NH(3)-dependent NAD(+) synthetase (P18843)

Identification
Name:NH(3)-dependent NAD(+) synthetase
Synonyms:
  • Nicotinamide adenine dinucleotide synthetase
  • NADS
  • Nitrogen regulatory protein
Gene Name:nadE
Enzyme Class:
Biological Properties
General Function:Involved in NAD+ synthase (glutamine-hydrolyzing) activity
Specific Function:Catalyzes a key step in NAD biosynthesis, transforming deamido-NAD into NAD by a two-step reaction
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Nicotinic acid adenine dinucleotide + 1.0Ammonia ↔ 1.0Adenosine monophosphate + 1.0Pyrophosphate + 1.0NAD
ReactionCard
SMPDB Reactions:
1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Pyrophosphate+1.0L-Glutamic acid+1.0Thumb+1.0Thumb
1.0Nicotinic acid adenine dinucleotide + 1.0Water + 1.0L-Glutamine + 1.0Adenosine triphosphate → 1.0Hydrogen ion + 1.0Adenosine monophosphate + 1.0Pyrophosphate + 1.0L-Glutamic acid + 1.0NAD + 1.0L-Glutamate
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Pyrophosphate+1.0Thumb
1.0Nicotinic acid adenine dinucleotide + 1.0Adenosine triphosphate + 1.0Ammonium → 1.0Hydrogen ion + 1.0Adenosine monophosphate + 1.0Pyrophosphate + 1.0NAD
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Nicotinic acid adenine dinucleotide + 1.0Ammonia ↔ 1.0Adenosine monophosphate + 1.0Pyrophosphate + 1.0NAD
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Nicotinic acid adenine dinucleotide + 1.0Ammonium → 1.0Adenosine monophosphate + 1.0Hydrogen ion + 1.0NAD + 1.0Pyrophosphate
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00045Adenosine monophosphateMetaboCard
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB00051AmmoniaMetaboCard
ECMDB21186AmmoniumMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00148L-GlutamateMetaboCard
ECMDB00641L-GlutamineMetaboCard
ECMDB00902NADMetaboCard
ECMDB01179Nicotinic acid adenine dinucleotideMetaboCard
ECMDB04142PyrophosphateMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
adenyl nucleotide binding
adenyl ribonucleotide binding
ATP binding
binding
carbon-nitrogen ligase activity, with glutamine as amido-N-donor
catalytic activity
ligase activity
ligase activity, forming carbon-nitrogen bonds
NAD+ synthase (glutamine-hydrolyzing) activity
nucleoside binding
purine nucleoside binding
Process
cellular metabolic process
coenzyme biosynthetic process
coenzyme metabolic process
cofactor metabolic process
metabolic process
NAD biosynthetic process
nicotinamide nucleotide biosynthetic process
pyridine nucleotide biosynthetic process
Gene Properties
Blattner:b1740
Gene OrientationClockwise
Centisome Percentage:39.24
Left Sequence End1820482
Right Sequence End1821309
Gene Sequence:
>828 bp
ATGAGTGTGCTCATTAATGAAAAACTGCATTCGCGGCGGCTGAAATGGCGCTGGCCGCTC
TCGCGTCAGGTGACCTTAAGCATTGGCACGTTAGCGGTTTTACTCACCGTATGGTGGACG
GTGGCGACGCTGCAACTGATTAGCCCGCTATTTTTGCCGCCGCCGCAACAGGTACTGGAA
