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Reviewed, UniProtKB/Swiss-Prot P18843 (NADE_ECOLI)

Last modified February 9, 2010. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    NH(3)-dependent NAD(+) synthetase
    EC=6.3.1.5
Alternative name(s):
    Nitrogen regulatory protein
    Nicotinamide adenine dinucleotide synthetase
      Short name=NADS
Gene names
Name: nadE
Synonyms: efg, ntrL
Ordered Locus Names: b1740, JW1729
OrganismEscherichia coli (strain K12) [Complete proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

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

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General annotation (Comments)

Function

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

Catalytic activity

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

Pathway

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

Subunit structure

Homodimer. HAMAP MF_00193

Post-translational modification

May be phosphorylated. HAMAP MF_00193

Sequence similarities

Belongs to the NAD synthetase family.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

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

Regions

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

Sites

Binding site331NAD HAMAP MF_00193
Binding site821ATP HAMAP MF_00193
Binding site881ATP By similarity
Binding site1401NAD HAMAP MF_00193
Binding site1601ATP HAMAP MF_00193
Binding site2111ATP By similarity
Binding site2611NAD HAMAP MF_00193

Experimental info

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

Secondary structure

1 ............................................ 275
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P18843-1 [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

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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: 3025172] [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: 9097039] [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 277:1453-1474(1997) [PubMed: 9278503] [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: 16738553] [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: 9298646] [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: 1512214] [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: 8195100] [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: 15699042] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF APOPROTEIN AND COMPLEX WITH SUBSTRATES; PRODUCTS AND COFACTORS.

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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.
RefSeqAP_002359.1.
NP_416254.1.

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[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-10295N.
IntActP18843. 479 interactions.
STRINGP18843.

2-D gel databases

SWISS-2DPAGEP18843.

Genome annotation databases

GeneID946946.
GenomeReviewsGene locus JW1729 in contig AP009048_GR.
Gene locus b1740 in contig U00096_GR.
KEGGecj:JW1729.
eco:b1740.

Organism-specific databases

EchoBASEEB0657.
EcoGeneEG10663. nadE.
CMRSearch...

Phylogenomic databases

eggNOGCOG0171.
HOGENOMHBG351567.
OMAHLYEKAP.

Enzyme and pathway databases

BioCycEcoCyc:NAD-SYNTH-MONOMER.
ECOL168927:B1740-MONOMER.
MetaCyc:NAD-SYNTH-MONOMER.

Gene expression databases

GenevestigatorP18843.

Family and domain databases

HAMAPMF_00193. NadE.
[Tree]
InterProIPR003694. NAD_synthase.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
Gene3DG3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
TIGRFAMsTIGR00552. nadE. 1 hit.
ProtoNetSearch...

Other Resources

DrugBankDB00131. Adenosine monophosphate.

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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: February 9, 2010
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

Escherichia coli

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents