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Literature summary extracted from

  • Zhai, R.G.; Rizzi, M.; Garavaglia, S.
    Nicotinamide/nicotinic acid mononucleotide adenylyltransferase, new insights into an ancient enzyme (2009), Cell. Mol. Life Sci., 66, 2805-2818.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.7.7.1
-
Staphylococcus aureus
2.7.7.1
-
Haemophilus influenzae
2.7.7.1
-
Escherichia coli
2.7.7.1
-
Homo sapiens
2.7.7.1
-
Synechocystis sp.
2.7.7.1
-
Methanocaldococcus jannaschii
2.7.7.1
-
Methanothermobacter thermautotrophicus

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.1 Bacillus anthracis
-
-
-
2.7.7.1 Escherichia coli
-
-
-
2.7.7.1 Haemophilus influenzae
-
-
-
2.7.7.1 Homo sapiens
-
-
-
2.7.7.1 Methanocaldococcus jannaschii Q57961
-
-
2.7.7.1 Methanothermobacter thermautotrophicus O26253
-
-
2.7.7.1 Pseudomonas aeruginosa
-
-
-
2.7.7.1 Staphylococcus aureus
-
-
-
2.7.7.1 Synechocystis sp.
-
-
-
2.7.7.18 Bacillus anthracis
-
-
-
2.7.7.18 Escherichia coli
-
-
-
2.7.7.18 Homo sapiens
-
-
-
2.7.7.18 Pseudomonas aeruginosa
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.7.1
-
Staphylococcus aureus
2.7.7.1
-
Haemophilus influenzae
2.7.7.1
-
Escherichia coli
2.7.7.1
-
Homo sapiens
2.7.7.1
-
Synechocystis sp.
2.7.7.1
-
Methanocaldococcus jannaschii
2.7.7.1
-
Methanothermobacter thermautotrophicus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.7.1 ATP + nicotinamide ribonucleotide
-
Staphylococcus aureus diphosphate + NAD+
-
r
2.7.7.1 ATP + nicotinamide ribonucleotide
-
Haemophilus influenzae diphosphate + NAD+
-
r
2.7.7.1 ATP + nicotinamide ribonucleotide
-
Escherichia coli diphosphate + NAD+
-
r
2.7.7.1 ATP + nicotinamide ribonucleotide
-
Homo sapiens diphosphate + NAD+
-
r
2.7.7.1 ATP + nicotinamide ribonucleotide
-
Pseudomonas aeruginosa diphosphate + NAD+
-
r
2.7.7.1 ATP + nicotinamide ribonucleotide
-
Synechocystis sp. diphosphate + NAD+
-
r
2.7.7.1 ATP + nicotinamide ribonucleotide
-
Bacillus anthracis diphosphate + NAD+
-
r
2.7.7.1 ATP + nicotinamide ribonucleotide
-
Methanocaldococcus jannaschii diphosphate + NAD+
-
r
2.7.7.1 ATP + nicotinamide ribonucleotide
-
Methanothermobacter thermautotrophicus diphosphate + NAD+
-
r
2.7.7.1 ATP + nicotinic acid mononucleotide
-
Staphylococcus aureus diphosphate + nicotinic acid adenine dinucleotide
-
r
2.7.7.1 ATP + nicotinic acid mononucleotide
-
Haemophilus influenzae diphosphate + nicotinic acid adenine dinucleotide
-
r
2.7.7.1 ATP + nicotinic acid mononucleotide
-
Escherichia coli diphosphate + nicotinic acid adenine dinucleotide
-
r
2.7.7.1 ATP + nicotinic acid mononucleotide
-
Homo sapiens diphosphate + nicotinic acid adenine dinucleotide
-
r
2.7.7.1 ATP + nicotinic acid mononucleotide
-
Pseudomonas aeruginosa diphosphate + nicotinic acid adenine dinucleotide
-
r
2.7.7.1 ATP + nicotinic acid mononucleotide
-
Synechocystis sp. diphosphate + nicotinic acid adenine dinucleotide
-
r
2.7.7.1 ATP + nicotinic acid mononucleotide
-
Bacillus anthracis diphosphate + nicotinic acid adenine dinucleotide
-
r
2.7.7.1 ATP + nicotinic acid mononucleotide
-
Methanocaldococcus jannaschii diphosphate + nicotinic acid adenine dinucleotide
-
r
2.7.7.1 ATP + nicotinic acid mononucleotide
-
Methanothermobacter thermautotrophicus diphosphate + nicotinic acid adenine dinucleotide
-
r
2.7.7.18 ATP + nicotinamide ribonucleotide
-
Escherichia coli diphosphate + NAD+
-
r
2.7.7.18 ATP + nicotinamide ribonucleotide
-
Homo sapiens diphosphate + NAD+
-
r
2.7.7.18 ATP + nicotinamide ribonucleotide
-
Pseudomonas aeruginosa diphosphate + NAD+
-
r
2.7.7.18 ATP + nicotinamide ribonucleotide
-
Bacillus anthracis diphosphate + NAD+
-
r
2.7.7.18 ATP + nicotinic acid mononucleotide
-
Escherichia coli nicotinic acid adenine dinucleotide + diphosphate
-
r
2.7.7.18 ATP + nicotinic acid mononucleotide
-
Homo sapiens nicotinic acid adenine dinucleotide + diphosphate
-
r
2.7.7.18 ATP + nicotinic acid mononucleotide
-
Pseudomonas aeruginosa nicotinic acid adenine dinucleotide + diphosphate
-
r
2.7.7.18 ATP + nicotinic acid mononucleotide
-
Bacillus anthracis nicotinic acid adenine dinucleotide + diphosphate
-
r

