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Information on EC 2.7.4.14 - UMP/CMP kinase and Organism(s) Dictyostelium discoideum and UniProt Accession P20425

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EC Tree
IUBMB Comments
This eukaryotic enzyme is a bifunctional enzyme that catalyses the phosphorylation of both CMP and UMP with similar efficiency. dCMP can also act as acceptor. Different from the monofunctional prokaryotic enzymes EC 2.7.4.25, (d)CMP kinase and EC 2.7.4.22, UMP kinase.
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This record set is specific for:
Dictyostelium discoideum
UNIPROT: P20425
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Word Map
The taxonomic range for the selected organisms is: Dictyostelium discoideum
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
+
=
+
Synonyms
cmpk2, cmpk, cmp kinase, ump-cmp kinase, cmpk1, ump/cmp kinase, cytidylate kinase, pyrimidine nucleoside monophosphate kinase, cytidine monophosphate kinase, cytidine/uridine monophosphate kinase 2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
uridine monophosphate/cytidine monophosphate kinase
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ATP:UMP-CMP phosphotransferase
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CMP kinase
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CMPK
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CTP:CMP phosphotransferase
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cytidine monophosphate kinase
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cytidylate kinase
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kinase, cytidylate (phosphorylating)
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MssA protein
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P25
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pyrimidine nucleoside monophosphate kinase
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UCK
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UMP-CMP kinase
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UMP/CMP kinase
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UMPK
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additional information
the enzyme belongs to the family of nucleoside monophosphate, NMP, kinases. These enzymes not only show high sequence and structure similarities but also share the alpha/beta-fold, a very common protein topology
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + UMP = ADP + UDP
show the reaction diagram
the mechanism is analogous to the phosphoryl transfer mechanism in cAMP-dependent protein kinase that phosphorylates the hydroxyl groups of serine residues
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
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PATHWAY SOURCE
PATHWAYS
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-, -, -
SYSTEMATIC NAME
IUBMB Comments
ATP:CMP(UMP) phosphotransferase
This eukaryotic enzyme is a bifunctional enzyme that catalyses the phosphorylation of both CMP and UMP with similar efficiency. dCMP can also act as acceptor. Different from the monofunctional prokaryotic enzymes EC 2.7.4.25, (d)CMP kinase and EC 2.7.4.22, UMP kinase.
CAS REGISTRY NUMBER
COMMENTARY hide
37278-21-0
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + CMP
ADP + CDP
show the reaction diagram
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-
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
KCY_DICDI
195
0
22074
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
after treatment with urea, UmpK protein unfolding and refolding kinetics, and folding mechanism, overview
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hutter, M.C.; Helms, V.
Phosphoryl transfer by a concerted reaction mechanism in UMP/CMP-kinase
Protein Sci.
9
2225-2231
2000
Dictyostelium discoideum
Manually annotated by BRENDA team
Lorenz, T.; Reinstein, J.
The influence of proline isomerization and off-pathway intermediates on the folding mechanism of eukaryotic UMP/CMP kinase
J. Mol. Biol.
381
443-455
2008
Dictyostelium discoideum (P20425), Dictyostelium discoideum
Manually annotated by BRENDA team