UKL4_ARATH
ID UKL4_ARATH Reviewed; 469 AA.
AC O65583; Q0WQS9; Q8LD95; Q9SYU2;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Uridine kinase-like protein 4;
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=UKL4; Synonyms=UPT1; OrderedLocusNames=At4g26510; ORFNames=M3E9.60;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kim C.J., Chen H., Cheuk R., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 297-469.
RC STRAIN=cv. Columbia;
RA Weers B.D., Thornburg R.W.;
RT "Characterization of the cDNA and gene for an Arabidopsis thaliana uracil
RT phosphoribosyltransferase.";
RL (er) Plant Gene Register PGR99-044(1999).
RN [7]
RP FUNCTION, 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 -!- 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=CAA18219.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79506.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL022223; CAA18219.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161565; CAB79506.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85211.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85212.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM66905.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM66906.1; -; Genomic_DNA.
DR EMBL; AY086133; AAM63338.1; -; mRNA.
DR EMBL; BT022059; AAY25471.1; -; mRNA.
DR EMBL; AK228608; BAF00520.1; -; mRNA.
DR EMBL; AF116860; AAD28199.1; -; mRNA.
DR PIR; T05053; T05053.
DR RefSeq; NP_001320072.1; NM_001341804.1.
DR RefSeq; NP_001328772.1; NM_001341805.1.
DR RefSeq; NP_567747.4; NM_118784.6.
DR RefSeq; NP_849448.4; NM_179117.5.
DR AlphaFoldDB; O65583; -.
DR SMR; O65583; -.
DR STRING; 3702.AT4G26510.1; -.
DR iPTMnet; O65583; -.
DR PaxDb; O65583; -.
DR PRIDE; O65583; -.
DR ProteomicsDB; 245305; -.
DR EnsemblPlants; AT4G26510.1; AT4G26510.1; AT4G26510.
DR EnsemblPlants; AT4G26510.2; AT4G26510.2; AT4G26510.
DR EnsemblPlants; AT4G26510.3; AT4G26510.3; AT4G26510.
DR EnsemblPlants; AT4G26510.4; AT4G26510.4; AT4G26510.
DR GeneID; 828757; -.
DR Gramene; AT4G26510.1; AT4G26510.1; AT4G26510.
DR Gramene; AT4G26510.2; AT4G26510.2; AT4G26510.
DR Gramene; AT4G26510.3; AT4G26510.3; AT4G26510.
DR Gramene; AT4G26510.4; AT4G26510.4; AT4G26510.
DR KEGG; ath:AT4G26510; -.
DR Araport; AT4G26510; -.
DR TAIR; locus:2131498; AT4G26510.
DR eggNOG; KOG4203; Eukaryota.
DR HOGENOM; CLU_021278_0_3_1; -.
DR InParanoid; O65583; -.
DR OMA; TIVHEYN; -.
DR OrthoDB; 929897at2759; -.
DR PhylomeDB; O65583; -.
DR BioCyc; ARA:AT4G26510-MON; -.
DR UniPathway; UPA00574; UER00636.
DR UniPathway; UPA00574; UER00637.
DR UniPathway; UPA00579; UER00640.
DR PRO; PR:O65583; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O65583; baseline and differential.
DR Genevisible; O65583; 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: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; Glycosyltransferase; GTP-binding; Kinase;
KW Multifunctional enzyme; Nucleotide-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..469
FT /note="Uridine kinase-like protein 4"
FT /id="PRO_0000120784"
FT REGION 46..249
FT /note="Uridine kinase"
FT /evidence="ECO:0000250"
FT REGION 259..469
FT /note="Uracil phosphoribosyltransferase"
FT /evidence="ECO:0000250"
FT BINDING 283
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 292
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 326..329
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 336
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000250"
FT BINDING 361
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000250"
FT BINDING 381
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 387
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000250"
FT BINDING 392..395
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000250"
FT BINDING 457..459
FT /ligand="uracil"
FT /ligand_id="ChEBI:CHEBI:17568"
FT /evidence="ECO:0000250"
FT BINDING 458
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000250"
FT CONFLICT 94
FT /note="E -> G (in Ref. 5; BAF00520)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 469 AA; 52639 MW; E5A6357C1DF76BC7 CRC64;
MGSKSVVDMI EAASRAHFSG LHVNGHMNGL EPSALKETTS ASEDIQRQPF VIGVAGGAAS
GKTTVCDMII QQLHDQRVVL INLDSFYHNL TEEELARVHE YNFDHPDAFD TEHLLSCMEK
LRQGQAVDIP KYDFKTYRSS VFRRVNPTDV IILEGILLFH DPRVRKLMNM KIFVCTDADV
RLARRIKRDT VENGRDIGTV LDQYSKFVKP AFDDFILPTK KYADIIIPRG GDNHVAIDLI
VQHICTKLGQ HDLCKIYPNL YVIHSTFQIR GMHTLIRDSQ TTKHDFVFYS DRLIRLVVEH
GLGHLPFTEK QVITPTGCVY SGVDFCKRLC GVSVIRSGES MENALRACCK GIKIGKILIH
REGDNGQQLV YEKLPNDISE RHVLLLDPIL GTGNSAVEAI NLLISKGVPE GNIIFLNLIS
APQGVHVVCK KFPRIKIVTS EIDNGLNEEF RVIPGMGEFG DRYFGTDDD
