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P18843 (NADE_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
NH(3)-dependent NAD(+) synthetase

EC=6.3.1.5
Alternative name(s):
Nicotinamide adenine dinucleotide synthetase
Short name=NADS
Nitrogen regulatory protein
Gene names
Name:nadE
Synonyms:efg, ntrL
Ordered Locus Names:b1740, JW1729
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length275 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes a key step in NAD biosynthesis, transforming deamido-NAD into NAD by a two-step reaction. HAMAP-Rule MF_00193

Catalytic activity

ATP + deamido-NAD+ + NH3 = AMP + diphosphate + NAD+. HAMAP-Rule MF_00193

Pathway

Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from deamido-NAD(+) (ammonia route): step 1/1. HAMAP-Rule MF_00193

Subunit structure

Homodimer.

Post-translational modification

May be phosphorylated. HAMAP-Rule MF_00193

Sequence similarities

Belongs to the NAD synthetase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 275275NH(3)-dependent NAD(+) synthetase HAMAP-Rule MF_00193
PRO_0000152167

Regions

Nucleotide binding46 – 538ATP HAMAP-Rule MF_00193
Nucleotide binding170 – 18011NAD HAMAP-Rule MF_00193

Sites

Binding site331NAD
Binding site821ATP
Binding site881ATP By similarity
Binding site1401NAD
Binding site1601ATP
Binding site2111ATP By similarity
Binding site2611NAD

Experimental info

Sequence conflict13 – 3119AKPQI…VDFLK → ENRRLMLKRKFVVVSISE in AAA79852. Ref.1

Secondary structure

............................................ 275
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P18843 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 85EE6EE01C648282

FASTA27530,637
        10         20         30         40         50         60 
MTLQQQIIKA LGAKPQINAE EEIRRSVDFL KSYLQTYPFI KSLVLGISGG QDSTLAGKLC 

        70         80         90        100        110        120 
QMAINELRLE TGNESLQFIA VRLPYGVQAD EQDCQDAIAF IQPDRVLTVN IKGAVLASEQ 

       130        140        150        160        170        180 
ALREAGIELS DFVRGNEKAR ERMKAQYSIA GMTSGVVVGT DHAAEAITGF FTKYGDGGTD 

       190        200        210        220        230        240 
INPLYRLNKR QGKQLLAALA CPEHLYKKAP TADLEDDRPS LPDEVALGVT YDNIDDYLEG 

       250        260        270 
KNVPQQVART IENWYLKTEH KRRPPITVFD DFWKK 

« Hide

References

« Hide 'large scale' references
[1]"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."
Allibert P., Willison J.C., Vignais P.M.
J. Bacteriol. 169:260-271(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"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."
Aiba H., Baba T., Fujita K., 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. expand/collapse author list , Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T.
DNA Res. 3:363-377(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, 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.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
Link A.J., Robison K., Church G.M.
Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-12.
Strain: K12 / EMG2.
[6]"An essential gene (efg) located at 38.1 minutes on the Escherichia coli chromosome."
Willison J.C.
J. Bacteriol. 174:5765-5766(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: GENE MAPPING.
[7]"The Escherichia coli efg gene and the Rhodobacter capsulatus adgA gene code for NH3-dependent NAD synthetase."
Willison J.C., Tissot G.
J. Bacteriol. 176:3400-3402(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[8]"Structures of Escherichia coli NAD synthetase with substrates and products reveal mechanistic rearrangements."
Jauch R., Humm A., Huber R., Wahl M.C.
J. Biol. Chem. 280:15131-15140(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF APOPROTEIN AND COMPLEX WITH SUBSTRATES; PRODUCTS AND COFACTOR.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M15328 Genomic DNA. Translation: AAA79852.1.
U00096 Genomic DNA. Translation: AAC74810.1.
AP009048 Genomic DNA. Translation: BAA15529.1.
PIRD64933.
RefSeqNP_416254.1. NC_000913.3.
YP_490001.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1WXEX-ray1.90A1-275[»]
1WXFX-ray2.30A1-275[»]
1WXGX-ray1.90A1-275[»]
1WXHX-ray1.90A1-275[»]
1WXIX-ray1.70A1-275[»]
ProteinModelPortalP18843.
SMRP18843. Positions 2-275.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-10295N.
IntActP18843. 480 interactions.
MINTMINT-1232772.
STRING511145.b1740.

Chemistry

DrugBankDB00131. Adenosine monophosphate.

2D gel databases

SWISS-2DPAGEP18843.

Proteomic databases

PaxDbP18843.
PRIDEP18843.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC74810; AAC74810; b1740.
BAA15529; BAA15529; BAA15529.
GeneID12933235.
946946.
KEGGecj:Y75_p1715.
eco:b1740.
PATRIC32118789. VBIEscCol129921_1812.

Organism-specific databases

EchoBASEEB0657.
EcoGeneEG10663. nadE.

Phylogenomic databases

eggNOGCOG0171.
HOGENOMHOG000238070.
KOK01916.
OMAGQILREM.
OrthoDBEOG64JFM7.
PhylomeDBP18843.

Enzyme and pathway databases

BioCycEcoCyc:NAD-SYNTH-MONOMER.
ECOL316407:JW1729-MONOMER.
MetaCyc:NAD-SYNTH-MONOMER.
UniPathwayUPA00253; UER00333.

Gene expression databases

GenevestigatorP18843.

Family and domain databases

Gene3D3.40.50.620. 1 hit.
HAMAPMF_00193. NadE.
InterProIPR022310. NAD/GMP_synthase.
IPR003694. NAD_synthase.
IPR022926. NH(3)-dep_NAD(+)_synth.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamPF02540. NAD_synthase. 1 hit.
[Graphical view]
TIGRFAMsTIGR00552. nadE. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP18843.
PROP18843.

Entry information

Entry nameNADE_ECOLI
AccessionPrimary (citable) accession number: P18843
Secondary accession number(s): P78235
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1997
Last modified: May 14, 2014
This is version 136 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene