SPS2_ORYSJ
ID SPS2_ORYSJ Reviewed; 403 AA.
AC Q75HZ9; A0A0P0WQS6; Q6L5D5;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Solanesyl-diphosphate synthase 2, chloroplastic {ECO:0000303|PubMed:20421194};
DE Short=OsSPS2 {ECO:0000303|PubMed:20421194};
DE EC=2.5.1.84 {ECO:0000269|PubMed:20421194};
DE AltName: Full=All-trans-nonaprenyl-diphosphate synthase 2 (geranyl-diphosphate specific) {ECO:0000305};
DE Flags: Precursor;
GN Name=SPS2 {ECO:0000303|PubMed:20421194};
GN OrderedLocusNames=Os05g0582300 {ECO:0000312|EMBL:BAS95534.1},
GN LOC_Os05g50550 {ECO:0000305};
GN ORFNames=OJ1651_G11.10 {ECO:0000312|EMBL:AAT44203.1},
GN OsJ_19688 {ECO:0000312|EMBL:EEE64831.1},
GN OSJNBb0035N21.17 {ECO:0000312|EMBL:AAS16899.2};
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=16261349; DOI=10.1007/s00438-005-0039-y;
RA Cheng C.-H., Chung M.C., Liu S.-M., Chen S.-K., Kao F.Y., Lin S.-J.,
RA Hsiao S.-H., Tseng I.C., Hsing Y.-I.C., Wu H.-P., Chen C.-S., Shaw J.-F.,
RA Wu J., Matsumoto T., Sasaki T., Chen H.-C., Chow T.-Y.;
RT "A fine physical map of the rice chromosome 5.";
RL Mol. Genet. Genomics 274:337-345(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).
RN [6]
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 [7]
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).
RN [8]
RP INTERACTION WITH FBN5, AND SUBCELLULAR LOCATION.
RX PubMed=28751900; DOI=10.3389/fpls.2017.01197;
RA Kim E.H., Lee D.W., Lee K.R., Jung S.J., Jeon J.S., Kim H.U.;
RT "Conserved function of Fibrillin5 in the plastoquinone-9 biosynthetic
RT pathway in Arabidopsis and rice.";
RL Front. Plant Sci. 8:1197-1197(2017).
CC -!- FUNCTION: Involved in providing solanesyl diphosphate for
CC plastoquinone-9 (PQ-9) formation. Geranyl diphosphate is the preferred
CC 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 -!- SUBUNIT: Homodimer (By similarity). Interacts with FBN5
CC (PubMed:28751900). {ECO:0000250|UniProtKB:Q5HZ00,
CC ECO:0000269|PubMed:28751900}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:20421194, ECO:0000269|PubMed:28751900}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, stems and roots. Highest
CC expression in leaves and roots. {ECO:0000269|PubMed:20421194}.
CC -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAS95534.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC098573; AAT44203.1; -; Genomic_DNA.
DR EMBL; AC134929; AAS16899.2; -; Genomic_DNA.
DR EMBL; AP008211; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP014961; BAS95534.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CM000142; EEE64831.1; -; Genomic_DNA.
DR EMBL; AK066579; BAG90037.1; -; mRNA.
DR RefSeq; XP_015639579.1; XM_015784093.1.
DR AlphaFoldDB; Q75HZ9; -.
DR SMR; Q75HZ9; -.
DR STRING; 4530.OS05T0582300-01; -.
DR PaxDb; Q75HZ9; -.
DR PRIDE; Q75HZ9; -.
DR KEGG; osa:107276142; -.
DR eggNOG; KOG0776; Eukaryota.
DR OrthoDB; 381154at2759; -.
DR BRENDA; 2.5.1.84; 4460.
DR PlantReactome; R-OSA-1119367; Polyisoprenoid biosynthesis.
DR Proteomes; UP000000763; Chromosome 5.
DR Proteomes; UP000007752; Chromosome 5.
DR Proteomes; UP000059680; Chromosome 5.
DR GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR GO; GO:0009536; C:plastid; IDA:CACAO.
DR GO; GO:0052923; F:all-trans-nonaprenyl-diphosphate synthase (geranyl-diphosphate specific) activity; IEA:UniProtKB-EC.
DR GO; GO:0004337; F:geranyltranstransferase 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 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; Transferase; Transit peptide.
FT TRANSIT 1..62
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 63..403
FT /note="Solanesyl-diphosphate synthase 2, chloroplastic"
FT /id="PRO_0000414852"
FT BINDING 123
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 126
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 161
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 168
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 168
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 172
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 172
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 177
FT /ligand="an all-trans-polyprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58914"
FT /evidence="ECO:0000250"
FT BINDING 178
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 254
FT /ligand="an all-trans-polyprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58914"
FT /evidence="ECO:0000250"
FT BINDING 255
FT /ligand="an all-trans-polyprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58914"
FT /evidence="ECO:0000250"
FT BINDING 292
FT /ligand="an all-trans-polyprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58914"
FT /evidence="ECO:0000250"
FT BINDING 309
FT /ligand="an all-trans-polyprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58914"
FT /evidence="ECO:0000250"
SQ SEQUENCE 403 AA; 44116 MW; 41C886646A8C04E4 CRC64;
MLSVSCPRVY MSRKALDFGQ LASCRCRWAG RSGMRVAPRR RMPCVCFVAS PSQPGLAAVD
VPAEAISSAR TTTMIPERIS VSSLLEVVSD DLLKLNNNLK SLVGAENPVL VSAAEQIFGA
GGKRLRPALV FLVSRATAEL AGLLELTTEH QRLAEIIEMI HTASLIHDDV IDDSGMRRGK
ETIHQLYGTR VAVLAGDFMF AQSSWFLANL ENIEVIKLIS QVIKDFASGE IKQASTLFDC
DVTLDDYLLK SYYKTASLLA SSTRSAAIFS GVSTTICEQM YEYGRNLGLS FQVVDDILDF
TQSAEQLGKP AGSDLAKGNL TAPVIFALQD EPKLREIIDS EFSESDSLAT AIDLVHRSGG
IRRAQELAKE KGDLALQNLQ CLPKSQFRST LENVVKYNLQ RID
