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Protein

NH(3)-dependent NAD(+) synthetase

Gene

nadE

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

Functioni

Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source.UniRule annotation1 Publication

Catalytic activityi

ATP + deamido-NAD+ + NH3 = AMP + diphosphate + NAD+.UniRule annotation1 Publication

Pathwayi: NAD(+) biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes NAD(+) from deamido-NAD(+) (ammonia route).UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. 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)DescriptionActionsGraphical viewLength
Binding sitei33Deamido-NADCombined sources1 Publication1
Metal bindingi52MagnesiumUniRule annotationCombined sources1 Publication1
Binding sitei82ATPCombined sources1 Publication1
Binding sitei88ATPCombined sources1 Publication1
Binding sitei136Deamido-NADCombined sources1 Publication1
Binding sitei140Deamido-NADUniRule annotationCombined sources1 Publication1
Binding sitei160ATPUniRule annotationCombined sources1 Publication1
Metal bindingi165MagnesiumUniRule annotationCombined sources1 Publication1
Binding sitei173Deamido-NADUniRule annotationCombined sources1 Publication1
Binding sitei180Deamido-NADUniRule annotationCombined sources1 Publication1
Binding sitei189ATPUniRule annotationCombined sources1 Publication1
Binding sitei211ATP; via amide nitrogen and carbonyl oxygenUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi46 – 53ATPUniRule annotationCombined sources1 Publication8
Nucleotide bindingi260 – 261Deamido-NADUniRule annotationCombined sources1 Publication2

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

Keywordsi

Molecular functionLigase
LigandATP-binding, Magnesium, Metal-binding, NAD, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:NAD-SYNTH-MONOMER
MetaCyc:NAD-SYNTH-MONOMER
UniPathwayiUPA00253; UER00333

Names & Taxonomyi

Protein namesi
Recommended name:
NH(3)-dependent NAD(+) synthetase1 PublicationUniRule annotation (EC:6.3.1.5UniRule annotation1 Publication)
Alternative name(s):
Nicotinamide adenine dinucleotide synthetase
Short name:
NADS
Nitrogen regulatory protein
Gene namesi
Name:nadE1 PublicationUniRule annotation
Synonyms:efg1 Publication, ntrL
Ordered Locus Names:b1740, JW1729
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10663 nadE

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc

Pathology & Biotechi

Chemistry databases

DrugBankiDB04099 Deamido-Nad+
DB04160 Diphosphate

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001521671 – 275NH(3)-dependent NAD(+) synthetaseAdd BLAST275

Post-translational modificationi

May be phosphorylated.

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP18843
PaxDbiP18843
PRIDEiP18843

2D gel databases

SWISS-2DPAGEiP18843

Interactioni

Subunit structurei

Homodimer.UniRule annotation2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
dnaAP030043EBI-548960,EBI-548951

Protein-protein interaction databases

BioGridi426222932 interactors.
DIPiDIP-10295N
IntActiP18843 479 interactors.
STRINGi316385.ECDH10B_1878

Structurei

Secondary structure

1275
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 11Combined sources9
Helixi19 – 36Combined sources18
Beta strandi42 – 46Combined sources5
Helixi51 – 71Combined sources21
Beta strandi77 – 82Combined sources6
Beta strandi85 – 87Combined sources3
Helixi91 – 101Combined sources11
Beta strandi104 – 108Combined sources5
Helixi112 – 125Combined sources14
Helixi131 – 152Combined sources22
Beta strandi155 – 158Combined sources4
Helixi163 – 166Combined sources4
Turni167 – 169Combined sources3
Turni173 – 177Combined sources5
Turni183 – 186Combined sources4
Helixi189 – 198Combined sources10
Helixi203 – 205Combined sources3
Helixi224 – 227Combined sources4
Helixi231 – 238Combined sources8
Helixi245 – 257Combined sources13
Helixi259 – 262Combined sources4
Helixi272 – 274Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP18843

Family & Domainsi

Sequence similaritiesi

Belongs to the NAD synthetase family.UniRule annotationCurated

Phylogenomic databases

eggNOGiENOG4107RA1 Bacteria
COG0171 LUCA
HOGENOMiHOG000238070
InParanoidiP18843
KOiK01916
OMAiCAINPIG
PhylomeDBiP18843

Family and domain databases

CDDicd00553 NAD_synthase, 1 hit
Gene3Di3.40.50.6201 hit
HAMAPiMF_00193 NadE_ammonia_dep, 1 hit
InterProiView protein in InterPro
IPR022310 NAD/GMP_synthase
IPR003694 NAD_synthase
IPR022926 NH(3)-dep_NAD(+)_synth
IPR014729 Rossmann-like_a/b/a_fold
PANTHERiPTHR23090 PTHR23090, 1 hit
PfamiView protein in Pfam
PF02540 NAD_synthase, 1 hit
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)DescriptionActionsGraphical viewLength
Sequence conflicti13 – 31AKPQI…VDFLK → ENRRLMLKRKFVVVSISE in AAA79852 (PubMed:3025172).CuratedAdd BLAST19

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
WP_000175026.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC74810; AAC74810; b1740
BAA15529; BAA15529; BAA15529
GeneIDi946946
KEGGiecj:JW1729
eco:b1740
PATRICifig|1411691.4.peg.516

Similar proteinsi

Entry informationi

Entry nameiNADE_ECOLI
AccessioniPrimary (citable) accession number: P18843
Secondary accession number(s): P78235
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1997
Last modified: March 28, 2018
This is version 161 of the entry and version 2 of the sequence. See 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