ID   UCK1_DANRE              Reviewed;         277 AA.
AC   Q66I71;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 103.
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; ORFNames=zgc:103645;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Larva;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (SEP-2004) 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}.
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DR   EMBL; BC081503; AAH81503.1; -; mRNA.
DR   RefSeq; NP_001004666.1; NM_001004666.1.
DR   AlphaFoldDB; Q66I71; -.
DR   SMR; Q66I71; -.
DR   STRING; 7955.ENSDARP00000065879; -.
DR   PaxDb; Q66I71; -.
DR   GeneID; 447928; -.
DR   KEGG; dre:447928; -.
DR   CTD; 83549; -.
DR   ZFIN; ZDB-GENE-040912-113; uck1.
DR   eggNOG; KOG4203; Eukaryota.
DR   InParanoid; Q66I71; -.
DR   OrthoDB; 929897at2759; -.
DR   PhylomeDB; Q66I71; -.
DR   Reactome; R-DRE-73614; Pyrimidine salvage.
DR   UniPathway; UPA00574; UER00637.
DR   UniPathway; UPA00579; UER00640.
DR   PRO; PR:Q66I71; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; 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; Reference proteome; Transferase.
FT   CHAIN           1..277
FT                   /note="Uridine-cytidine kinase 1"
FT                   /id="PRO_0000346101"
FT   REGION          241..277
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        255..269
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         24..32
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HA47"
FT   BINDING         81
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BZX2"
FT   BINDING         109
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BZX2"
FT   BINDING         114
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BZX2"
FT   BINDING         163
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BZX2"
FT   BINDING         172
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BZX2"
FT   BINDING         180
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BZX2"
FT   BINDING         209
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HA47"
SQ   SEQUENCE   277 AA;  31457 MW;  F5EB9BD3333A2E8D CRC64;
     MNSSGLLCDN ERPRHRPFLI GVSGGTASGK STVCAKIMEL LGQNKVDHHQ RKVTIVSQDS
     FYRVLTPEQK AKALKGQYNF DHPDAFDTEF MCQTLKDIVE GKVVEVPTYD FVTHSRLPEK
     ICVYPADVVL FEGILVFYTQ EVRDMFHMKQ FVDTDSDVRL SRRVLRDMNR GRDLEQILTQ
     YTTFVKPAFE EFCLPTKKYA DVIIPRGVDN MVAINLIVQH IQDILNGDIC KWQRGSVNGH
     NHGRSLKRGV AEHGENPSGS SSNLTKRPLL EPSTRPH