AAACTACTCACCATTGCCGGACCGCAAGGCTTTATGGACGCCACGCTGTGGCAGCATCTG
GCAGCCAGTCTGACGCGCATTATGCTGGCGCTATTTGCAGCGGTGTTGTTCGGTATTCCG
GTCGGGATCGCGATGGGACTTAGCCCTACGGTACGCGGCATTCTGGATCCGATAATCGAG
CTTTATCGTCCGGTGCCGCCGCTGGCTTATTTGCCGCTGATGGTGATCTGGTTTGGTATT
GGTGAAACCTCGAAGATCTTACTGATCTATTTAGCGATTTTTGCACCGGTGGCGATGTCG
GCGCTGGCGGGGGTGAAAAGCGTGCAGCAGGTTCGCATTCGTGCCGCCCAGTCGCTGGGT
GCCAGCCGTGCGCAGGTGCTGTGGTTTGTCATTTTGCCCGGTGCGCTGCCGGAAATCCTC
ACCGGATTACGTATTGGTCTGGGGGTGGGCTGGTCTACGCTGGTGGCGGCGGAGCTGATT
GCCGCGACGCGCGGTTTAGGATTTATGGTTCAGTCAGCGGGTGAATTTCTCGCAACTGAC
GTGGTGCTGGCGGGGATCGCGGTGATTGCGATTATCGCCTTTCTTTTAGAACTGGGTCTG
CGCGCGTTACAGCGCCGCCTGACGCCCTGGCATGGAGAAGTACAATGA
Protein Properties
Pfam Domain Function:
Protein Residues:275
Protein Molecular Weight:30637
Protein Theoretical pI:5
PDB File:1WXI
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>NH(3)-dependent NAD(+) synthetase
MTLQQQIIKALGAKPQINAEEEIRRSVDFLKSYLQTYPFIKSLVLGISGGQDSTLAGKLC
QMAINELRLETGNESLQFIAVRLPYGVQADEQDCQDAIAFIQPDRVLTVNIKGAVLASEQ
ALREAGIELSDFVRGNEKARERMKAQYSIAGMTSGVVVGTDHAAEAITGFFTKYGDGGTD
INPLYRLNKRQGKQLLAALACPEHLYKKAPTADLEDDRPSLPDEVALGVTYDNIDDYLEG
KNVPQQVARTIENWYLKTEHKRRPPITVFDDFWKK
References
External Links:
ResourceLink
Uniprot ID:P18843
Uniprot Name:NADE_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674508
PDB ID:1WXI
Ecogene ID:EG10663
Ecocyc:EG10663
ColiBase:b1740
Kegg Gene:b1740
EchoBASE ID:EB0657
CCDB:NADE_ECOLI
BacMap:16129694
General Reference:
  • Aiba, H., Baba, T., Hayashi, K., Inada, T., Isono, K., Itoh, T., Kasai, H., Kashimoto, K., Kimura, S., Kitakawa, M., Kitagawa, M., Makino, K., Miki, T., Mizobuchi, K., Mori, H., Mori, T., Motomura, K., Nakade, S., Nakamura, Y., Nashimoto, H., Nishio, Y., Oshima, T., Saito, N., Sampei, G., Horiuchi, T., et, a. l. .. (1996). "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map." DNA Res 3:363-377. Pubmed: 9097039
  • Allibert, P., Willison, J. C., Vignais, P. M. (1987). "Complementation of nitrogen-regulatory (ntr-like) mutations in Rhodobacter capsulatus by an Escherichia coli gene: cloning and sequencing of the gene and characterization of the gene product." J Bacteriol 169:260-271. Pubmed: 3025172
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Jauch, R., Humm, A., Huber, R., Wahl, M. C. (2005). "Structures of Escherichia coli NAD synthetase with substrates and products reveal mechanistic rearrangements." J Biol Chem 280:15131-15140. Pubmed: 15699042
  • Link, A. J., Robison, K., Church, G. M. (1997). "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Electrophoresis 18:1259-1313. Pubmed: 9298646
  • Willison, J. C. (1992). "An essential gene (efg) located at 38.1 minutes on the Escherichia coli chromosome." J Bacteriol 174:5765-5766. Pubmed: 1512214
  • Willison, J. C., Tissot, G. (1994). "The Escherichia coli efg gene and the Rhodobacter capsulatus adgA gene code for NH3-dependent NAD synthetase." J Bacteriol 176:3400-3402. Pubmed: 8195100