UPP_ARATH
ID UPP_ARATH Reviewed; 296 AA.
AC Q9M336; Q3EAK0; Q8LFM4;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Uracil phosphoribosyltransferase, chloroplastic;
DE Short=UPRTase;
DE EC=2.4.2.9 {ECO:0000269|PubMed:19563437};
DE AltName: Full=UMP pyrophosphorylase;
DE Flags: Precursor;
GN Name=UPP; Synonyms=PYRR; OrderedLocusNames=At3g53900; ORFNames=F5K20.200;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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] (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).
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 [5]
RP DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=19413687; DOI=10.1111/j.1469-8137.2009.02843.x;
RA Zrenner R., Riegler H., Marquard C.R., Lange P.R., Geserick C.,
RA Bartosz C.E., Chen C.T., Slocum R.D.;
RT "A functional analysis of the pyrimidine catabolic pathway in
RT Arabidopsis.";
RL New Phytol. 183:117-132(2009).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, GENE FAMILY, AND
RP NOMENCLATURE.
RX PubMed=19563437; DOI=10.1111/j.1365-313x.2009.03963.x;
RA Mainguet S.E., Gakiere B., Majira A., Pelletier S., Bringel F., Guerard F.,
RA Caboche M., Berthome R., Renou J.P.;
RT "Uracil salvage is necessary for early Arabidopsis development.";
RL Plant J. 60:280-291(2009).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 (ISOFORM 2), CLEAVAGE OF
RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM 2), AND IDENTIFICATION
RP BY MASS SPECTROMETRY [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 -!- FUNCTION: Uracil phosphoribosyltransferase (UPRT) that catalyzes the
CC conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP)
CC to UMP and diphosphate. Is probably the only functional UPRT, since the
CC dual-domain proteins of the UKL family seem to lack this activity.
CC {ECO:0000269|PubMed:19563437}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=diphosphate + UMP = 5-phospho-alpha-D-ribose 1-diphosphate +
CC uracil; Xref=Rhea:RHEA:13017, ChEBI:CHEBI:17568, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57865, ChEBI:CHEBI:58017; EC=2.4.2.9;
CC Evidence={ECO:0000269|PubMed:19563437};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:13019;
CC Evidence={ECO:0000305|PubMed:19563437};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. The magnesium is bound as Mg-PRPP.
CC {ECO:0000250};
CC -!- ACTIVITY REGULATION: Allosterically activated by GTP. {ECO:0000250}.
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage pathway;
CC UMP from uracil: step 1/1.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9M336-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9M336-2; Sequence=VSP_039281;
CC -!- DEVELOPMENTAL STAGE: Slightly induced 12 days after germination.
CC {ECO:0000269|PubMed:19413687}.
CC -!- INDUCTION: Up-regulated when pyrimidine catabolism is impaired.
CC {ECO:0000269|PubMed:19413687}.
CC -!- DOMAIN: The N-terminal sequence (1-125) is sufficient to address
CC heterologous proteins to chloroplasts.
CC -!- DISRUPTION PHENOTYPE: Growth retardation, pale-green to albino
CC phenotype and flimsy roots with less branching. Loss of uracil
CC phosphoribosyltransferase activity. {ECO:0000269|PubMed:19563437}.
CC -!- SIMILARITY: Belongs to the UPRTase family. {ECO:0000305}.
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DR EMBL; AL132960; CAB88352.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79156.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79157.1; -; Genomic_DNA.
DR EMBL; AY056189; AAL07038.1; -; mRNA.
DR EMBL; AY113998; AAM45046.1; -; mRNA.
DR EMBL; AY084756; AAM61325.1; -; mRNA.
DR PIR; T45930; T45930.
DR RefSeq; NP_190958.1; NM_115250.3. [Q9M336-1]
DR RefSeq; NP_850699.1; NM_180368.2. [Q9M336-2]
DR AlphaFoldDB; Q9M336; -.
DR SMR; Q9M336; -.
