UKL2_ARATH
ID UKL2_ARATH Reviewed; 483 AA.
AC Q9LK34;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Uridine/cytidine kinase UKL1, chloroplastic {ECO:0000305};
DE EC=2.7.1.48 {ECO:0000269|PubMed:21828290, ECO:0000269|PubMed:31101721, ECO:0000269|PubMed:31907295};
DE AltName: Full=Uridine kinase-like protein 2 {ECO:0000303|PubMed:19563437};
DE AltName: Full=Uridine/cytidine kinase 2 {ECO:0000303|PubMed:31101721};
DE Flags: Precursor;
GN Name=UKL2 {ECO:0000303|PubMed:19563437};
GN Synonyms=UCK2 {ECO:0000303|PubMed:31101721};
GN OrderedLocusNames=At3g27190 {ECO:0000312|Araport:AT3G27190};
GN ORFNames=K17E12.1 {ECO:0000312|EMBL:BAB02114.1};
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=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(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].
RA Cheuk R., Chen H., Kim C.J., Shinn P., Carninci P., Hayashizaki Y.,
RA Ishida J., Kamiya A., Kawai J., Narusaka M., Sakurai T., Satou M., Seki M.,
RA Shinozaki K., Ecker J.R.;
RT "Arabidopsis cDNA clones.";
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP FUNCTION, DISRUPTION PHENOTYPE, GENE FAMILY, AND 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 [6]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=21828290; DOI=10.1105/tpc.111.085829;
RA Chen M., Thelen J.J.;
RT "Plastid uridine salvage activity is required for photoassimilate
RT allocation and partitioning in Arabidopsis.";
RL Plant Cell 23:2991-3006(2011).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=31101721; DOI=10.1104/pp.19.00329;
RA Ohler L., Niopek-Witz S., Mainguet S.E., Moehlmann T.;
RT "Pyrimidine salvage: physiological functions and interaction with
RT chloroplast biogenesis.";
RL Plant Physiol. 180:1816-1828(2019).
RN [8]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=31907295; DOI=10.1105/tpc.19.00639;
RA Chen M., Witte C.P.;
RT "A kinase and a glycosylase catabolize pseudouridine in the peroxisome to
RT prevent toxic pseudouridine monophosphate accumulation.";
RL Plant Cell 32:722-739(2020).
CC -!- FUNCTION: Involved in the pyrimidine salvage pathway (PubMed:21828290,
CC PubMed:31101721, PubMed:31907295). Phosphorylates uridine to uridine
CC monophosphate (UMP) (PubMed:21828290, PubMed:31101721,
CC PubMed:31907295). Phosphorylates cytidine to cytidine monophosphate
CC (CMP) (PubMed:31101721). Does not possess uracil
CC phosphoribosyltransferase (UPRTase) activity that catalyzes the
CC conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP)
CC to UMP and diphosphate (PubMed:19563437, PubMed:21828290,
CC PubMed:31101721). {ECO:0000269|PubMed:19563437,
CC ECO:0000269|PubMed:21828290, ECO:0000269|PubMed:31101721,
CC ECO:0000269|PubMed:31907295}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + cytidine = ADP + CMP + H(+); Xref=Rhea:RHEA:24674,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17562, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:60377, ChEBI:CHEBI:456216; EC=2.7.1.48;
CC Evidence={ECO:0000269|PubMed:31101721};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24675;
CC Evidence={ECO:0000269|PubMed:31101721};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + uridine = ADP + H(+) + UMP; Xref=Rhea:RHEA:16825,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16704, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57865, ChEBI:CHEBI:456216; EC=2.7.1.48;
CC Evidence={ECO:0000269|PubMed:21828290, ECO:0000269|PubMed:31101721,
CC ECO:0000269|PubMed:31907295};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16826;
CC Evidence={ECO:0000269|PubMed:21828290, ECO:0000269|PubMed:31101721,
CC ECO:0000269|PubMed:31907295};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.16 uM for cytidine {ECO:0000269|PubMed:31101721};
CC KM=1.18 uM for uridine {ECO:0000269|PubMed:21828290};
CC Vmax=2.01 umol/h/mg enzyme with cytidine as substrate
CC {ECO:0000269|PubMed:31101721};
CC Vmax=243.9 umol/h/mg enzyme with uridine as substrate
CC {ECO:0000269|PubMed:21828290};
CC -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via salvage pathway;
CC CTP from cytidine: step 1/3. {ECO:0000305}.
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage pathway;
CC UMP from uridine: step 1/1. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:21828290}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype (PubMed:19563437). No
CC decrease in uracil phosphoribosyltransferase activity
CC (PubMed:19563437). Loss of sensitivity to 5'-fluorouracil and 5'-
CC fluorouridine (PubMed:21828290). {ECO:0000269|PubMed:19563437,
CC ECO:0000269|PubMed:21828290}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the uridine kinase
CC family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the UPRTase family.
CC {ECO:0000305}.
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DR EMBL; AP000381; BAB02114.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77277.1; -; Genomic_DNA.
