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UniProtKB/Swiss-Prot entry P18843

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name NADE_ECOLI
Primary accession number P18843
Secondary accession number P78235
Integrated into Swiss-Prot on November 1, 1990
Sequence was last modified on November 1, 1997 (Sequence version 2)
Annotations were last modified on    June 10, 2008 (Entry version 82)
Name and origin of the protein
Protein name NH(3)-dependent NAD(+) synthetase
Synonyms EC 6.3.1.5
Nitrogen regulatory protein
Nicotinamide adenine dinucleotide synthetase
NADS
Gene name
Name: nadE
Synonyms: efg, ntrL
OrderedLocusNames: b1740, JW1729
From
Escherichia coli (strain K12) [TaxID: 83333] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3025172 [NCBI, ExPASy, EBI, Israel, Japan]
Allibert P., Willison J.C., Vignais P.M.;
"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(1987).
[2]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1093/dnares/3.6.363; PubMed=9097039 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"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(1996).
[3]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1474(1997).
[4]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan]
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[5]
 PROTEIN SEQUENCE OF 1-12.
STRAIN=K12 / EMG2;
PubMed=9298646 [NCBI, ExPASy, EBI, Israel, Japan]
Link A.J., Robison K., Church G.M.;
"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12.";
Electrophoresis 18:1259-1313(1997).
[6]
 GENE MAPPING.
PubMed=1512214 [NCBI, ExPASy, EBI, Israel, Japan]
Willison J.C.;
"An essential gene (efg) located at 38.1 minutes on the Escherichia coli chromosome.";
J. Bacteriol. 174:5765-5766(1992).
[7]
 CHARACTERIZATION.
PubMed=8195100 [NCBI, ExPASy, EBI, Israel, Japan]
Willison J.C., Tissot G.;
"The Escherichia coli efg gene and the Rhodobacter capsulatus adgA gene code for NH3-dependent NAD synthetase.";
J. Bacteriol. 176:3400-3402(1994).
[8]
 X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF APOPROTEIN AND COMPLEX WITH SUBSTRATES; PRODUCTS AND COFACTORS.
DOI=10.1074/jbc.M413195200; PubMed=15699042 [NCBI, ExPASy, EBI, Israel, Japan]
Jauch R., Humm A., Huber R., Wahl M.C.;
"Structures of Escherichia coli NAD synthetase with substrates and products reveal mechanistic rearrangements.";
J. Biol. Chem. 280:15131-15140(2005).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M15328; AAA79852.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC74810.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAA15529.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR D64933; D64933.
RefSeq AP_002359.1; -.
NP_416254.1; -.
3D structure databases
PDB
1WXE; X-ray; 1.90 A; A=1-275.[ExPASy / RCSB / EBI]
1WXF; X-ray; 2.30 A; A=1-275.[ExPASy / RCSB / EBI]
1WXG; X-ray; 1.90 A; A=1-275.[ExPASy / RCSB / EBI]
1WXH; X-ray; 1.90 A; A=1-275.[ExPASy / RCSB / EBI]
1WXI; X-ray; 1.70 A; A=1-275.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1WXE; -.
1WXF; -.
1WXG; -.
1WXH; -.
1WXI; -.
ModBase P18843.
Protein-protein interaction databases
DIP DIP:10295N; -.
IntAct P18843; -.
Enzyme and pathway databases
BioCyc EcoCyc:NAD-SYNTH-MON; -.
2D gel databases
SWISS-2DPAGE P18843; -.
Organism-specific databases
EchoBASE EB0657; -.
EcoGene EG10663; nadE.
Ontologies
GO
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
QuickGo view.
Family and domain databases
HAMAP MF_00193; -; 1.
PBIL [Tree]
InterPro IPR003694; NAD_synthase.
IPR014729; Rossmann-like_a/b/a_fold.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1.
Pfam PF02540; NAD_synthase; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR00552; nadE; 1.
BLOCKS P18843.
Genome annotation databases
GeneID 946946; -.
GenomeReviews U00096_GR; b1740.
AP009048_GR; JW1729.
KEGG ecj:JW1729; -.
eco:b1740; -.
Phylogenomic databases
HOGENOM P18843; -.
Other
DrugBank DB00131; Adenosine monophosphate.
Genome annotation databases
CMR P18843; b1740.
Other
ProtoNet P18843.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; ATP-binding; Complete proteome; Direct protein sequencing; Ligase; NAD; Nucleotide-binding; Phosphoprotein.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   275  275     NH(3)-dependent NAD(+) synthetase. PRO_0000152167
NP_BIND   46    53  8     ATP. 
NP_BIND   170   180  11     NAD. 
BINDING   33    33        NAD. 
BINDING   82    82        ATP. 
BINDING   88    88        ATP (By similarity). 
BINDING   140   140        NAD. 
BINDING   160   160        ATP. 
BINDING   211   211        ATP (By similarity). 
BINDING   261   261        NAD. 
CONFLICT   13    31        AKPQINAEEEIRRSVDFLK -> ENRRLMLKRKFVVVSISE (in Ref. 1; AAA79852). 
HELIX   3    11  9      
HELIX   19    36  18      
STRAND   42    46  5      
HELIX   51    71  21      
STRAND   77    82  6      
STRAND   85    87  3      
HELIX   91   101  11      
STRAND   104   108  5      
HELIX   112   125  14      
HELIX   131   152  22      
STRAND   155   158  4      
HELIX   163   166  4      
TURN   167   169  3      
TURN   173   177  5      
TURN   183   186  4      
HELIX   189   198  10      
HELIX   203   205  3      
STRAND   226   229  4      
HELIX   231   238  8      
HELIX   245   257  13      
HELIX   259   262  4      
HELIX   272   274  3      
Sequence information
Length: 275 AA [This is the length of the unprocessed precursor] Molecular weight: 30637 Da [This is the MW of the unprocessed precursor] CRC64: 85EE6EE01C648282 [This is a checksum on the sequence] 
        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
P18843 in FASTA format

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