KPRS3_ARATH
ID KPRS3_ARATH Reviewed; 411 AA.
AC Q93Z66; Q9SAD2; Q9SGY0; Q9XFR3;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Ribose-phosphate pyrophosphokinase 3, chloroplastic;
DE EC=2.7.6.1;
DE AltName: Full=Phosphoribosyl pyrophosphate synthase 3;
DE Flags: Precursor;
GN Name=PRS3; OrderedLocusNames=At1g10700; ORFNames=F20B24.13, T16B5.16;
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 42-411.
RC STRAIN=cv. Columbia; TISSUE=Leaf;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD31343.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAF17658.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB43552.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AC007354; AAD31343.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC009398; AAF17658.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28630.1; -; Genomic_DNA.
DR EMBL; AY058091; AAL24199.1; -; mRNA.
DR EMBL; AY090310; AAL90971.1; -; mRNA.
DR EMBL; AJ012406; CAB43552.1; ALT_INIT; mRNA.
DR PIR; D86240; D86240.
DR PIR; T52591; T52591.
DR RefSeq; NP_172540.1; NM_100946.3.
DR AlphaFoldDB; Q93Z66; -.
DR SMR; Q93Z66; -.
DR BioGRID; 22853; 2.
DR STRING; 3702.AT1G10700.1; -.
DR PaxDb; Q93Z66; -.
DR PRIDE; Q93Z66; -.
DR ProteomicsDB; 250759; -.
DR EnsemblPlants; AT1G10700.1; AT1G10700.1; AT1G10700.
DR GeneID; 837613; -.
DR Gramene; AT1G10700.1; AT1G10700.1; AT1G10700.
DR KEGG; ath:AT1G10700; -.
DR Araport; AT1G10700; -.
DR TAIR; locus:2019973; AT1G10700.
DR eggNOG; KOG1448; Eukaryota.
DR HOGENOM; CLU_048814_1_0_1; -.
DR InParanoid; Q93Z66; -.
DR OMA; ENFWITD; -.
DR OrthoDB; 893352at2759; -.
DR PhylomeDB; Q93Z66; -.
DR BioCyc; ARA:AT1G10700-MON; -.
DR PRO; PR:Q93Z66; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q93Z66; baseline and differential.
DR Genevisible; Q93Z66; 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; IEA:UniProtKB-EC.
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 CDD; cd06223; PRTases_typeI; 1.
DR Gene3D; 3.40.50.2020; -; 2.
DR InterPro; IPR029099; Pribosyltran_N.
DR InterPro; IPR000836; PRibTrfase_dom.
DR InterPro; IPR029057; PRTase-like.
DR InterPro; IPR005946; Rib-P_diPkinase.
DR PANTHER; PTHR10210; PTHR10210; 1.
DR Pfam; PF00156; Pribosyltran; 1.
DR Pfam; PF13793; Pribosyltran_N; 1.
DR SUPFAM; SSF53271; SSF53271; 2.
DR TIGRFAMs; TIGR01251; ribP_PPkin; 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..39
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 40..411
FT /note="Ribose-phosphate pyrophosphokinase 3, chloroplastic"
FT /id="PRO_0000141094"
FT REGION 314..329
FT /note="Binding of phosphoribosylpyrophosphate"
FT /evidence="ECO:0000255"
FT BINDING 231
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT BINDING 233
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
SQ SEQUENCE 411 AA; 44697 MW; 606F5C00AE98E007 CRC64;
MAAISPANAT TAASLSLPQF SSTSSSLSSS SSPSFLNFKT ASVSNRCIKC GVRSLENHSG
HRSLDFLSNG DPISLINPNS SSPITMAAAT SESGSKSSKR VCLFHSDETR DLAERIVAKS
DCIELRSINW KKFDDGFPNL FIQNAQGIRG QHVAFLASFS SPAVIFEQLS VIYALPKLFV
SSFTLVLPFF PTGTSERMED EGDVATAFTL ARILSNIPTS RGGPTSLVTF DIHALQERFY
FGDTILPCFE SGIPLLKSRL QSLPDSDNIS IAFPDDGAWK RFHKQLQHYP TIVCNKVRMG
DKRIVRIKEG DAEGRHVVIV DDLVQSGGTL IECQKVLAAH GAAKISAYVT HGIFPRSSWK
RFKLDTKGDP AEGLSYFWIT DSCGMTVKEV MNKPPFEVLS LAGSIASALQ V
