Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 2.7.4.14 - UMP/CMP kinase and Organism(s) Arabidopsis thaliana and UniProt Accession O04905

for references in articles please use BRENDA:EC2.7.4.14
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Arabidopsis thaliana
UNIPROT: O04905
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
hide
ATP
+
UMP
=
ADP
+
UDP
+
=
+
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
ATP:UMP-CMP phosphotransferase
-
-
-
-
CMP kinase
-
-
-
-
CMPK
-
-
-
-
CTP:CMP phosphotransferase
-
-
-
-
cytidine monophosphate kinase
-
-
-
-
cytidylate kinase
-
-
-
-
kinase, cytidylate (phosphorylating)
-
-
-
-
MssA protein
-
-
-
-
P25
-
-
-
-
pyrimidine nucleoside monophosphate kinase
-
-
-
-
UCK
-
-
-
-
UMP-CMP kinase
-
-
-
-
UMP/CMP kinase
-
-
-
-
UMPK
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + UMP = ADP + UDP
show the reaction diagram
random bi-bi mechanism
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -
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
-
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
-
-
-
?
ATP + UMP
ADP + UDP
show the reaction diagram
-
-
-
?
ATP + CMP
ADP + CDP
show the reaction diagram
-
-
-
-
?
ATP + UMP
ADP + UDP
show the reaction diagram
-
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
P1,P5-di(adenosine-5')pentaphosphate
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.029 - 0.292
ATP
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0012 - 0.00653
P1,P5-di(adenosine-5') pentaphosphate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
growth for 14 days without phosphate, increase in enzyme transkript level, coordinate regulation of aspartate transcarbamoylase, ATCase, EC 2.1.3.2, carbamoyl phosphate synthetase, CPSase, EC 6.3.5.5, UMP synthase, EC 2.4.1.10, EC 4.1.1.23, uracil phosphoribosyltransferase, UPRTase, EC 2.4.2.9, UMP kinase, EC 2.7.4.14
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
KCY3_ARATH
202
0
22482
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22448
x * 22448, mass spectroscopy, calculation from nucleotide sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 22448, mass spectroscopy, calculation from nucleotide sequence
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G21A
-
mutant enzyme is degraded during the purification phase
G22A
-
mutant enzyme with decreased turnover-number/KmATP value. Turnover-number is 59% of that of the wild-type enzyme
G24A
-
mutant enzyme with decreased turnover-number/KmATP value. Turnover-number is 48% of that of the wild-type enzyme
G26A
-
mutant enzyme with decreased turnover-number/KmATP value
G27R
-
mutant enzyme is degraded during the purification phase. Turnover-number is 45% of that of the wild-type enzyme
K27E
-
mutant enzyme with 2600fold decreased turnover-number/KmATP value. Turnover-number is 21% of that of the wild-type enzyme
K27M
-
mutant enzyme with 1000fold decreased turnover-number/KmATP value. Turnover-number is 22% of that of the wild-type enzyme
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
58
10 min, 50% loss of activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cDNA is subcloned into pGEX-4T-3 and expressed as a glutathione S-transferase fusion protein in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Zhou, L.; Lacroute, F.; Thornburg, R.
Cloning, expression in Escherichia coli, and characterization of Arabidopsis thaliana UMP/CMP kinase
Plant Physiol.
117
245-254
1998
Arabidopsis thaliana (O04905), Arabidopsis thaliana
Manually annotated by BRENDA team
Zhou, L.; Thornburg, R.
Site-specific mutations of conserved residues in the phosphate-binding loop of the Arabidopsis UMP/CMP kinase alter ATP and UMP binding
Arch. Biochem. Biophys.
358
297-302
1998
Arabidopsis thaliana
Manually annotated by BRENDA team
Hewitt, M.M.; Carr, J.M.; Williamson, C.L.; Slocum, R.D.
Effects of phosphate limitation on expression of genes involved in pyrimidine synthesis and salvaging in Arabidopsis
Plant Physiol. Biochem.
43
91-99
2005
Arabidopsis thaliana
Manually annotated by BRENDA team