KPRS2_ORYSJ
ID KPRS2_ORYSJ Reviewed; 399 AA.
AC Q69XQ6; Q69XQ7;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 2.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Ribose-phosphate pyrophosphokinase 2, chloroplastic;
DE EC=2.7.6.1;
DE AltName: Full=Phosphoribosyl pyrophosphate synthase 2;
DE Flags: Precursor;
GN OrderedLocusNames=Os06g0617800, LOC_Os06g41360;
GN ORFNames=P0012B02.3-1, P0012B02.3-2;
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=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=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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-ribose 5-phosphate = 5-phospho-alpha-D-ribose 1-
CC diphosphate + AMP + H(+); Xref=Rhea:RHEA:15609, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58017, ChEBI:CHEBI:78346,
CC ChEBI:CHEBI:456215; EC=2.7.6.1;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=2;
CC IsoId=Q69XQ6-1; Sequence=Displayed;
CC Name=1;
CC IsoId=Q69XQ6-2; Sequence=VSP_013704;
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to an intron retention.
CC -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD35420.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP003609; BAD35420.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP003609; BAD35421.1; -; Genomic_DNA.
DR EMBL; AP014962; BAS98633.1; -; Genomic_DNA.
DR EMBL; AK065878; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK067505; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK068485; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_015644180.1; XM_015788694.1. [Q69XQ6-1]
DR AlphaFoldDB; Q69XQ6; -.
DR SMR; Q69XQ6; -.
DR STRING; 4530.OS06T0617800-01; -.
DR PaxDb; Q69XQ6; -.
DR PRIDE; Q69XQ6; -.
DR EnsemblPlants; Os06t0617800-01; Os06t0617800-01; Os06g0617800. [Q69XQ6-2]
DR EnsemblPlants; Os06t0617800-02; Os06t0617800-02; Os06g0617800. [Q69XQ6-2]
DR EnsemblPlants; Os06t0617800-03; Os06t0617800-03; Os06g0617800. [Q69XQ6-2]
DR GeneID; 4341535; -.
DR Gramene; Os06t0617800-01; Os06t0617800-01; Os06g0617800. [Q69XQ6-2]
DR Gramene; Os06t0617800-02; Os06t0617800-02; Os06g0617800. [Q69XQ6-2]
DR Gramene; Os06t0617800-03; Os06t0617800-03; Os06g0617800. [Q69XQ6-2]
DR KEGG; osa:4341535; -.
DR eggNOG; KOG1448; Eukaryota.
DR InParanoid; Q69XQ6; -.
DR OrthoDB; 1043963at2759; -.
DR PlantReactome; R-OSA-1119278; PRPP biosynthesis I.
DR Proteomes; UP000000763; Chromosome 6.
DR Proteomes; UP000059680; Chromosome 6.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0002189; C:ribose phosphate diphosphokinase complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004749; F:ribose phosphate diphosphokinase activity; IBA:GO_Central.
DR GO; GO:0006015; P:5-phosphoribose 1-diphosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IBA:GO_Central.
DR GO; GO:0009156; P:ribonucleoside monophosphate biosynthetic process; IEA:InterPro.
DR CDD; cd06223; PRTases_typeI; 1.
DR Gene3D; 3.40.50.2020; -; 2.
DR HAMAP; MF_00583_B; RibP_PPkinase_B; 1.
DR InterPro; IPR000842; PRib_PP_synth_CS.
DR InterPro; IPR029099; Pribosyltran_N.
DR InterPro; IPR000836; PRibTrfase_dom.
DR InterPro; IPR029057; PRTase-like.
DR InterPro; IPR005946; Rib-P_diPkinase.
DR InterPro; IPR037515; Rib-P_diPkinase_bac.
DR PANTHER; PTHR10210; PTHR10210; 1.
DR Pfam; PF14572; Pribosyl_synth; 1.
DR Pfam; PF13793; Pribosyltran_N; 1.
DR SUPFAM; SSF53271; SSF53271; 1.
DR TIGRFAMs; TIGR01251; ribP_PPkin; 1.
DR PROSITE; PS00114; PRPP_SYNTHASE; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Chloroplast; Kinase; Magnesium;
KW Metal-binding; Nucleotide biosynthesis; Nucleotide-binding; Plastid;
KW Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..32
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 33..399
FT /note="Ribose-phosphate pyrophosphokinase 2, chloroplastic"
FT /id="PRO_0000141098"
FT REGION 299..314
FT /note="Binding of phosphoribosylpyrophosphate"
FT /evidence="ECO:0000255"
FT BINDING 214
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 216
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 225
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 229
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT VAR_SEQ 340..399
FT /note="SPPAIERLSGGIFEEVIVTNSILLPEHKCFPQLTVLSMANLVAETIWHVHRD
FT GSVSSIFQ -> RFGSWFIVTSMIHVIVLIHWLVAKEPCYGMIRQIGFMFDQYKNDRVE
FT Q (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:12869764"
FT /id="VSP_013704"
SQ SEQUENCE 399 AA; 43086 MW; 275952D85DB19C06 CRC64;
MAAKAAALSS SPFVSSRRLS SPAASLRART PRCVMGSEQV RVVVEEEGKT KKRMGVAEPR
SAPPAVWTPR APAQEARLAA LRTDGRDSRL KIFSGTANRP LAQEIASYLG VDLGKVLIKR
FADGEIYVQL QESVRGCDVF LVQPTCSPVN ENLMELFVMI DACRRASARS ITVVIPYFGY
ARADRKAQGR EAITAKLSAN LLTEAGSDRV IVCDIHSTQA LGYFDIPVDH IHGQPVILDY
LASKTISKDL VVVSPDVGGV VRARAFAKKL SDAPLAIVDK RRQGHNMSEV MHLIGDVKGK
VAIMVDDMID TAGTITSAAA LLKQEGAEAV YACSTHAVFS PPAIERLSGG IFEEVIVTNS
ILLPEHKCFP QLTVLSMANL VAETIWHVHR DGSVSSIFQ