Subunits

EC Number Subunits Comment Organism
2.7.7.1 monomer
-
Escherichia coli
2.7.7.1 monomer
-
Pseudomonas aeruginosa
2.7.7.1 oligomer
-
Staphylococcus aureus
2.7.7.1 oligomer
-
Haemophilus influenzae
2.7.7.1 oligomer
-
Homo sapiens
2.7.7.1 oligomer
-
Synechocystis sp.
2.7.7.1 oligomer
-
Bacillus anthracis
2.7.7.1 oligomer
-
Methanocaldococcus jannaschii
2.7.7.1 oligomer
-
Methanothermobacter thermautotrophicus
2.7.7.18 dimer
-
Bacillus anthracis
2.7.7.18 homohexamer
-
Homo sapiens
2.7.7.18 monomer
-
Escherichia coli
2.7.7.18 monomer
-
Pseudomonas aeruginosa

Synonyms

EC Number Synonyms Comment Organism
2.7.7.1 hNMNAT
-
Homo sapiens
2.7.7.1 NadM-Nudix
-
Synechocystis sp.
2.7.7.1 NadR
-
Haemophilus influenzae
2.7.7.1 NaMNAT
-
Staphylococcus aureus
2.7.7.1 NaMNAT
-
Escherichia coli
2.7.7.1 nicotinamide/nicotinic acid mononucleotide adenylyltransferase nicotinate nucleotide can also act as acceptor, see also EC 2.7.7.18 nicotinate-nucleotide adenylyltransferase Staphylococcus aureus
2.7.7.1 nicotinamide/nicotinic acid mononucleotide adenylyltransferase nicotinate nucleotide can also act as acceptor, see also EC 2.7.7.18 nicotinate-nucleotide adenylyltransferase Haemophilus influenzae
2.7.7.1 nicotinamide/nicotinic acid mononucleotide adenylyltransferase nicotinate nucleotide can also act as acceptor, see also EC 2.7.7.18 nicotinate-nucleotide adenylyltransferase Escherichia coli
2.7.7.1 nicotinamide/nicotinic acid mononucleotide adenylyltransferase nicotinate nucleotide can also act as acceptor, see also EC 2.7.7.18 nicotinate-nucleotide adenylyltransferase Homo sapiens
2.7.7.1 nicotinamide/nicotinic acid mononucleotide adenylyltransferase nicotinate nucleotide can also act as acceptor, see also EC 2.7.7.18 nicotinate-nucleotide adenylyltransferase Pseudomonas aeruginosa
2.7.7.1 nicotinamide/nicotinic acid mononucleotide adenylyltransferase nicotinate nucleotide can also act as acceptor, see also EC 2.7.7.18 nicotinate-nucleotide adenylyltransferase Synechocystis sp.
2.7.7.1 nicotinamide/nicotinic acid mononucleotide adenylyltransferase nicotinate nucleotide can also act as acceptor, see also EC 2.7.7.18 nicotinate-nucleotide adenylyltransferase Bacillus anthracis
2.7.7.1 nicotinamide/nicotinic acid mononucleotide adenylyltransferase nicotinate nucleotide can also act as acceptor, see also EC 2.7.7.18 nicotinate-nucleotide adenylyltransferase Methanocaldococcus jannaschii
2.7.7.1 nicotinamide/nicotinic acid mononucleotide adenylyltransferase nicotinate nucleotide can also act as acceptor, see also EC 2.7.7.18 nicotinate-nucleotide adenylyltransferase Methanothermobacter thermautotrophicus
