Uridylate kinase

Uridylate kinase (UK) catalyzes the reversible transfer of phosphate from UMP to UDP using ATP as a phosphate source. UDP is the starting point of synthesis of all other pyrimidine nucleotides. The eukaryotic UK has specificity to both UMP and CMP while the bacterial one is specific for UMP. The bacterial UK is Mg+2 dependent and is activated by GTP and repressed by UTP. The bacterial UK is composed of a C terminal ATP-binding domain and an N terminal UMP-binding domain.

3D structures of uridylate kinase3D structures of uridylate kinase

1ybd – UK – Neisseria meningitides
1z9d – UK – Streptococcus pyogenes
2a1f - UK - Haemophilus influenza
2brx – PfUK – Pyrococcus furiosus
2ij9 – UK (mutant) – Archaeoglobus fulgidus
2va1 - UK – Ureaplasma parvum
3ek5 – XcUK – Xanthomonas campestris

Uridylate kinase complex with nucleotides

1ukz – yUK + AMP + ADP
2bne – EcUK (mutant) + UMP – Escherichia coli
2bnd - EcUK (mutant) + UDP
2bnf - EcUK (mutant) + UTP
2v4y - EcUK (mutant) + GTP
2bmu - PfUK + UMP + AMPPNP
2bri - PfUK + AMPPNP
2ji5 - PfUK (mutant) + UTP
2j4j - SsUK + UMP + AMPPCP – Sulfolobus solfataricus
2j4k - SsUK + UMP
2j4l - SsUK + UTP
2jjx - UK + ATP + Mg – bacillus anthracis
1uky – yUK + ADP – yeast
3ek5 - XcUK + GTP
3nwy – UK + UTP + GTP – Mycobacterium tuberculosis