KPRS4_ARATH
ID KPRS4_ARATH Reviewed; 337 AA.
AC Q680A5; Q9S7B9;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Ribose-phosphate pyrophosphokinase 4;
DE EC=2.7.6.1;
DE AltName: Full=Phosphoribosyl pyrophosphate synthase 4;
GN Name=PRS4; OrderedLocusNames=At2g42910; ORFNames=F23E6.7, F7D19.9;
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 [MRNA].
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).
RN [2]
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 [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 246-337.
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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
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 -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase family.
CC {ECO:0000305}.
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DR EMBL; AJ012407; CAB43553.1; -; mRNA.
DR EMBL; AC006580; AAM15296.1; -; Genomic_DNA.
DR EMBL; AC006931; AAD21718.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10186.1; -; Genomic_DNA.
DR EMBL; AY128402; AAM91605.1; -; mRNA.
DR EMBL; BT000083; AAN15402.1; -; mRNA.
DR EMBL; AY087406; AAM64955.1; -; mRNA.
DR EMBL; AK175962; BAD43725.1; -; mRNA.
DR PIR; T52589; T52589.
DR RefSeq; NP_181819.1; NM_129852.3.
DR AlphaFoldDB; Q680A5; -.
DR SMR; Q680A5; -.
DR BioGRID; 4229; 4.
DR IntAct; Q680A5; 1.
DR STRING; 3702.AT2G42910.1; -.
DR iPTMnet; Q680A5; -.
DR PaxDb; Q680A5; -.
DR PRIDE; Q680A5; -.
DR ProteomicsDB; 237164; -.
DR EnsemblPlants; AT2G42910.1; AT2G42910.1; AT2G42910.
DR GeneID; 818892; -.
DR Gramene; AT2G42910.1; AT2G42910.1; AT2G42910.
DR KEGG; ath:AT2G42910; -.
DR Araport; AT2G42910; -.
DR TAIR; locus:2045590; AT2G42910.
DR eggNOG; KOG1448; Eukaryota.
DR HOGENOM; CLU_048814_0_0_1; -.
DR InParanoid; Q680A5; -.
DR OMA; DSDCIHL; -.
DR OrthoDB; 893352at2759; -.
DR PhylomeDB; Q680A5; -.
DR BioCyc; ARA:AT2G42910-MON; -.
DR PRO; PR:Q680A5; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q680A5; baseline and differential.
DR Genevisible; Q680A5; AT.
DR GO; GO:0005737; C:cytoplasm; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; 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; 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; 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 SUPFAM; SSF53271; SSF53271; 2.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Kinase; Magnesium; Metal-binding;
KW Nucleotide biosynthesis; Nucleotide-binding; Reference proteome;
KW Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..337
FT /note="Ribose-phosphate pyrophosphokinase 4"
FT /id="PRO_0000141095"
FT REGION 241..256
FT /note="Binding of phosphoribosylpyrophosphate"
FT /evidence="ECO:0000255"
FT BINDING 158
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT BINDING 160
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CONFLICT 293
FT /note="K -> R (in Ref. 6; BAD43725)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 337 AA; 37560 MW; AF17B157D3B70022 CRC64;
MSENAANNIM ETKICTDAIV SELQKKKVHL FYCLECEELA RNIAAESDHI TLQSINWRSF
ADGFPNLFIN NAHDIRGQHV AFLASFSSPA VIFEQISVIY LLPRLFVASF TLVLPFFPTG
SFERMEEEGD VATAFTMARI VSNIPISRGG PTSVVIYDIH ALQERFYFAD QVLPLFETGI
PLLTKRLQQL PETEKVIVAF PDDGAWKRFH KLLDHYPTVV CTKVREGDKR IVRLKEGNPA
GCHVVIVDDL VQSGGTLIEC QKVLAAHGAV KVSAYVTHGV FPKSSWERFT HKKNGLEEAF
AYFWITDSCP QTVKAIGNKA PFEVLSLAGS IADALQI
