ID   UCK1B_XENLA             Reviewed;         271 AA.
AC   Q6GPD9;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Uridine-cytidine kinase 1-B;
DE            Short=UCK 1-B;
DE            EC=2.7.1.48 {ECO:0000250|UniProtKB:Q9HA47};
DE   AltName: Full=Cytidine monophosphokinase 1-B;
DE   AltName: Full=Uridine monophosphokinase 1-B;
GN   Name=uck1-b;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-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; BC073200; AAH73200.1; -; mRNA.
DR   RefSeq; NP_001085688.1; NM_001092219.1.
DR   AlphaFoldDB; Q6GPD9; -.
DR   SMR; Q6GPD9; -.
DR   DNASU; 444114; -.
DR   GeneID; 444114; -.
DR   KEGG; xla:444114; -.
DR   OrthoDB; 929897at2759; -.
DR   UniPathway; UPA00574; UER00637.
DR   UniPathway; UPA00579; UER00640.
DR   Proteomes; UP000186698; Chromosome 8L.
DR   Bgee; 444114; Expressed in oocyte and 19 other tissues.
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..271
FT                   /note="Uridine-cytidine kinase 1-B"
FT                   /id="PRO_0000346103"
FT   REGION          240..271
FT                   /note="Disordered"
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   271 AA;  30745 MW;  C3FC2DAF5DE47B12 CRC64;
     MASAGSLDVP ERGHQRPFLI GVSGGTASGK STVCEKIMEL LGQNEVDHRQ RKVVILSQDR
     FYKVLTPEQK ARALKGQYNF DHPDAFDNEL MDRTLTQILD GQIVAVPMYD FITHSRLPET
     TTVYPADVVL FEGILAFYNQ EIRDMFQLKL FVDTDSDVRL SRRVLRDMKR GRDLEQILTQ
     YTTFVKPAFE EFSLPTKKYA DVIIPRGVDN MVAINLIVQH IQDILNGDIC KWQRGVQNGR
     SQKRTLPGQG DSGGLLLQGK RTHLESSSRP H