URK1_SCHPO
ID URK1_SCHPO Reviewed; 454 AA.
AC O74427;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Uridine kinase;
DE EC=2.7.1.48;
DE AltName: Full=Uridine monophosphokinase;
GN Name=urk1; ORFNames=SPCC162.11c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Catalyzes the conversion of uridine into UMP and cytidine
CC into CMP in the pyrimidine salvage pathway. {ECO:0000250}.
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 -!- 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 -!- 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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the uridine kinase family. {ECO:0000305}.
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DR EMBL; CU329672; CAA19591.1; -; Genomic_DNA.
DR PIR; T41020; T41020.
DR RefSeq; NP_588233.1; NM_001023223.2.
DR AlphaFoldDB; O74427; -.
DR SMR; O74427; -.
DR BioGRID; 275520; 238.
DR STRING; 4896.SPCC162.11c.1; -.
DR MaxQB; O74427; -.
DR PaxDb; O74427; -.
DR PRIDE; O74427; -.
DR EnsemblFungi; SPCC162.11c.1; SPCC162.11c.1:pep; SPCC162.11c.
DR PomBase; SPCC162.11c; urk1.
DR VEuPathDB; FungiDB:SPCC162.11c; -.
DR eggNOG; KOG4203; Eukaryota.
DR HOGENOM; CLU_021278_0_2_1; -.
DR InParanoid; O74427; -.
DR OMA; RTKTMYG; -.
DR PhylomeDB; O74427; -.
DR Reactome; R-SPO-73614; Pyrimidine salvage.
DR UniPathway; UPA00574; UER00637.
DR UniPathway; UPA00579; UER00640.
DR PRO; PR:O74427; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0032153; C:cell division site; HDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0044732; C:mitotic spindle pole body; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004845; F:uracil phosphoribosyltransferase activity; NAS:PomBase.
DR GO; GO:0004849; F:uridine kinase activity; ISO:PomBase.
DR GO; GO:0044211; P:CTP salvage; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006206; P:pyrimidine nucleobase metabolic process; NAS:PomBase.
DR GO; GO:0008655; P:pyrimidine-containing compound salvage; IBA:GO_Central.
DR GO; GO:0044206; P:UMP salvage; IEA:UniProtKB-UniPathway.
DR CDD; cd02023; UMPK; 1.
DR Gene3D; 3.40.50.2020; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR006083; PRK/URK.
DR InterPro; IPR029057; PRTase-like.
DR InterPro; IPR000764; Uridine_kinase-like.
DR Pfam; PF00485; PRK; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF53271; SSF53271; 1.
DR TIGRFAMs; TIGR00235; udk; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Nucleus;
KW Reference proteome; Transferase.
FT CHAIN 1..454
FT /note="Uridine kinase"
FT /id="PRO_0000311758"
FT BINDING 28..35
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 454 AA; 51390 MW; 80EC445495854654 CRC64;
MPEAFERYSS NPTYEPPWRK VRFIGIAGPS GSGKTSVAQL IVKALNLPHV VILSLDSFYK
SLNAEQKKRA FNNDYDFDSP EAIDWDLLFV KLLELKQGRK VDIPIYSFNE HNRLPETNTL
FGASIIILEG IFALYDEKIR SLLDVSVFLD TDSDVCLSRR LNRDINYRGR DIVGVLEQYN
KFVKPSYENF VRRQLSYTDL IVPRGRDNKL AIDMVINFIR RTLSIQSETH VKNIDSLQQI
VPTIPHLPLN LVQLKITPEI SAIRTILINK NTHPDDLQFF LSRIGTMLMN LAGDSLAYEK
KTITLHNGNQ WEGLQMAKEL CGVSVLRSGG TLETALCRQF PTVCLGKILV QINKVTQEPT
LHYHKLPRGI ATMNVVLMAS HLTTHADVLM ATQILVDFGV PEENIIIVVY VCYSESIKAL
AYIFPKVTIV TAFLESVAEP VVGRLDIEKV YYGC
