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Information on EC 2.7.7.18 - nicotinate-nucleotide adenylyltransferase and Organism(s) Homo sapiens and UniProt Accession Q9HAN9

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Homo sapiens
UNIPROT: Q9HAN9 not found.
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The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
nicotinate mononucleotide adenylyltransferase, nicotinic acid mononucleotide adenylyltransferase, pfnmnat, namn at, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
adenylyltransferase, nicotinate mononucleotide
-
-
-
-
deamido-NAD+ pyrophosphorylase
-
-
-
-
deamidonicotinamide adenine dinucleotide pyrophosphorylase
-
-
-
-
NaMN AT
-
-
-
-
NaMN-ATase
-
-
-
-
nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1
-
-
nicotinic acid mononucleotide adenylyltransferase
-
-
-
-
NMN/NaMN adenylyltransferase 3
-
NMNAT2
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nucleotidyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
ATP:nicotinate-ribonucleotide adenylyltransferase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9026-98-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
show the reaction diagram
ATP + nicotinic acid mononucleotide
nicotinic acid adenine dinucleotide + diphosphate
show the reaction diagram
-
-
-
-
r
ATP + reduced nicotinamide nucleotide
diphosphate + NADH + H+
show the reaction diagram
-
-
-
?
nicotinic acid mononucleotide + ATP
nicotinic acid adenine dinucleotide + diphosphate
show the reaction diagram
activity observed with GTP, ITP
-
-
r
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD+
product inhibition
nicotinic acid adenine dinucleotide
product inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.119
diphosphate
-
0.07
NAD+
-
0.021
nicotinamide mononucleotide
range 0.021-0.032 mM
0.015
nicotinic acid mononucleotide
-
0.0304
reduced nicotinamide nucleotide
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isoform NMNAT1
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
sequence of isoform NMNAT1 contains a predicted nuclear localization signal
Manually annotated by BRENDA team
isoform NMNAT2 localizes to the cis-Golgi and endoplasmic reticulum-Golgi intermediate compartment. It is palmitoylated at two adjacent cysteine residues of its isoform-specific domain and thereby anchored at the cytoplasmic surface
Manually annotated by BRENDA team
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
NMNA1_HUMAN
279
0
31932
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
34439
4 * 34439, calculated
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homohexamer
-
-
homotetramer
4 * 34439, calculated
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
homology modeling of structure, based on structures of isoform NMNAT1 and NMNAT3 and molecular docking of potential inhibitors
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
R232Q
mutation impairs NAD synthase and chaperone functions
additional information
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in HeLa S3 cells
expression in HeLa S3 cells
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
loss of function mutations in two stillborn siblings lead to fetal akinesia deformation sequence, severely reduced skeletal muscle mass and hydrops fetalis. Both protein variants are incapable of supporting axon survival in mouse primary neuron cultures when overexpressed. Variants display altered protein stability and/or defects in NAD+ synthesis and chaperone functions
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Zhai, R.G.; Rizzi, M.; Garavaglia, S.
Nicotinamide/nicotinic acid mononucleotide adenylyltransferase, new insights into an ancient enzyme
Cell. Mol. Life Sci.
66
2805-2818
2009
Bacillus anthracis, Escherichia coli, Homo sapiens, Pseudomonas aeruginosa
Manually annotated by BRENDA team
Lau, C.; Niere, M.; Ziegler, M.
The NMN/NaMN adenylyltransferase (NMNAT) protein family
Front. Biosci.
14
410-431
2009
Arabidopsis thaliana, Escherichia coli (P0A752), Homo sapiens (Q96T66), Saccharomyces cerevisiae (P53204)
Manually annotated by BRENDA team
Lau, C.; Dolle, C.; Gossmann, T.; Agledal, L.; Niere, M.; Ziegler, M.
Isoform-specific targeting and interaction domains in human nicotinamide mononucleotide adenylyltransferases
J. Biol. Chem.
285
18868-18876
2010
Homo sapiens (Q96T66), Homo sapiens (Q9BZQ4), Homo sapiens (Q9HAN9)
Manually annotated by BRENDA team
Lukacs, M.; Gilley, J.; Zhu, Y.; Orsomando, G.; Angeletti, C.; Liu, J.; Yang, X.; Park, J.; Hopkin, R.J.; Coleman, M.P.; Zhai, R.G.; Stottmann, R.W.
Severe biallelic loss-of-function mutations in nicotinamide mononucleotide adenylyltransferase 2 (NMNAT2) in two fetuses with fetal akinesia deformation sequence
Exp. Neurol.
320
112961
2019
Homo sapiens (Q9BZQ4)
Manually annotated by BRENDA team
Eren, G.
Homology modeling of human nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2 Insights into isoenzyme-specific differences using molecular docking simulatons
Lett. Drug Des. Discov.
14
727-736
2017
Homo sapiens (Q9BZQ4)
-
Manually annotated by BRENDA team