ID   UCK1_BOVIN              Reviewed;         277 AA.
AC   Q0P5A4;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Uridine-cytidine kinase 1;
DE            Short=UCK 1;
DE            EC=2.7.1.48 {ECO:0000250|UniProtKB:Q9HA47};
DE   AltName: Full=Cytidine monophosphokinase 1;
DE   AltName: Full=Uridine monophosphokinase 1;
GN   Name=UCK1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Ascending colon;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Phosphorylates uridine and cytidine to uridine monophosphate
CC       and cytidine monophosphate. Does not phosphorylate deoxyribonucleosides
CC       or purine ribonucleosides. Can use ATP or GTP as a phosphate donor.
CC       {ECO:0000250|UniProtKB:Q9HA47}.
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:0000250|UniProtKB:Q9HA47};
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:0000250|UniProtKB:Q9HA47};
CC   -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via salvage pathway;
CC       CTP from cytidine: step 1/3. {ECO:0000250|UniProtKB:Q9HA47}.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage pathway;
CC       UMP from uridine: step 1/1. {ECO:0000250|UniProtKB:Q9HA47}.
CC   -!- SIMILARITY: Belongs to the uridine kinase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC120304; AAI20305.1; -; mRNA.
DR   RefSeq; NP_001069260.1; NM_001075792.1.
DR   AlphaFoldDB; Q0P5A4; -.
DR   SMR; Q0P5A4; -.
DR   BioGRID; 176315; 1.
DR   STRING; 9913.ENSBTAP00000014316; -.
DR   PaxDb; Q0P5A4; -.
DR   GeneID; 519697; -.
DR   KEGG; bta:519697; -.
DR   CTD; 83549; -.
DR   eggNOG; KOG4203; Eukaryota.
DR   HOGENOM; CLU_021278_1_1_1; -.
DR   InParanoid; Q0P5A4; -.
DR   OrthoDB; 929897at2759; -.
DR   TreeFam; TF316686; -.
DR   UniPathway; UPA00574; UER00637.
DR   UniPathway; UPA00579; UER00640.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0043771; F:cytidine kinase activity; ISS:UniProtKB.
DR   GO; GO:0004849; F:uridine kinase activity; ISS:UniProtKB.
DR   GO; GO:0044211; P:CTP salvage; ISS:UniProtKB.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0044206; P:UMP salvage; ISS:UniProtKB.
DR   CDD; cd02023; UMPK; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR006083; PRK/URK.
DR   InterPro; IPR029920; UCK-1.
DR   InterPro; IPR000764; Uridine_kinase-like.
DR   PANTHER; PTHR10285:SF66; PTHR10285:SF66; 1.
DR   Pfam; PF00485; PRK; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00235; udk; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Transferase.
FT   CHAIN           1..277
FT                   /note="Uridine-cytidine kinase 1"
FT                   /id="PRO_0000346099"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          246..277
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         30..38
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HA47"
FT   BINDING         87
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BZX2"
FT   BINDING         115
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BZX2"
FT   BINDING         120
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BZX2"
FT   BINDING         169
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BZX2"
FT   BINDING         178
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BZX2"
FT   BINDING         186
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BZX2"
FT   BINDING         215
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HA47"
FT   MOD_RES         251
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HA47"
SQ   SEQUENCE   277 AA;  31195 MW;  8D1284FE5D93A465 CRC64;
     MASAGGGDCE GAGPEADRPH QRPFLIGVSG GTASGKSTVC EKIMELLGQN EVDHRQRKLV
     ILSQDRFYKV LTAEQKAKAL KGQYNFDHPD AFDNDLMHRT LKNIVEGKTV EVPTYDFVTH
     SRLAETTVVY PADVVLFEGI LVFYSQEIRD MFHLRLFVDT DSDVRLSRRV LRDVQRGRDL
     EQILTQYTTF VKPAFEEFCL PTKKYADVII PRGVDNMVAI NLIVQHIQDI LNGDICKWHR
     AGANGRSHKR TFPEPGEHPA VLASGKRSHL ESSSRPH