UCK1_MACFA
ID UCK1_MACFA Reviewed; 254 AA.
AC Q4R4K2;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 71.
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=QnpA-18547;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Parietal cortex;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) 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; AB169892; BAE01973.1; -; mRNA.
DR AlphaFoldDB; Q4R4K2; -.
DR SMR; Q4R4K2; -.
DR UniPathway; UPA00574; UER00637.
DR UniPathway; UPA00579; UER00640.
DR Proteomes; UP000233100; Unplaced.
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; -; 2.
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; 2.
DR Pfam; PF00485; PRK; 2.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Transferase.
FT CHAIN 1..254
FT /note="Uridine-cytidine kinase 1"
FT /id="PRO_0000346100"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..254
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 146
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9BZX2"
FT BINDING 155
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9BZX2"
FT BINDING 163
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9BZX2"
FT BINDING 192
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9HA47"
FT MOD_RES 228
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9HA47"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HA47"
SQ SEQUENCE 254 AA; 28683 MW; AB5262AE6E02E168 CRC64;
MASAGGDECE GAAPEADRPH QRPFLIGVSG GTASGKSTVC EKIMGLLGQN EVEQRQRKVV
ILSQDRFYKV LTAEQKAKAL KGQYNFDHPD AFDNDLMHRT LKNIVEGKTV EVPTYDFVTH
SSQEIRDMFH LRLFVDTDSD VRLSRRVLRD VRRGRDLEQI LTQYTTFVKP AFEEFCLPTK
KYADVIIPRG VDNMVAINLI VQHIQDILNG DICKWHRGGS NGRSYKRTFS EPGDHPGMLT
SGKRSHLESS SRPH
