UKL3_ARATH
ID UKL3_ARATH Reviewed; 466 AA.
AC Q8VYB2; A8MQ84; Q9LG32;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Uridine kinase-like protein 3;
DE Includes:
DE RecName: Full=Uridine kinase;
DE Short=UK;
DE EC=2.7.1.48;
DE Includes:
DE RecName: Full=Putative uracil phosphoribosyltransferase;
DE Short=UPRTase;
DE EC=2.4.2.9;
DE AltName: Full=UMP pyrophosphorylase;
GN Name=UKL3; OrderedLocusNames=At1g55810; ORFNames=F20N2.21;
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] (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).
RC TISSUE=Rosette leaf;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
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).
CC -!- FUNCTION: Involved in the pyrimidine salvage pathway. The uracil
CC phosphoribosyltransferase (UPRT) activity, that catalyzes the
CC conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP)
CC to UMP and diphosphate, is unsure. {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 -!- 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 -!- 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 -!- 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 -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via salvage pathway;
CC CTP from cytidine: step 1/3.
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage pathway;
CC UMP from uridine: step 1/1.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8VYB2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8VYB2-2; Sequence=VSP_039280;
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. No decrease in uracil
CC phosphoribosyltransferase activity. {ECO:0000269|PubMed:19563437}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF79310.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC002304; AAF79310.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE33300.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33301.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33302.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM61033.1; -; Genomic_DNA.
DR EMBL; AY072218; AAL60039.1; -; mRNA.
DR EMBL; AY122946; AAM67479.1; -; mRNA.
DR EMBL; AK317232; BAH19913.1; -; mRNA.
DR RefSeq; NP_001323277.1; NM_001333736.1. [Q8VYB2-1]
DR RefSeq; NP_175977.1; NM_104458.4. [Q8VYB2-1]
DR RefSeq; NP_974036.2; NM_202307.3. [Q8VYB2-2]
DR RefSeq; NP_974037.1; NM_202308.2. [Q8VYB2-1]
DR AlphaFoldDB; Q8VYB2; -.
DR SMR; Q8VYB2; -.
DR BioGRID; 27256; 1.
DR STRING; 3702.AT1G55810.3; -.
DR PaxDb; Q8VYB2; -.
DR PRIDE; Q8VYB2; -.
DR ProteomicsDB; 246396; -. [Q8VYB2-1]
DR EnsemblPlants; AT1G55810.1; AT1G55810.1; AT1G55810. [Q8VYB2-1]
DR EnsemblPlants; AT1G55810.2; AT1G55810.2; AT1G55810. [Q8VYB2-2]
DR EnsemblPlants; AT1G55810.3; AT1G55810.3; AT1G55810. [Q8VYB2-1]
DR EnsemblPlants; AT1G55810.6; AT1G55810.6; AT1G55810. [Q8VYB2-1]
DR GeneID; 842031; -.
DR Gramene; AT1G55810.1; AT1G55810.1; AT1G55810. [Q8VYB2-1]
DR Gramene; AT1G55810.2; AT1G55810.2; AT1G55810. [Q8VYB2-2]
DR Gramene; AT1G55810.3; AT1G55810.3; AT1G55810. [Q8VYB2-1]
DR Gramene; AT1G55810.6; AT1G55810.6; AT1G55810. [Q8VYB2-1]
DR KEGG; ath:AT1G55810; -.
DR Araport; AT1G55810; -.
DR TAIR; locus:2012125; AT1G55810.
DR eggNOG; KOG4203; Eukaryota.
DR InParanoid; Q8VYB2; -.
DR OMA; FIRRRET; -.
DR PhylomeDB; Q8VYB2; -.
DR UniPathway; UPA00574; UER00636.
DR UniPathway; UPA00574; UER00637.
DR UniPathway; UPA00579; UER00640.
DR PRO; PR:Q8VYB2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8VYB2; baseline and differential.
DR Genevisible; Q8VYB2; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0004845; F:uracil phosphoribosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004849; F:uridine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0071456; P:cellular response to hypoxia; HEP:TAIR.
DR GO; GO:0044211; P:CTP salvage; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0044206; P:UMP salvage; IEA:UniProtKB-UniPathway.
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; IPR000764; Uridine_kinase-like.
DR Pfam; PF00485; PRK; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF53271; SSF53271; 1.
DR TIGRFAMs; TIGR00235; udk; 1.
PE 2: Evidence at transcript level;
KW Allosteric enzyme; Alternative splicing; Glycosyltransferase; GTP-binding;
KW Kinase; Multifunctional enzyme; Nucleotide-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..466
FT /note="Uridine kinase-like protein 3"
FT /id="PRO_0000394516"
FT REGION 41..246
FT /note="Uridine kinase"
FT /evidence="ECO:0000250"
FT REGION 256..466
FT /note="Uracil phosphoribosyltransferase"
FT /evidence="ECO:0000250"
FT BINDING 280
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 289
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 323..326
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 333
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000250"
FT BINDING 358
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000250"
FT BINDING 378
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 384
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000250"
FT BINDING 389..392
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000250"
FT BINDING 454..456
FT /ligand="uracil"
FT /ligand_id="ChEBI:CHEBI:17568"
FT /evidence="ECO:0000250"
FT BINDING 455
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000250"
FT VAR_SEQ 366..370
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_039280"
SQ SEQUENCE 466 AA; 52443 MW; 3FA6783CB49727F7 CRC64;
MASKSDVNII ETSSKVHFSG FHQMDGLASN RPEQMAEEEE HGQPFVIGVA GGAASGKTTV
CDMIMQQLHD QRAVVVNQDS FYHNVNEVEL VRVHDYNFDH PDAFDTEQLL SSMEKLRKGQ
AVDIPNYDFK SYKNNVFPPR RVNPSDVIIL EGILIFHDPR VRDLMNMKIF VDADADVRLA
RRIKRDTVEK GRDIATVLDQ YSKFVKPAFE DFILPTKKYA DIIIPRGGDN HVAIDLIVQH
IHTKLGQHDL CKIYPNLYVI QSTFQIRGMH TLIRDSKTTK HDFIFYSDRL IRLVVEHGLG
HLPFTEKQVV TPTGSVYSGV DFCKKLCGVS VIRSGESMEN ALRACCKGIK IGKILIHREG
DNGQQLIYEK LPSDISERHV LLLDPILGTG NSAVQAIRLL ISKGVPESNI IFLNLISAPE
GVNVVCKKFP RIKIVTSEIE LGLNDEFRVV PGMGEFGDRY FGTDDE
