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Information on EC 2.7.1.236 - NAD+ 3'-kinase
for references in articles please use BRENDA:EC2.7.1.236
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EC Tree 2 Transferases
2.7 Transferring phosphorus-containing groups
2.7.1 Phosphotransferases with an alcohol group as acceptor
2.7.1.236 NAD+ 3'-kinase
IUBMB Comments
The enzyme, best characterized from the plant pathogenic bacterium Xanthomonas oryzae pv. oryzicola, is considered a bacterial type III effector. The product, 3′-NADP, is believed to enhance bacterial virulence on plants through manipulation of primary metabolic pathways. In vitro the enzyme is also active with nicotinate adenine dinucleotide (deamido-NAD).
The expected taxonomic range for this enzyme is: Xanthomonas oryzae pv. oryzicola
showSynonyms
avrrxo1, xopaj, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AvrRxo1
AvrRxo1
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + NAD+ = ADP + 3'-NADP+
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
ATP:NAD+ 3'-phosphotransferase
The enzyme, best characterized from the plant pathogenic bacterium Xanthomonas oryzae pv. oryzicola, is considered a bacterial type III effector. The product, 3'-NADP, is believed to enhance bacterial virulence on plants through manipulation of primary metabolic pathways. In vitro the enzyme is also active with nicotinate adenine dinucleotide (deamido-NAD).
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + NAAD+
ADP + 3'-NAADP+
-
Substrates: NAAD+ is nicotinic acid adenine dinucleotide
Products: -
Products: -
?
ATP + NAD+
ADP + 3'-NADP+
-
Substrates: -
Products: -
Products: -
?
ATP + NAD+
ADP + 3'-NADP+
Substrates: -
Products: -
Products: -
?
ATP + NAD+
ADP + 3'-NADP+
Substrates: -
Products: -
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?
additional information
?
-
-
Substrates: the enzyme accepts neither GDP nor GTP as phosphate acceptors
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?
additional information
?
-
Substrates: the enzyme does not possess uridine diphosphate-N-acetylglucosamine kinase activity
Products: -
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?
additional information
?
-
-
Substrates: the enzyme does not possess uridine diphosphate-N-acetylglucosamine kinase activity
Products: -
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?
additional information
?
-
Substrates: the enzyme does not possess uridine diphosphate-N-acetylglucosamine kinase activity
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + NAAD+
ADP + 3'-NAADP+
-
Substrates: NAAD+ is nicotinic acid adenine dinucleotide
Products: -
Products: -
?
ATP + NAD+
ADP + 3'-NADP+
-
Substrates: -
Products: -
Products: -
?
ATP + NAD+
ADP + 3'-NADP+
Substrates: -
Products: -
Products: -
?
ATP + NAD+
ADP + 3'-NADP+
Substrates: -
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1
ATP
-
with NAAD+ or NAD+ as cosubstrate, at pH 7.5 and 25°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
the enzyme functions from inside maize cells to elicit Rxo1-dependent pathogen recognition
physiological function
the enzyme has a significant virulence function that can increase bacterial growth on the host plant. The enzyme functions to enhance bacterial multiplication in plants, and full virulence function is dependent on its putative kinase activity
physiological function
-
the enzyme functions from inside maize cells to elicit Rxo1-dependent pathogen recognition
-
physiological function
-
the enzyme has a significant virulence function that can increase bacterial growth on the host plant. The enzyme functions to enhance bacterial multiplication in plants, and full virulence function is dependent on its putative kinase activity
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
AvrRxo1-ORF1:AvrRxo1-ORF2 tetramer complex, hanging drop vapor diffusion method, using either 0.8 M NaH2PO4, 0.8 M KH2PO4, 15% (v/v) glycerol, 8 mM dithiothreitol, and 0.1 M HEPES pH 7.5 (native or selenomethione-labeled enzyme) or 1.6 M (NH4)2SO4, 18% (v/v) glycerol, 8 mM dithiothreitol, 100 mM Na-citrate pH 5.0 (sulfate complex)
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
T167N
T167N
-
the mutant retains a low level of kinase activity that is insufficient to cause visible toxicity
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
glutathione Sepharose 4B affinity resin Q-Sepharose ion-exchange column chromatography
Ni-NTA column chromatography, HiTrap heparin column chromatography, and Superdex 75 gel filtration
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli C41 cells and Xanthomonas oryzae strain X11-5A
expressed in Escherichia coli strain BL21 (DE3), Nicotiana benthamiana and Oryza sativa leaves
-
expressed in Xanthomonas oryzae pv. oryzae strain PXO99A
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Schuebel, F.; Rocker, A.; Edelmann, D.; Schessner, J.; Brieke, C.; Meinhart, A.
3-NADP and 3-NAADP, two metabolites formed by the bacterial type III effector AvrRxo1
J. Biol. Chem.
291
22868-22880
2016
Xanthomonas oryzae pv. oryzicola
brenda
Zhao, B.; Ardales, E.Y.; Raymundo, A.; Bai, J.; Trick, H.N.; Leach, J.E.; Hulbert, S.H.
The avrRxo1 gene from the rice pathogen Xanthomonas oryzae pv. oryzicola confers a nonhost defense reaction on maize with resistance gene Rxo1
Mol. Plant Microbe Interact.
17
771-779
2004
Xanthomonas oryzae pv. oryzicola (Q6TKR8), Xanthomonas oryzae pv. oryzicola, Xanthomonas oryzae pv. oryzicola BLS256 (Q6TKR8)
brenda
Shidore, T.; Broeckling, C.D.; Kirkwood, J.S.; Long, J.J.; Miao, J.; Zhao, B.; Leach, J.E.; Triplett, L.R.
The effector AvrRxo1 phosphorylates NAD in planta
PLoS Pathog.
13
e1006442
2017
Xanthomonas oryzae pv. oryzicola
brenda
Han, Q.; Zhou, C.; Wu, S.; Liu, Y.; Triplett, L.; Miao, J.; Tokuhisa, J.; Deblais, L.; Robinson, H.; Leach, J.E.; Li, J.; Zhao, B.
Crystal structure of Xanthomonas AvrRxo1-ORF1, a type III effector with a polynucleotide kinase domain, and its interactor AvrRxo1-ORF2
Structure
23
1900-1909
2015
Xanthomonas oryzae pv. oryzicola (Q6TKR8), Xanthomonas oryzae pv. oryzicola, Xanthomonas oryzae pv. oryzicola BLS256 (Q6TKR8)
brenda
EXTERNAL LINKS (specific for EC-Number 2.7.1.236)
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Release 2026.1 (March 2026)
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