KPRS2_ARATH
ID KPRS2_ARATH Reviewed; 400 AA.
AC Q42583; Q9LQM0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Ribose-phosphate pyrophosphokinase 2, chloroplastic;
DE EC=2.7.6.1;
DE AltName: Full=PRS II;
DE AltName: Full=Phosphoribosyl pyrophosphate synthase 2;
DE Flags: Precursor;
GN Name=PRS2; OrderedLocusNames=At1g32380; ORFNames=F5D14.15;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 89-400.
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 -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase family.
CC {ECO:0000305}.
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DR EMBL; AC007767; AAF81335.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31475.1; -; Genomic_DNA.
DR EMBL; AF439851; AAL27519.1; -; mRNA.
DR EMBL; AY125555; AAM78065.1; -; mRNA.
DR EMBL; X92974; CAA63552.1; -; mRNA.
DR PIR; G86448; G86448.
DR PIR; S71262; S71262.
DR RefSeq; NP_174516.1; NM_102972.3.
DR AlphaFoldDB; Q42583; -.
DR SMR; Q42583; -.
DR BioGRID; 25365; 37.
DR IntAct; Q42583; 5.
DR STRING; 3702.AT1G32380.1; -.
DR PaxDb; Q42583; -.
DR PRIDE; Q42583; -.
DR ProteomicsDB; 237139; -.
DR EnsemblPlants; AT1G32380.1; AT1G32380.1; AT1G32380.
DR GeneID; 840131; -.
DR Gramene; AT1G32380.1; AT1G32380.1; AT1G32380.
DR KEGG; ath:AT1G32380; -.
DR Araport; AT1G32380; -.
DR TAIR; locus:2033792; AT1G32380.
DR eggNOG; KOG1448; Eukaryota.
DR HOGENOM; CLU_033546_1_0_1; -.
DR InParanoid; Q42583; -.
DR OrthoDB; 1043963at2759; -.
DR PhylomeDB; Q42583; -.
DR BioCyc; ARA:AT1G32380-MON; -.
DR PRO; PR:Q42583; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q42583; baseline and differential.
DR Genevisible; Q42583; 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 ATP-binding; Chloroplast; Kinase; Magnesium; Metal-binding;
KW Nucleotide biosynthesis; Nucleotide-binding; Plastid; Reference proteome;
KW Transferase; Transit peptide.
FT TRANSIT 1..44
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 45..400
FT /note="Ribose-phosphate pyrophosphokinase 2, chloroplastic"
FT /id="PRO_0000141093"
FT REGION 300..315
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:0000255"
FT BINDING 216
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT BINDING 225
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT BINDING 229
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
SQ SEQUENCE 400 AA; 43333 MW; A0BCCA950296E1BF CRC64;
MASLALTSPP SVKIPSYLSS SSSSLFSRSS ISFRTTESRS RICVSGYAKC NLPKALNGNA
RVPIINETTI PKFFDSSRLE KSVSRNNTKL KLFSGTANPA LSQEIAWYMG LELGKVSIKR
FADGEIYVQL KESVRGCDVF LVQPTCTPTN ENLMELLIMV DACRRASAKK VTAVIPYFGY
ARADRKTQGR ESIAAKLVAN LITEAGADRV LACDLHSGQS MGYFDIPVDH VYCQPVILDY
LASKSISSED LVVVSPDVGG VARARAFAKK LSDAPLAIVD KRRHGHNVAE VMNLIGDVKG
KVAVMVDDII DTAGTIVKGA ALLHEEGARE VYACCTHAVF SPPAIERLSS GLLQEVIVTN
TLPVAEKNYF PQLTILSVAN LLGETIWRVH DDSSVSSIFL
