KPRS5_ARATH
ID KPRS5_ARATH Reviewed; 394 AA.
AC O64888; Q8L7T8;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Ribose-phosphate pyrophosphokinase 5, chloroplastic;
DE EC=2.7.6.1;
DE AltName: Full=Phosphoribosyl pyrophosphate synthase 5;
DE Flags: Precursor;
GN Name=PRS5; OrderedLocusNames=At2g44530; ORFNames=F16B22.2;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(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 -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=O64888-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC27455.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAM14963.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC003672; AAC27455.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC004521; AAM14963.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC10434.1; -; Genomic_DNA.
DR EMBL; AY127024; AAM83248.1; -; mRNA.
DR EMBL; BT001041; AAN46795.1; -; mRNA.
DR PIR; T02409; T02409.
DR RefSeq; NP_181981.2; NM_130017.5. [O64888-1]
DR AlphaFoldDB; O64888; -.
DR SMR; O64888; -.
DR BioGRID; 4397; 34.
DR IntAct; O64888; 1.
DR STRING; 3702.AT2G44530.1; -.
DR iPTMnet; O64888; -.
DR PaxDb; O64888; -.
DR EnsemblPlants; AT2G44530.1; AT2G44530.1; AT2G44530. [O64888-1]
DR GeneID; 819061; -.
DR Gramene; AT2G44530.1; AT2G44530.1; AT2G44530. [O64888-1]
DR KEGG; ath:AT2G44530; -.
DR Araport; AT2G44530; -.
DR TAIR; locus:2042351; AT2G44530.
DR eggNOG; KOG1448; Eukaryota.
DR InParanoid; O64888; -.
DR PhylomeDB; O64888; -.
DR BioCyc; ARA:AT2G44530-MON; -.
DR PRO; PR:O64888; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O64888; baseline and differential.
DR Genevisible; O64888; AT.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
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..33
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 34..394
FT /note="Ribose-phosphate pyrophosphokinase 5, chloroplastic"
FT /id="PRO_0000141096"
FT REGION 288..303
FT /note="Binding of phosphoribosylpyrophosphate"
FT /evidence="ECO:0000255"
FT BINDING 202
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT BINDING 204
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT BINDING 213
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT BINDING 217
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
SQ SEQUENCE 394 AA; 42625 MW; 022EFEF64AF12D60 CRC64;
MASIVQPSPT FPALNLRRSS LIRPPSSVRF PLKCNAADPY KFDGGNSAGF HLLTGDTVPA
SFSRTRLEDS IYQNTTRLRI FSGTANPILA QEISCYLGLD LGKIKIKRFA DGEIYVQLQE
SVRGCDVFLV QPTCPPANEN LMELLVMIDA CRRASAKTIT AVIPYFGYAR ADRKTQGRES
IAAKLVANLI TQSGADRVLA CDLHSGQSMG YFDIPVDHVY GQPVILDYLA SKAISSEDLV
VVSPDVGGVA RARAFAKKLS DAPLAIVDKR RHGHNVAEVM NLIGDVKGKV AIMVDDMIDT
AGTISKGAAL LHQEGAREVY ACTTHAVFSP PAISRLSSGL FQEVIITNTI PLSEKNYFPQ
LTVLSVANLL GETIWRVHDD CSGAIEPFST LGID
