Information on EC 2.7.1.166 - 3-deoxy-D-manno-octulosonic acid kinase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.7.1.166
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RECOMMENDED NAME
GeneOntology No.
3-deoxy-D-manno-octulosonic acid kinase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
alpha-Kdo-(2->6)-lipid IVA + ATP = 4-O-phospho-alpha-Kdo-(2->6)-lipid IVA + ADP
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Kdo transfer to lipid IVA II
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Kdo8N transfer to lipid IVA
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Lipopolysaccharide biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
ATP:(KDO)-lipid IVA 3-deoxy-alpha-D-manno-oct-2-ulopyranose 4-phosphotransferase
The enzyme phosphorylates the 4-OH position of KDO in (KDO)-lipid IVA.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain VP161
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
adaptive strategies adopted by the organism during persistent infection: genome sequencing of three isolates from patients with chronic obstructive lung disease reveals sequential acquisition of single-nucleotide variants in the AMP permease sapC, the heme acquisition systems hgpB, hgpC, hup and hxuC, the 3-deoxy-D-manno-octulosonic acid kinase kdkA, the long-chain fatty acid transporter ompP1, and the phosphoribosylamine glycine ligase purD
malfunction
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-deoxy-alpha-D-manno-oct-2-ulopyranosyl-(2->6)-2-deoxy-2-[[(3R)-3-hydroxypentadecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose + ATP
3-deoxy-4-O-phosphono-alpha-D-manno-oct-2-ulopyranosyl-(2->6)-2-deoxy-2-[[(3R)-3-hydroxypentadecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose + ADP
show the reaction diagram
3-deoxy-alpha-D-manno-oct-2-ulopyranosyl-(2->6)-2-deoxy-2-[[(3R)-3-hydroxypentadecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose + CTP
3-deoxy-4-O-phosphono-alpha-D-manno-oct-2-ulopyranosyl-(2->6)-2-deoxy-2-[[(3R)-3-hydroxypentadecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose + CDP
show the reaction diagram
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phosphorylation at the 4-OH position of KDO. 7.6% of the activity with ATP. (KDO)-lipid IV(A) = 3-deoxy-alpha-D-manno-oct-2-ulopyranosyl-(2->6)-2-deoxy-2-[[(3R)-3-hydroxypentadecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose. (4-O-phospho-KDO)-lipid IV(A) = 3-deoxy-4-O-phosphono-alpha-D-manno-oct-2-ulopyranosyl-(2->6)-2-deoxy-2-[[(3R)-3-hydroxypentadecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
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?
3-deoxy-alpha-D-manno-oct-2-ulopyranosyl-(2->6)-2-deoxy-2-[[(3R)-3-hydroxypentadecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose + GTP
3-deoxy-4-O-phosphono-alpha-D-manno-oct-2-ulopyranosyl-(2->6)-2-deoxy-2-[[(3R)-3-hydroxypentadecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose + GDP
show the reaction diagram
3-deoxy-alpha-D-manno-oct-2-ulopyranosyl-(2->6)-2-deoxy-2-[[(3R)-3-hydroxypentadecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose + UTP
3-deoxy-4-O-phosphono-alpha-D-manno-oct-2-ulopyranosyl-(2->6)-2-deoxy-2-[[(3R)-3-hydroxypentadecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose + UDP
show the reaction diagram
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phosphorylation at the 4-OH position of KDO. 10.5% of the activity with ATP. (KDO)-lipid IV(A) = 3-deoxy-alpha-D-manno-oct-2-ulopyranosyl-(2->6)-2-deoxy-2-[[(3R)-3-hydroxypentadecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose. (4-O-phospho-KDO)-lipid IV(A) = 3-deoxy-4-O-phosphono-alpha-D-manno-oct-2-ulopyranosyl-(2->6)-2-deoxy-2-[[(3R)-3-hydroxypentadecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
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?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
3-deoxy-alpha-D-manno-oct-2-ulopyranosyl-(2->6)-2-deoxy-2-[[(3R)-3-hydroxypentadecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose + ATP
3-deoxy-4-O-phosphono-alpha-D-manno-oct-2-ulopyranosyl-(2->6)-2-deoxy-2-[[(3R)-3-hydroxypentadecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose + ADP
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
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absolute requirement
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0116
3-deoxy-alpha-D-manno-oct-2-ulopyranosyl-(2->6)-2-deoxy-2-[[(3R)-3-hydroxypentadecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
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pH 7.5, 30C, (KDO)-lipid IV(A) = 3-deoxy-alpha-D-manno-oct-2-ulopyranosyl-(2->6)-2-deoxy-2-[[(3R)-3-hydroxypentadecanoyl]amino]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
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Hepes buffer
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
both Escherichia coli strains which express waaA and kdkA from Haemophilus influenzae synthesize an lipopolysaccharide containing a single Kdo residue that is exclusively phosphorylated at position 4
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expression in Escherichia coli behind a T7 promoter, overproduction
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gene kdkA, genotyping of clinical isolates
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A112V
spontaneous KdkA mutant strain isolated from birds inoculated with high doses of a heptosyltransferase hptA mutant. The birds developed fowl cholera and the Pasteurella multocida isolates recovered from diseased birds no longer express truncated lipopolysaccharide. Mutation results in low level of enzymic acitivity
D193N
spontaneous KdkA mutant strain isolated from birds inoculated with high doses of a heptosyltransferase hptA mutant. The birds developed fowl cholera and the Pasteurella multocida isolates recovered from diseased birds no longer express truncated lipopolysaccharide. Mutation leads to complete loss of enzymic acitivity
H168Y
spontaneous KdkA mutant strain isolated from birds inoculated with high doses of a heptosyltransferase hptA mutant. The birds developed fowl cholera and the Pasteurella multocida isolates recovered from diseased birds no longer express truncated lipopolysaccharide. Residue is critical for Kdo kinase function and therefore glycoform A lipopolysaccharide assembly
R123P
spontaneous KdkA mutant strain isolated from birds inoculated with high doses of a heptosyltransferase hptA mutant. The birds developed fowl cholera and the Pasteurella multocida isolates recovered from diseased birds no longer express truncated lipopolysaccharide. Mutation is likely to have a significant impact on the secondary structure and probably affects the hinge action of the linker region
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