2.7.7.1 NMNAT
-
Staphylococcus aureus
2.7.7.1 NMNAT
-
Haemophilus influenzae
2.7.7.1 NMNAT
-
Escherichia coli
2.7.7.1 NMNAT
-
Homo sapiens
2.7.7.1 NMNAT
-
Pseudomonas aeruginosa
2.7.7.1 NMNAT
-
Synechocystis sp.
2.7.7.1 NMNAT
-
Bacillus anthracis
2.7.7.1 NMNAT
-
Methanocaldococcus jannaschii
2.7.7.1 NMNAT
-
Methanothermobacter thermautotrophicus
2.7.7.18 nicotinamide/nicotinic acid mononucleotide adenylyltransferase
-
Escherichia coli
2.7.7.18 nicotinamide/nicotinic acid mononucleotide adenylyltransferase
-
Pseudomonas aeruginosa
2.7.7.18 nicotinamide/nicotinic acid mononucleotide adenylyltransferase
-
Bacillus anthracis
2.7.7.18 nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1
-
Homo sapiens

General Information

EC Number General Information Comment Organism
2.7.7.1 physiological function NMNAT appears to be a multifunctional protein that sits both at the core of central metabolism and at the crossroads of multiple cellular processes Staphylococcus aureus
2.7.7.1 physiological function NMNAT appears to be a multifunctional protein that sits both at the core of central metabolism and at the crossroads of multiple cellular processes Haemophilus influenzae
2.7.7.1 physiological function NMNAT appears to be a multifunctional protein that sits both at the core of central metabolism and at the crossroads of multiple cellular processes Escherichia coli
2.7.7.1 physiological function NMNAT appears to be a multifunctional protein that sits both at the core of central metabolism and at the crossroads of multiple cellular processes Homo sapiens
2.7.7.1 physiological function NMNAT appears to be a multifunctional protein that sits both at the core of central metabolism and at the crossroads of multiple cellular processes Pseudomonas aeruginosa
2.7.7.1 physiological function NMNAT appears to be a multifunctional protein that sits both at the core of central metabolism and at the crossroads of multiple cellular processes Synechocystis sp.
2.7.7.1 physiological function NMNAT appears to be a multifunctional protein that sits both at the core of central metabolism and at the crossroads of multiple cellular processes Bacillus anthracis
2.7.7.1 physiological function NMNAT appears to be a multifunctional protein that sits both at the core of central metabolism and at the crossroads of multiple cellular processes Methanocaldococcus jannaschii
2.7.7.1 physiological function NMNAT appears to be a multifunctional protein that sits both at the core of central metabolism and at the crossroads of multiple cellular processes Methanothermobacter thermautotrophicus