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Information on EC 2.7.1.23 - NAD+ kinase and Organism(s) Thermotoga maritima and UniProt Accession Q9X255

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This record set is specific for:
Thermotoga maritima
UNIPROT: Q9X255 not found.
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The taxonomic range for the selected organisms is: Thermotoga maritima
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
nad kinase, nadk, nad+ kinase, nadk2, utr1p, nad(h) kinase, osnadk1, slr0400, sll1415, c5orf33, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ATP:NAD 2'-phosphotransferase
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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
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NADK
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nicotinamide adenine dinucleotide kinase
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Poly(P)/ATP NAD kinase
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polyphosphate/ATP-NAD kinase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
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PATHWAY SOURCE
PATHWAYS
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-, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
ATP:NAD+ 2'-phosphotransferase
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CAS REGISTRY NUMBER
COMMENTARY hide
9032-66-0
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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
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?
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
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?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals of SeMet-containing PPNK_THEMA are obtained at room temperature in hanging drops. Crystal structure of inorganic polyphosphate/ATP-NAD kinase is determined at 2.3 A resolution. The crystal structure is solved using single-wavelength anomalous diffraction data collected at the Se absorption-peak wavelength in a state in which no cofactors or substrates are bound. It revealed that the 258-amino-acid protein is folded into two distinct domains. The N-terminal alpha/beta-domain spans the first 100 amino acids and the last 30 amino acids of the polypeptide and has several topological matches in the PDB, whereas the other domain, which spans the middle 130 residues, adopts a unique beta-sandwich architecture and only appreciably matches the recently deposited PDB structures of NAD kinases
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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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
Oganesyan, V.; Huang, C.; Adams, P.D.; Jancarik, J.; Yokota, H.A.; Kim, R.; Kim, S.H.
Structure of a NAD kinase from Thermotoga maritima at 2.3 A resolution
Acta Crystallogr. Sect. F
61
640-646
2005
Thermotoga maritima (Q9X255), Thermotoga maritima
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