Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

NH(3)-dependent NAD(+) synthetase

Gene

nadE

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Pathway: NAD(+) biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes NAD(+) from deamido-NAD(+) (ammonia route).
Proteins known to be involved in this subpathway in this organism are:
  1. NH(3)-dependent NAD(+) synthetase (nadE), NH(3)-dependent NAD(+) synthetase (nadE)
This subpathway is part of the pathway NAD(+) biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes NAD(+) from deamido-NAD(+) (ammonia route), the pathway NAD(+) biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei33 – 331NAD1 Publication
Binding sitei82 – 821ATP1 Publication
Binding sitei88 – 881ATPBy similarity
Binding sitei140 – 1401NAD1 Publication
Binding sitei160 – 1601ATP1 Publication
Binding sitei211 – 2111ATPBy similarity
Binding sitei261 – 2611NAD1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi46 – 538ATP1 Publication
Nucleotide bindingi170 – 18011NAD1 PublicationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • 'de novo' NAD biosynthetic process from aspartate Source: EcoCyc
  • cellular response to DNA damage stimulus Source: EcoliWiki
  • NAD salvage Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Ligandi

ATP-binding, NAD, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:NAD-SYNTH-MONOMER.
ECOL316407:JW1729-MONOMER.
MetaCyc:NAD-SYNTH-MONOMER.
UniPathwayiUPA00253; UER00333.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:nadE
Synonyms:efg, ntrL
Ordered Locus Names:b1740, JW1729
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10663. nadE.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 275275NH(3)-dependent NAD(+) synthetasePRO_0000152167Add
BLAST

Post-translational modificationi

May be phosphorylated.

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP18843.
PRIDEiP18843.

2D gel databases

SWISS-2DPAGEP18843.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

DIPiDIP-10295N.
IntActiP18843. 480 interactions.
MINTiMINT-1232772.
STRINGi511145.b1740.

Structurei

Secondary structure

1
275
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 119Combined sources
Helixi19 – 3618Combined sources
Beta strandi42 – 465Combined sources
Helixi51 – 7121Combined sources
Beta strandi77 – 826Combined sources
Beta strandi85 – 873Combined sources
Helixi91 – 10111Combined sources
Beta strandi104 – 1085Combined sources
Helixi112 – 12514Combined sources
Helixi131 – 15222Combined sources
Beta strandi155 – 1584Combined sources
Helixi163 – 1664Combined sources
Turni167 – 1693Combined sources
Turni173 – 1775Combined sources
Turni183 – 1864Combined sources
Helixi189 – 19810Combined sources
Helixi203 – 2053Combined sources
Helixi224 – 2274Combined sources
Helixi231 – 2388Combined sources
Helixi245 – 25713Combined sources
Helixi259 – 2624Combined sources
Helixi272 – 2743Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WXEX-ray1.90A1-275[»]
1WXFX-ray2.30A1-275[»]
1WXGX-ray1.90A1-275[»]
1WXHX-ray1.90A1-275[»]
1WXIX-ray1.70A1-275[»]
ProteinModelPortaliP18843.
SMRiP18843. Positions 2-275.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP18843.

Family & Domainsi

Sequence similaritiesi

Belongs to the NAD synthetase family.Curated

Phylogenomic databases

eggNOGiCOG0171.
HOGENOMiHOG000238070.
InParanoidiP18843.
KOiK01916.
OMAiRHKRTVP.
OrthoDBiEOG64JFM7.
PhylomeDBiP18843.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
HAMAPiMF_00193. NadE.
InterProiIPR022310. NAD/GMP_synthase.
IPR003694. NAD_synthase.
IPR022926. NH(3)-dep_NAD(+)_synth.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamiPF02540. NAD_synthase. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00552. nadE. 1 hit.

Sequencei

Sequence statusi: Complete.

P18843-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTLQQQIIKA LGAKPQINAE EEIRRSVDFL KSYLQTYPFI KSLVLGISGG
60 70 80 90 100
QDSTLAGKLC QMAINELRLE TGNESLQFIA VRLPYGVQAD EQDCQDAIAF
110 120 130 140 150
IQPDRVLTVN IKGAVLASEQ ALREAGIELS DFVRGNEKAR ERMKAQYSIA
160 170 180 190 200
GMTSGVVVGT DHAAEAITGF FTKYGDGGTD INPLYRLNKR QGKQLLAALA
210 220 230 240 250
CPEHLYKKAP TADLEDDRPS LPDEVALGVT YDNIDDYLEG KNVPQQVART
260 270
IENWYLKTEH KRRPPITVFD DFWKK
Length:275
Mass (Da):30,637
Last modified:November 1, 1997 - v2
Checksum:i85EE6EE01C648282
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti13 – 3119AKPQI…VDFLK → ENRRLMLKRKFVVVSISE in AAA79852 (PubMed:3025172).CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15328 Genomic DNA. Translation: AAA79852.1.
U00096 Genomic DNA. Translation: AAC74810.1.
AP009048 Genomic DNA. Translation: BAA15529.1.
PIRiD64933.
RefSeqiNP_416254.1. NC_000913.3.

Genome annotation databases

EnsemblBacteriaiAAC74810; AAC74810; b1740.
BAA15529; BAA15529; BAA15529.
GeneIDi946946.
KEGGiecj:Y75_p1715.
eco:b1740.
PATRICi32118789. VBIEscCol129921_1812.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15328 Genomic DNA. Translation: AAA79852.1.
U00096 Genomic DNA. Translation: AAC74810.1.
AP009048 Genomic DNA. Translation: BAA15529.1.
PIRiD64933.
RefSeqiNP_416254.1. NC_000913.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WXEX-ray1.90A1-275[»]
1WXFX-ray2.30A1-275[»]
1WXGX-ray1.90A1-275[»]
1WXHX-ray1.90A1-275[»]
1WXIX-ray1.70A1-275[»]
ProteinModelPortaliP18843.
SMRiP18843. Positions 2-275.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-10295N.
IntActiP18843. 480 interactions.
MINTiMINT-1232772.
STRINGi511145.b1740.

2D gel databases

SWISS-2DPAGEP18843.

Proteomic databases

PaxDbiP18843.
PRIDEiP18843.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74810; AAC74810; b1740.
BAA15529; BAA15529; BAA15529.
GeneIDi946946.
KEGGiecj:Y75_p1715.
eco:b1740.
PATRICi32118789. VBIEscCol129921_1812.

Organism-specific databases

EchoBASEiEB0657.
EcoGeneiEG10663. nadE.

Phylogenomic databases

eggNOGiCOG0171.
HOGENOMiHOG000238070.
InParanoidiP18843.
KOiK01916.
OMAiRHKRTVP.
OrthoDBiEOG64JFM7.
PhylomeDBiP18843.

Enzyme and pathway databases

UniPathwayiUPA00253; UER00333.
BioCyciEcoCyc:NAD-SYNTH-MONOMER.
ECOL316407:JW1729-MONOMER.
MetaCyc:NAD-SYNTH-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP18843.
PROiP18843.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
HAMAPiMF_00193. NadE.
InterProiIPR022310. NAD/GMP_synthase.
IPR003694. NAD_synthase.
IPR022926. NH(3)-dep_NAD(+)_synth.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamiPF02540. NAD_synthase. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00552. nadE. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. 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.

Entry informationi

Entry nameiNADE_ECOLI
AccessioniPrimary (citable) accession number: P18843
Secondary accession number(s): P78235
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1997
Last modified: June 24, 2015
This is version 143 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.