NH(3)-dependent NAD(+) synthetase

Details

Name
NH(3)-dependent NAD(+) synthetase
Synonyms
  • 6.3.1.5
  • efg
  • NADS
  • Nicotinamide adenine dinucleotide synthetase
  • Nitrogen regulatory protein
  • ntrL
Gene Name
nadE
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0010928|NH(3)-dependent NAD(+) synthetase
MTLQQQIIKALGAKPQINAEEEIRRSVDFLKSYLQTYPFIKSLVLGISGGQDSTLAGKLC
QMAINELRLETGNESLQFIAVRLPYGVQADEQDCQDAIAFIQPDRVLTVNIKGAVLASEQ
ALREAGIELSDFVRGNEKARERMKAQYSIAGMTSGVVVGTDHAAEAITGFFTKYGDGGTD
INPLYRLNKRQGKQLLAALACPEHLYKKAPTADLEDDRPSLPDEVALGVTYDNIDDYLEG
KNVPQQVARTIENWYLKTEHKRRPPITVFDDFWKK
Number of residues
275
Molecular Weight
30636.56
Theoretical pI
5.24
GO Classification
Functions
ATP binding / NAD+ synthase (glutamine-hydrolyzing) activity / NAD+ synthase activity
Processes
'de novo' NAD biosynthetic process from aspartate / cellular response to DNA damage stimulus / NAD salvage
Components
cytosol
General Function
Nad+ synthase activity
Specific Function
Catalyzes a key step in NAD biosynthesis, transforming deamido-NAD into NAD by a two-step reaction.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0010929|NH(3)-dependent NAD(+) synthetase (nadE)
ATGACATTGCAACAACAAATAATAAAGGCGCTGGGCGCAAAACCGCAGATTAATGCTGAA
GAGGAAATTCGTCGTAGTGTCGATTTTCTGAAAAGCTACCTGCAAACTTATCCGTTCATT
AAATCACTGGTGCTCGGGATCAGCGGCGGTCAGGACTCCACGCTTGCCGGAAAGCTGTGC
CAGATGGCGATTAATGAGCTGCGCCTGGAAACCGGCAACGAATCACTGCAATTTATTGCC
GTACGCCTGCCCTATGGTGTTCAGGCCGACGAACAAGATTGCCAGGATGCCATTGCCTTT
ATTCAACCGGATCGCGTATTAACCGTTAATATCAAGGGCGCGGTATTGGCCAGCGAACAG
GCATTGCGGGAAGCAGGCATTGAACTGAGCGATTTTGTCCGTGGCAATGAAAAAGCGCGT
GAGCGGATGAAAGCACAATATAGCATTGCGGGTATGACCAGCGGTGTCGTGGTGGGCACC
GATCATGCAGCAGAAGCCATTACCGGATTCTTCACTAAATATGGTGACGGCGGTACGGAC
ATTAATCCGCTGTATCGTCTCAACAAACGTCAGGGTAAACAGTTACTGGCGGCATTAGCT
TGCCCGGAACACCTTTATAAGAAAGCGCCAACGGCCGATCTGGAAGATGATCGCCCTTCT
CTGCCAGATGAAGTGGCACTCGGCGTGACCTATGACAATATCGACGACTATCTGGAAGGG
AAAAACGTACCTCAACAGGTCGCCAGAACAATAGAGAACTGGTATCTGAAAACCGAACAT
AAACGCCGTCCGCCAATTACCGTTTTCGATGATTTCTGGAAAAAGTAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP18843
UniProtKB Entry NameNADE_ECOLI
GenBank Protein ID146974
GenBank Gene IDM15328
General References
  1. Allibert P, Willison JC, Vignais PM: 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. 1987 Jan;169(1):260-71. [Article]
  2. 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 al.: 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. 1996 Dec 31;3(6):363-77. [Article]
  3. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
  4. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
  5. Link AJ, Robison K, Church GM: Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12. Electrophoresis. 1997 Aug;18(8):1259-313. [Article]
  6. Willison JC: An essential gene (efg) located at 38.1 minutes on the Escherichia coli chromosome. J Bacteriol. 1992 Sep;174(17):5765-6. [Article]
  7. Willison JC, Tissot G: The Escherichia coli efg gene and the Rhodobacter capsulatus adgA gene code for NH3-dependent NAD synthetase. J Bacteriol. 1994 Jun;176(11):3400-2. [Article]
  8. Jauch R, Humm A, Huber R, Wahl MC: Structures of Escherichia coli NAD synthetase with substrates and products reveal mechanistic rearrangements. J Biol Chem. 2005 Apr 15;280(15):15131-40. Epub 2005 Feb 7. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB02937Gamma-Arsono-Beta, Gamma-Methyleneadenosine-5'-DiphosphateexperimentalunknownDetails
DB04099Deamido-Nad+experimentalunknownDetails