KPRS1_ARATH
ID KPRS1_ARATH Reviewed; 403 AA.
AC Q42581; Q67XL7; Q67YH7; Q84LR8; Q8GUH0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 21-NOV-2003, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Ribose-phosphate pyrophosphokinase 1, chloroplastic;
DE EC=2.7.6.1;
DE AltName: Full=PRS I;
DE AltName: Full=Phosphoribosyl pyrophosphate synthase 1;
DE Flags: Precursor;
GN Name=PRS1; OrderedLocusNames=At2g35390; ORFNames=T32F12.23;
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] (ISOFORM 1).
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).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=16244158; DOI=10.1104/pp.105.063479;
RA Xiao Y.-L., Smith S.R., Ishmael N., Redman J.C., Kumar N., Monaghan E.L.,
RA Ayele M., Haas B.J., Wu H.C., Town C.D.;
RT "Analysis of the cDNAs of hypothetical genes on Arabidopsis chromosome 2
RT reveals numerous transcript variants.";
RL Plant Physiol. 139:1323-1337(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Underwood B.A., Xiao Y.-L., Moskal W.A. Jr., Monaghan E.L., Wang W.,
RA Redman J.C., Wu H.C., Utterback T., Town C.D.;
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 41-403 (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=10082968; DOI=10.1016/s0167-4838(99)00022-9;
RA Krath B.N., Eriksen T.A., Poulsen T.S., Hove-Jensen B.;
RT "Cloning and sequencing of cDNAs specifying a novel class of phosphoribosyl
RT diphosphate synthase in Arabidopsis thaliana.";
RL Biochim. Biophys. Acta 1430:403-408(1999).
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=1;
CC IsoId=Q42581-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q42581-2; Sequence=VSP_013267;
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to an intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC36182.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAA58717.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AC005314; AAC36182.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC09103.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09104.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62892.1; -; Genomic_DNA.
DR EMBL; BT002515; AAO00875.1; -; mRNA.
DR EMBL; AY261787; AAP21681.1; -; mRNA.
DR EMBL; AK175326; BAD43089.1; -; mRNA.
DR EMBL; AK175885; BAD43648.1; -; mRNA.
DR EMBL; AK175907; BAD43670.1; -; mRNA.
DR EMBL; AK176491; BAD44254.1; -; mRNA.
DR EMBL; AK176555; BAD44318.1; -; mRNA.
DR EMBL; AK176801; BAD44564.1; -; mRNA.
DR EMBL; AY773861; AAV63890.1; -; mRNA.
DR EMBL; X83764; CAA58717.1; ALT_INIT; mRNA.
DR PIR; S51270; S51270.
DR RefSeq; NP_001325018.1; NM_001336555.1. [Q42581-2]
DR RefSeq; NP_181082.1; NM_129091.4. [Q42581-2]
DR RefSeq; NP_850244.1; NM_179913.3. [Q42581-1]
DR AlphaFoldDB; Q42581; -.
DR SMR; Q42581; -.
DR BioGRID; 3452; 34.
DR IntAct; Q42581; 1.
DR STRING; 3702.AT2G35390.2; -.
DR PaxDb; Q42581; -.
DR PRIDE; Q42581; -.
DR ProteomicsDB; 237048; -. [Q42581-1]
DR EnsemblPlants; AT2G35390.1; AT2G35390.1; AT2G35390. [Q42581-2]
DR EnsemblPlants; AT2G35390.2; AT2G35390.2; AT2G35390. [Q42581-1]
DR EnsemblPlants; AT2G35390.4; AT2G35390.4; AT2G35390. [Q42581-2]
DR GeneID; 818106; -.
DR Gramene; AT2G35390.1; AT2G35390.1; AT2G35390. [Q42581-2]
DR Gramene; AT2G35390.2; AT2G35390.2; AT2G35390. [Q42581-1]
DR Gramene; AT2G35390.4; AT2G35390.4; AT2G35390. [Q42581-2]
DR KEGG; ath:AT2G35390; -.
DR Araport; AT2G35390; -.
DR TAIR; locus:2062405; AT2G35390.
DR eggNOG; KOG1448; Eukaryota.
DR InParanoid; Q42581; -.
DR PhylomeDB; Q42581; -.
DR BioCyc; ARA:AT2G35390-MON; -.
DR PRO; PR:Q42581; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q42581; baseline and differential.
DR Genevisible; Q42581; AT.
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..49
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 50..403
FT /note="Ribose-phosphate pyrophosphokinase 1, chloroplastic"
FT /id="PRO_0000141092"
FT REGION 303..318
FT /note="Binding of phosphoribosylpyrophosphate"
FT /evidence="ECO:0000255"
FT BINDING 217
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT BINDING 219
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT BINDING 228
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT BINDING 232
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..51
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_013267"
FT CONFLICT 178
FT /note="I -> T (in Ref. 5; BAD44564)"
FT /evidence="ECO:0000305"
FT CONFLICT 194
FT /note="E -> K (in Ref. 3; AAO00875)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 403 AA; 43695 MW; B6BFA443773A8D90 CRC64;
MASLGLSFPP AAKTPTYLAS SSSTFFSNSS LSVRTSQFRS RNSVFACVKC DMPESLNVGN
GNPSIPIINE RTLPKFLESA RMEKSVNRTN TRLKLFSGTA NPALAQEIAW YMGLDLGKVN
IKRFADGEIY VQLQESVRGC DVYLVQPTCT PTNENLMELL IMVDACRRAS AKKVTAVIPY
FGYARADRKT QGRESIAAKL VANLITEAGA DRVLACDLHS GQSMGYFDIP VDHVYCQPVI
LDYLASKSIP SEDLVVVSPD VGGVARARAF AKKLSDAPLA IVDKRRSGHN VAEVMNLIGD
VRGKVAIMVD DMIDTAGTIV KGAALLHQEG AREVYACCTH AVFSPPAIER LSGGLLQEVI
VTNTLPVAEK NYFPQLTILS VANLLGETIW RVHDDSSVSS IFL
