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SWISS-2DPAGE 
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Sample Preparation and Post-separation Analysis



Searching in 'SWISS-2DPAGE' for entry matching: P18843




SWISS-2DPAGE:  P18843


P18843


General information about the entry
View entry in simple text format
Entry nameNADE_ECOLI
Primary accession numberP18843
integrated into SWISS-2DPAGE on October 31, 1999 (release 11)
2D Annotations were last modified onDecember 30, 2004 (version 2)
General Annotations were last modified on May 19, 2011 (version 9)
Name and origin of the protein
DescriptionRecName: Full=NH(3)-dependent NAD(+) synthetase; EC=6.3.1.5; AltName: Full=Nicotinamide adenine dinucleotide synthetase; Short=NADS; AltName: Full=Nitrogen regulatory protein;.
Gene nameName=nadE
Synonyms=efg, ntrL
OrderedLocusNames=b1740, JW1729
Annotated speciesEscherichia coli [TaxID: 562]
TaxonomyBacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
References
[1]   MAPPING ON GEL
PubMed=11680886; [NCBI, ExPASy, EBI, Israel, Japan]
Tonella L., Hoogland C., Binz P.-A., Appel R.D., Hochstrasser D.F., Sanchez J.-C.
''''''New perspectives in the Escherichia coli proteome investigation'';'';''
Proteomics 1(1):409-423(2001)
2D PAGE maps for identified proteins
How to interpret a protein

ECOLI5-6 {Escherichia coli(5-6)}
Escherichia coli
ECOLI5-6
  map experimental info
  protein estimated location
 
ECOLI5-6

MAP LOCATIONS:
pI=5.43; Mw=45820  [identification data]
pI=5.34; Mw=42978  [identification data]

MAPPING (identification):
Peptide mass fingerprinting [1].

Copyright
This SWISS-2DPAGE entry is copyright the Swiss Institute of Bioinformatics. There are no restrictions on its use by non-profit institutions as long as its content is in no way modified and this statement is not removed. Usage by and for commercial entities requires a license agreement (See http://world-2dpage.expasy.org/swiss-2dpage/docs/license.html or send email from legal@sib.swiss).
Cross-references
UniProtKB/Swiss-ProtP18843; NADE_ECOLI.
2D PAGE maps for identified proteins
  • How to interpret a protein map
  • You may obtain an estimated location of the protein on various 2D PAGE maps, provided the whole amino acid sequence is known. The estimation is obtained according to the computed protein's pI and Mw.
  • Warning 1: the displayed region reflects an area around the theoretical pI and molecular weight of the protein and is only provided for the user's information. It should be used with caution, as the experimental and theoretical positions of a protein may differ significantly.
  • Warning 2: the 2D PAGE map is built on demand. This may take some few seconds to be computed.



External data extracted from UniProtKB/Swiss-Prot
Extracted from UniProtKB/Swiss-Prot, release: 2011_10
Entry nameNADE_ECOLI
Primary accession numberP18843
Secondary accession number(s) P78235
Sequence was last modified on November 1, 1997 (version 2)
Annotations were last modified on October 19, 2011 (version 112)
Name and origin of the protein
DescriptionRecName: Full=NH(3)-dependent NAD(+) synthetase; EC=6.3.1.5; AltName: Full=Nicotinamide adenine dinucleotide synthetase; Short=NADS; AltName: Full=Nitrogen regulatory protein;
Gene nameName=nadE
Synonyms=efg, ntrL
OrderedLocusNames=b1740, JW1729
Encoded onName=nadE; Synonyms=efg, ntrL; OrderedLocusNames=b1740, JW1729
Keywords3D-structure; ATP-binding; Complete proteome; Direct protein sequencing; Ligase; NAD; Nucleotide-binding; Phosphoprotein; Reference proteome.
Copyright
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/help/license. Distributed under the Creative Commons Attribution-NoDerivs License
Cross-references
EMBLM15328; AAA79852.1; -; Genomic_DNA
EMBLU00096; AAC74810.1; -; Genomic_DNA
EMBLAP009048; BAA15529.1; -; Genomic_DNA
PIRD64933; D64933; .
RefSeqNP_416254.1; NC_000913.2; .
PDB1WXE; X-ray; 1.90 A; A=1-275
PDB1WXF; X-ray; 2.30 A; A=1-275
PDB1WXG; X-ray; 1.90 A; A=1-275
PDB1WXH; X-ray; 1.90 A; A=1-275
PDB1WXI; X-ray; 1.70 A; A=1-275
PDBsum1WXE; -; .
PDBsum1WXF; -; .
PDBsum1WXG; -; .
PDBsum1WXH; -; .
PDBsum1WXI; -; .
ProteinModelPortalP18843; -; .
SMRP18843; 2-275; .
DIPDIP-10295N; -; .
IntActP18843; 479; .
MINTMINT-1232772; -; .
SWISS-2DPAGEP18843; -; .
EnsemblBacteriaEBESCT00000001633; EBESCP00000001633; EBESCG00000001347; .
EnsemblBacteriaEBESCT00000017247; EBESCP00000016538; EBESCG00000016306; .
GeneID946946; -; .
GenomeReviewsAP009048_GR; JW1729; .
GenomeReviewsU00096_GR; b1740; .
KEGGecj:JW1729; -; .
KEGGeco:b1740; -; .
EchoBASEEB0657; -; .
EcoGeneEG10663; nadE; .
eggNOGCOG0171; -; .
GeneTreeEBGT00050000009560; -; .
HOGENOMHBG351567; -; .
OMAGLNKRRV; -; .
ProtClustDBPRK00768; -; .
BioCycEcoCyc:NAD-SYNTH-MONOMER; -; .
BioCycMetaCyc:NAD-SYNTH-MONOMER; -; .
DrugBankDB00131; Adenosine monophosphate; .
GenevestigatorP18843; -; .
GOGO:0005524; F:ATP binding; IEA:UniProtKB-KW; .
GOGO:0003952; F:NAD+ synthase (glutamine-hydrolyzing) activity; IEA:InterPro; .
GOGO:0008795; F:NAD+ synthase activity; IDA:EcoCyc; .
GOGO:0034628; P:de novo NAD biosynthetic process from aspartate; IDA:EcoCyc; .
GOGO:0034355; P:NAD salvage; IDA:EcoCyc; .
HAMAPMF_00193; NadE; 1; -
InterProIPR022310; NAD/GMP_synthase; .
InterProIPR003694; NAD_synthase; .
InterProIPR022926; NH(3)-dep_NAD(+)_synth; .
InterProIPR014729; Rossmann-like_a/b/a_fold; .
Gene3DG3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1; .
PfamPF02540; NAD_synthase; 1; .
TIGRFAMsTIGR00552; NadE; 1; .



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Database constructed and maintained by SIB, using the Make2D-DB II package (ver. 3.10.2) from the World-2DPAGE Constellation of the ExPASy web server