DR BioGRID; 9874; 14.
DR IntAct; Q9M336; 14.
DR STRING; 3702.AT3G53900.2; -.
DR PaxDb; Q9M336; -.
DR PRIDE; Q9M336; -.
DR ProteomicsDB; 228537; -. [Q9M336-1]
DR EnsemblPlants; AT3G53900.1; AT3G53900.1; AT3G53900. [Q9M336-2]
DR EnsemblPlants; AT3G53900.2; AT3G53900.2; AT3G53900. [Q9M336-1]
DR GeneID; 824557; -.
DR Gramene; AT3G53900.1; AT3G53900.1; AT3G53900. [Q9M336-2]
DR Gramene; AT3G53900.2; AT3G53900.2; AT3G53900. [Q9M336-1]
DR KEGG; ath:AT3G53900; -.
DR Araport; AT3G53900; -.
DR TAIR; locus:2084385; AT3G53900.
DR eggNOG; KOG4203; Eukaryota.
DR HOGENOM; CLU_067096_0_0_1; -.
DR InParanoid; Q9M336; -.
DR PhylomeDB; Q9M336; -.
DR BioCyc; ARA:AT3G53900-MON; -.
DR BioCyc; MetaCyc:AT3G53900-MON; -.
DR BRENDA; 2.4.2.9; 399.
DR UniPathway; UPA00574; UER00636.
DR PRO; PR:Q9M336; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M336; baseline and differential.
DR Genevisible; Q9M336; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0009536; C:plastid; IDA:TAIR.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0004845; F:uracil phosphoribosyltransferase activity; IMP:TAIR.
DR GO; GO:0016036; P:cellular response to phosphate starvation; IEP:TAIR.
DR GO; GO:0032502; P:developmental process; IMP:TAIR.
DR GO; GO:0044206; P:UMP salvage; IEA:UniProtKB-UniPathway.
DR GO; GO:0006223; P:uracil salvage; IEA:InterPro.
DR CDD; cd06223; PRTases_typeI; 1.
DR Gene3D; 3.40.50.2020; -; 1.
DR InterPro; IPR000836; PRibTrfase_dom.
DR InterPro; IPR029057; PRTase-like.
DR InterPro; IPR005765; Ura_phspho_trans.
DR SUPFAM; SSF53271; SSF53271; 1.
DR TIGRFAMs; TIGR01091; upp; 1.
PE 1: Evidence at protein level;
KW Acetylation; Allosteric enzyme; Alternative splicing; Chloroplast;
KW Glycosyltransferase; GTP-binding; Nucleotide-binding; Plastid;
KW Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..61
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 62..296
FT /note="Uracil phosphoribosyltransferase, chloroplastic"
FT /id="PRO_0000394518"
FT BINDING 148..151
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 158
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000250"
FT BINDING 183
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000250"
FT BINDING 211
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000250"
FT BINDING 216..219
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000250"
FT BINDING 281..283
FT /ligand="uracil"
FT /ligand_id="ChEBI:CHEBI:17568"
FT /evidence="ECO:0000250"
FT BINDING 282
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..65
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_039281"
FT INIT_MET Q9M336-2:1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES Q9M336-2:2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 296 AA; 32195 MW; 3961CEFEC086034F CRC64;
MACSIGNAFR CSSDTLRFAP RQQCSSRLNP NPSSFLSFNS SPILAQNLGA SSSSLSRRTI
RARTKMAASE ASINGSNRML VFVPPHPLIK HWISVLRNEQ TPCPVFRNAI AELGRLLMYE
ASREWLPTVV GEIMSPMGPA SVEFIDPREP IAVVPILRAG LALAEHASSV LPANKIYHLG
VSRDEKTLLP SVYLNKLPDE FPKNSRVFLV DPVLATGGTI MAAMDLLKER GLSVQQIKVI
CAIAAPPALS KLNEKFPGLH VYAGIIDPEV NEKGYIIPGL GDAGDRSFGT ETHWVK
