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Information on EC 2.7.4.22 - UMP kinase and Organism(s) Bacillus subtilis and UniProt Accession O31749

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IUBMB Comments
This enzyme is strictly specific for UMP as substrate and is used by prokaryotes in the de novo synthesis of pyrimidines, in contrast to eukaryotes, which use the dual-specificity enzyme UMP/CMP kinase (EC 2.7.4.14) for the same purpose . This enzyme is the subject of feedback regulation, being inhibited by UTP and activated by GTP .
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This record set is specific for:
Bacillus subtilis
UNIPROT: O31749
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The taxonomic range for the selected organisms is: Bacillus subtilis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
+
=
+
Synonyms
umpk, ump kinase, uridine monophosphate kinase, uridylate kinase, ump-kinase, umpks, ssumpk, xc1936, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ATP:UMP phosphotransferase
-
uridine monophosphate kinase
-
uridylate kinase
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:UMP phosphotransferase
This enzyme is strictly specific for UMP as substrate and is used by prokaryotes in the de novo synthesis of pyrimidines, in contrast to eukaryotes, which use the dual-specificity enzyme UMP/CMP kinase (EC 2.7.4.14) for the same purpose [2]. This enzyme is the subject of feedback regulation, being inhibited by UTP and activated by GTP [1].
CAS REGISTRY NUMBER
COMMENTARY hide
9036-23-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + 5-fluoro-UMP
ADP + 5-fluoro-UDP
show the reaction diagram
-
-
-
?
ATP + 6-aza-UMP
ADP + 6-aza-UDP
show the reaction diagram
-
-
-
?
ATP + UMP
ADP + UDP
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + UMP
ADP + UDP
show the reaction diagram
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dUTP
five times weaker than UTP
TTP
not inhibitory
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3'-anthraniloyl-2'-deoxyguanosine-5'-triphosphate
-
3'-anthraniloyl-dGTP
strong activator
GMP
not activating
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.12
5-fluoro-UMP
-
0.14
6-aza-UMP
-
0.9 - 30
ATP
0.008 - 0.155
UMP
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.66
UMP
at 2.0 mM ATP, without GTP, no inhibition at 30 mM ATP
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.6
with 6-aza-UMP as substrate
18.1
at 8.0 mM ATP, without GTP
2.7
at 2.0 mM ATP, without GTP
24
with 5-fluoro-UMP as substrate
25
His-tagged protein
26
native protein
28.6
at 2.0 mM ATP, with 0.5 mM GTP
39.1
at 8.0 mM ATP, with 0.5 mM GTP
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
154000
gel filtration
26080
28120
His-tagged protein, monomer, mass spectroscopy
28250
His-tagged protein, monomer, calculated from amino acid sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
N137A
Tm 10°C lower than wild type, loss of cooperativity with ATP, sensitive to activation by GTP
T135A
Tm 10°C lower than wild type, loss of cooperativity with ATP, increase in Km for UMP, sensitive to activation by GTP
T135A/N137A
Tm 10°C lower than wild type, at pH 7.4 in 50 mM Tris irreversible inactivated within hours
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
42
half-maximal inactivation
70
half-maximal inactivation in the presence of 1 mM UTP
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
room temperature, 50 mM Tris-HCl (pH 7.4), 0.1 M NaCl, 2 mM UTP, 2 weeks, no loss of activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
of the recombinant protein by affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli strain BL21(DE3)/pDIA17
expression in Escherichia coli, site directed mutagenesis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Gagyi, C.; Bucurenci, N.; Sirbu, O.; Labesse, G.; Ionescu, M.; Ofiteru, A.; Assairi, L.; Landais, S.; Danchin, A.; Barzu, O.; Gilles, A.M.
UMP kinase from the Gram-positive bacterium Bacillus subtilis is strongly dependent on GTP for optimal activity
Eur. J. Biochem.
270
3196-3204
2003
Bacillus subtilis (O31749), Bacillus subtilis, Escherichia coli (P0A7E9), Escherichia coli
Manually annotated by BRENDA team
Evrin, C.; Straut, M.; Slavova-Azmanova, N.; Bucurenci, N.; Onu, A.; Assairi, L.; Ionescu, M.; Palibroda, N.; Barzu, O.; Gilles, A.
Regulatory mechanisms differ in UMP kinases from Gram-negative and Gram-positive bacteria
J. Biol. Chem.
282
7242-7253
2007
Streptococcus pneumoniae, Enterococcus faecalis, Haemophilus influenzae, Staphylococcus aureus, Salmonella enterica subsp. enterica serovar Typhimurium, Escherichia coli (A7ZWB7), Bacillus subtilis (O31749), Neisseria meningitidis (P65932)
Manually annotated by BRENDA team