DR EMBL; BT010743; AAR23713.1; -; mRNA.
DR EMBL; AK175542; BAD43305.1; -; mRNA.
DR RefSeq; NP_189355.1; NM_113633.6.
DR AlphaFoldDB; Q9LK34; -.
DR SMR; Q9LK34; -.
DR BioGRID; 7668; 3.
DR STRING; 3702.AT3G27190.1; -.
DR iPTMnet; Q9LK34; -.
DR PaxDb; Q9LK34; -.
DR PRIDE; Q9LK34; -.
DR ProteomicsDB; 245304; -.
DR EnsemblPlants; AT3G27190.1; AT3G27190.1; AT3G27190.
DR GeneID; 822338; -.
DR Gramene; AT3G27190.1; AT3G27190.1; AT3G27190.
DR KEGG; ath:AT3G27190; -.
DR Araport; AT3G27190; -.
DR TAIR; locus:2086523; AT3G27190.
DR eggNOG; KOG4203; Eukaryota.
DR HOGENOM; CLU_021278_0_3_1; -.
DR InParanoid; Q9LK34; -.
DR OMA; DQCLNEE; -.
DR OrthoDB; 929897at2759; -.
DR PhylomeDB; Q9LK34; -.
DR BioCyc; ARA:AT3G27190-MON; -.
DR UniPathway; UPA00574; UER00637.
DR UniPathway; UPA00579; UER00640.
DR PRO; PR:Q9LK34; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LK34; baseline and differential.
DR Genevisible; Q9LK34; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0004849; F:uridine kinase activity; IDA:TAIR.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IMP:TAIR.
DR GO; GO:0044211; P:CTP salvage; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:2001006; P:regulation of cellulose biosynthetic process; IMP:TAIR.
DR GO; GO:1901141; P:regulation of lignin biosynthetic process; IMP:TAIR.
DR GO; GO:2000904; P:regulation of starch metabolic process; IMP:TAIR.
DR GO; GO:0044206; P:UMP salvage; IDA:TAIR.
DR CDD; cd06223; PRTases_typeI; 1.
DR CDD; cd02023; UMPK; 1.
DR Gene3D; 3.40.50.2020; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000836; PRibTrfase_dom.
DR InterPro; IPR006083; PRK/URK.
DR InterPro; IPR029057; PRTase-like.
DR InterPro; IPR029930; UCKL1_plant.
DR InterPro; IPR000764; Uridine_kinase-like.
DR PANTHER; PTHR10285:SF142; PTHR10285:SF142; 1.
DR Pfam; PF00485; PRK; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF53271; SSF53271; 1.
DR TIGRFAMs; TIGR00235; udk; 1.
PE 1: Evidence at protein level;
KW Allosteric enzyme; Chloroplast; Glycosyltransferase; GTP-binding; Kinase;
KW Multifunctional enzyme; Nucleotide-binding; Plastid; Reference proteome;
KW Transferase; Transit peptide.
FT TRANSIT 1..47
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 48..483
FT /note="Uridine/cytidine kinase UKL1, chloroplastic"
FT /id="PRO_0000394515"
FT REGION 59..264
FT /note="Uridine kinase"
FT /evidence="ECO:0000250"
FT REGION 274..483
FT /note="Uracil phosphoribosyltransferase"
FT /evidence="ECO:0000250"
FT BINDING 298
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 307
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 341..344
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 351
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000250"
FT BINDING 376
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000250"
FT BINDING 396
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 402
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000250"
FT BINDING 407..410
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000250"
FT BINDING 472..474
FT /ligand="uracil"
FT /ligand_id="ChEBI:CHEBI:17568"
FT /evidence="ECO:0000250"
FT BINDING 473
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000250"
SQ SEQUENCE 483 AA; 54210 MW; 2862F7AED187020F CRC64;
MPEDSTAIDY VMEKASGPHF SGLRLDGLLS SPSKSSVSSP SHFRLSNSSF SATDDPAAPH
QPFVIGVTGG TASGKTTVCD MIIQQLHDHR IVLVNQDSFY RGLTSEELEH VQEYNFDHPD
AFDTEQLLHC VDILKSGQPY QIPIYDFKTH QRKVDAFRQV NACDVIILEG ILVFHDSRVR
DLMNMKIFVD TDADVRLARR IRRDTVERGR DVDSVLEQYA KFVKPAFDDF VLPSKKYADV
IIPRGGDNHV AVDLIVQHIH TKLGQHDLCK IYPNVFVIET TFQIRGMHTL IREKDISKHD
FVFYSDRLIR LVVEHGLGHL PFTEKQVVTP TGSVYSGVDF CKKLCGVSVI RSGESMENAL
RACCKGIKIG KILIHRDGDN GMQLIYEKLP SDISERHVLL LDPVLGTGNS ANQAIELLIQ
KGVPEAHIIF LNLISAPEGI HCVCKRFPKL KIVTSEIDQC LNEEFRVIPG LGEFGDRYFG
TDE
