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Information on EC 2.7.1.23 - NAD+ kinase and Organism(s) Bacillus subtilis and UniProt Accession O31612

for references in articles please use BRENDA:EC2.7.1.23
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This record set is specific for:
Bacillus subtilis
UNIPROT: O31612 not found.
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The taxonomic range for the selected organisms is: Bacillus subtilis
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
nad kinase, nadk, nad+ kinase, nadk2, nad(h) kinase, utr1p, osnadk1, slr0400, c5orf33, sll1415, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ATP:NAD 2'-phosphotransferase
-
-
-
-
DPN kinase
-
-
-
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kinase (phosphorylating), nicotinamide adenine dinucleotide
-
-
-
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kinase, nicotinamide adenine dinucleotide (phosphorylating)
-
-
-
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NAD kinase
-
-
-
-
NADK
-
-
-
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nicotinamide adenine dinucleotide kinase
-
-
-
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Poly(P)/ATP NAD kinase
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-
-
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polyphosphate/ATP-NAD kinase
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
ATP:NAD+ 2'-phosphotransferase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9032-66-0
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + NAD+
ADP + NADP+
show the reaction diagram
-
-
-
?
NADH + poly(P)4
NADPH + poly(P)3
show the reaction diagram
-
-
-
?
ATP + NAD+
ADP + NADP+
show the reaction diagram
dATP + NAD+
dADP + NADP+
show the reaction diagram
-
77% of the activity with ATP
-
-
?
dCTP + NAD+
dCDP + NADP+
show the reaction diagram
-
30% of the activity with ATP
-
-
?
dGTP + NAD+
dGDP + NADP+
show the reaction diagram
-
77% of the activity with ATP
-
-
?
diphosphate + NAD+
phosphate + NADP+
show the reaction diagram
-
10% of the activity with ATP
-
-
?
dTTP + NAD+
dTDP + NADP+
show the reaction diagram
-
35% of the activity with ATP
-
-
?
GTP + NAD+
GDP + NADP+
show the reaction diagram
-
69% of the activity with ATP
-
-
?
polyphosphate + NAD+
?
show the reaction diagram
-
50% of the activity with ATP
-
-
?
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 + NAD+
ADP + NADP+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
HgCl2
-
1 mM, 75% inhibition
NADP+
-
0.05 mM, 75% inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
quinolinic acid
-
allosteric activator
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1
NAD+
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.36
ATP
-
-
5.46
NAD+
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9
-
glycine-NaOH buffer
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 10
-
pH 7.0: about 35% of maximal activity, pH 10.0: about 50% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 50
-
25°C: about 45% of maximal activity, 50°C: about 70% of maximal activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30000
-
2 * 30000, SDS-PAGE
60000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
2 * 30000
dimer
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
-
15 min, 50% loss of activity
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Garavaglia, S.; Galizzi, A.; Rizzi, M.
Allosteric regulation of Bacillus subtilis NAD kinase by quinolinic acid
J. Bacteriol.
185
4844-4850
2003
Bacillus subtilis
Manually annotated by BRENDA team
Kawai, S.; Murata, K.
Structure and function of NAD kinase and NADP phosphatase: key enzymes that regulate the intracellular balance of NAD(H) and NADP(H)
Biosci. Biotechnol. Biochem.
72
919-930
2008
Arabidopsis thaliana, Arabidopsis thaliana (Q500Y9), Arabidopsis thaliana (Q56YN3), Arabidopsis thaliana (Q9C5W3), Archaeoglobus fulgidus, Bacillus subtilis (O31612), Bacillus subtilis (O34934), Candida albicans, Columba livia, Cyberlindnera jadinii, Dictyostelium discoideum, Escherichia coli (P0A7B3), Glycine max, Homo sapiens, Homo sapiens (O95544), Lactuca sativa, Listeria monocytogenes, Methanocaldococcus jannaschii (Q58327), Micrococcus luteus (Q8VUL9), Mycobacterium tuberculosis (P9WHV7), Mycobacterium tuberculosis H37Rv (P9WHV7), Oryza sativa, Pyrococcus horikoshii (O58801), Saccharomyces cerevisiae (C7GKE4), Saccharomyces cerevisiae (P21373), Saccharomyces cerevisiae (P32622), Saccharomyces cerevisiae (Q06892), Saccharomyces cerevisiae, Salmonella enterica, Schizosaccharomyces pombe, Sorghum sp., Sphingomonas sp. A1 (Q6L7J5), Synechococcus elongatus PCC 6301, Thermotoga maritima, Triticum sp.
Manually annotated by BRENDA team
Li, B.; Wang, X.; Tai, L.; Ma, T.; Shalmani, A.; Liu, W.; Li, W.; Chen, K.
NAD kinases Metabolic targets controlling redox co-enzymes and reducing power partitioning in plant stress and development
Front. Plant Sci.
9
379
2018
Arabidopsis thaliana (Q500Y9), Arabidopsis thaliana (Q56YN3), Arabidopsis thaliana (Q9C5W3), Archaeoglobus fulgidus (P0A7B3), Bacillus subtilis (M4KX93), Escherichia coli (P0A7B3), Escherichia coli K12 (P0A7B3), Glycine max (I1KAE3), Glycine max (I1LPA7), Glycine max (I1LVA5), Glycine max (K7LNT1), Glycine max (K7LY64), Homo sapiens (O95544), Homo sapiens (Q4G0N4), Pyrococcus horikoshii (O58801), Pyrococcus horikoshii ATCC 700860 (O58801), Solanum lycopersicum (A0A3Q7E928), Solanum lycopersicum (A0A3Q7JHB9), Sphingomonas sp. (O58801), Strongylocentrotus purpuratus (C3RSF7), Strongylocentrotus purpuratus (P21373)
Manually annotated by BRENDA team