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Information on EC 2.7.1.23 - NAD+ kinase and Organism(s) Archaeoglobus fulgidus and UniProt Accession O30297

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This record set is specific for:
Archaeoglobus fulgidus
UNIPROT: O30297 not found.
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The taxonomic range for the selected organisms is: Archaeoglobus fulgidus
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
hide
ATP
+
NAD+
=
ADP
+
NADP+
+
=
+
Synonyms
nad kinase, nadk, nad+ kinase, nadk2, nad(h) kinase, utr1p, osnadk1, slr0400, sll1415, c5orf33, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ATP:NAD 2'-phosphotransferase
-
-
-
-
DPN kinase
-
-
-
-
kinase (phosphorylating), nicotinamide adenine dinucleotide
-
-
-
-
kinase, nicotinamide adenine dinucleotide (phosphorylating)
-
-
-
-
NAD kinase
-
-
-
-
NADK
-
-
-
-
nicotinamide adenine dinucleotide kinase
-
-
-
-
Poly(P)/ATP NAD kinase
-
-
-
-
polyphosphate/ATP-NAD kinase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + NAD+ = ADP + NADP+
show the reaction diagram
AMP portion of ATP uses the same binding site as the nicotinamide ribose portion of NAD/NADP, proposal for phosphate transfer mechanism
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
-
-
-
?
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
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with ATP, NAD, or NADP, AMP portion of ATP uses the same binding site as the nicotinamide ribose portion of NAD/NADP
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
one of the key enzymes regulating the balance of NAD(H) and NADP(H)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Liu, J.; Lou, Y.; Yokota, H.; Adams, P.D.; Kim, R.; Kim, S.H.
Crystal structures of an NAD kinase from Archaeoglobus fulgidus in complex with ATP, NAD, or NADP
J. Mol. Biol.
354
289-303
2005
Archaeoglobus fulgidus (O30297), Archaeoglobus fulgidus
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