
FT /ligand="an all-trans-polyprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58914"
FT /evidence="ECO:0000250"
SQ SEQUENCE 430 AA; 47064 MW; FD65E337BAE68381 CRC64;
MSWRWALARR VAALGATSGG GDGATAQAQR LFSSAAALLG RHPPPPSPPH YQIRSKVVGC
RGATFVSSRW LHDAQYQVRQ DGLSRSEEQQ DPFELVADEL SLLANRLRSM VAAEVPKLAS
AAEYFFKVGA EGKRFRPTVL LLMASALKFP LSDSTEVGVL TILANKLRTR QQNIAEITEM
IHVASLLHDD VLDDADTRRG VSSLNCIMGN KLSVLAGDFL LSRACVALAA LGNTEVVSLM
ATAVEHLVTG ETMQISTSRE QRRSMDYYLQ KTYYKTASLI SNSCKAVAIL AGHTADVSML
AYEYGRNLGL AFQLIDDVLD FTGTSASLGK GSLTDIRHGI ITAPMLYAME EFPQLHEVVD
RGFDNPANVE LALDYLQKSR GIEKTKELAR EHANRAIKAI EALPDSDDED VLTSRRALID
ITERVITRTK
