NH(3)-dependent NAD(+) synthetase - Escherichia coli (strain K12)

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P18843 (NADE_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 127. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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 names

Name:	nadE
Synonyms:	efg, ntrL
Ordered Locus Names:	b1740, JW1729

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	275 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes a key step in NAD biosynthesis, transforming deamido-NAD into NAD by a two-step reaction. HAMAP-Rule MF_00193
Catalytic activity	ATP + deamido-NAD⁺ + NH₃ = AMP + diphosphate + NAD⁺. HAMAP-Rule MF_00193
Pathway	Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from deamido-NAD(+) (ammonia route): step 1/1. HAMAP-Rule MF_00193
Subunit structure	Homodimer.
Post-translational modification	May be phosphorylated. HAMAP-Rule MF_00193
Sequence similarities	Belongs to the NAD synthetase family.

Ontologies

Keywords
Ligand	ATP-binding NAD Nucleotide-binding
Molecular function	Ligase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	NAD salvage Inferred from direct assay PubMed 10544053. Source: EcoCyc de novo NAD biosynthetic process from aspartate Inferred from direct assay PubMed 10544053. Source: EcoCyc response to DNA damage stimulus Inferred from expression pattern PubMed 11967071. Source: EcoliWiki
Molecular_function	ATP binding Inferred from electronic annotation. Source: HAMAP NAD+ synthase (glutamine-hydrolyzing) activity Inferred from electronic annotation. Source: InterPro NAD+ synthase activity Inferred from direct assay PubMed 10544053. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 275

275

NH(3)-dependent NAD(+) synthetase HAMAP-Rule MF_00193

PRO_0000152167

Regions

Nucleotide binding

46 – 53

ATP HAMAP-Rule MF_00193

Nucleotide binding

170 – 180

NAD HAMAP-Rule MF_00193

Sites

Binding site

NAD

Binding site

ATP

Binding site

ATP By similarity

Binding site

140

NAD

Binding site

160

ATP

Binding site

211

ATP By similarity

Binding site

261

NAD

Experimental info

Sequence conflict

13 – 31

AKPQI…VDFLK → ENRRLMLKRKFVVVSISE in AAA79852. Ref.1

Secondary structure

275

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P18843 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 85EE6EE01C648282
Show »

FASTA

275

30,637

        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

References

	« Hide 'large scale' referencesShow '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] [Europe PMC] [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. Horiuchi T. DNA Res. 3:363-377(1996) [PubMed] [Europe PMC] [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] [Europe PMC] [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] [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; PRODUCTS AND COFACTORS.
+	Additional computationally mapped references.

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.

PIR

D64933.

RefSeq

NP_416254.1. NC_000913.2.
YP_490001.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1WXE	X-ray	1.90	A	1-275	[»]
1WXF	X-ray	2.30	A	1-275	[»]
1WXG	X-ray	1.90	A	1-275	[»]
1WXH	X-ray	1.90	A	1-275	[»]
1WXI	X-ray	1.70	A	1-275	[»]

ProteinModelPortal

P18843.

SMR

P18843. Positions 2-275.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-10295N.

IntAct

P18843. 479 interactions.

MINT

MINT-1232772.

STRING

511145.b1740.

2D gel databases

SWISS-2DPAGE

P18843.

Proteomic databases

PaxDb

P18843.

PRIDE

P18843.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC74810; AAC74810; b1740.
BAA15529; BAA15529; BAA15529.

GeneID

12933235.
946946.

KEGG

ecj:Y75_p1715.
eco:b1740.

PATRIC

32118789. VBIEscCol129921_1812.

Organism-specific databases

EchoBASE

EB0657.

EcoGene

EG10663. nadE.

Phylogenomic databases

eggNOG

COG0171.

HOGENOM

HOG000238070.

K01916.

OMA

DFVRGNI.

ProtClustDB

PRK00768.

Enzyme and pathway databases

BioCyc

EcoCyc:NAD-SYNTH-MONOMER.
ECOL316407:JW1729-MONOMER.
MetaCyc:NAD-SYNTH-MONOMER.

UniPathway

UPA00253; UER00333.

Gene expression databases

Genevestigator

P18843.

Family and domain databases

Gene3D

3.40.50.620. 1 hit.

HAMAP

MF_00193. NadE.

InterPro

IPR022310. NAD/GMP_synthase.
IPR003694. NAD_synthase.
IPR022926. NH(3)-dep_NAD(+)_synth.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]

Pfam

PF02540. NAD_synthase. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00552. nadE. 1 hit.

ProtoNet

Search...

Other

DrugBank

DB00131. Adenosine monophosphate.

EvolutionaryTrace

P18843.

Entry information

Entry name

NADE_ECOLI

Accession

Primary (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:	May 1, 2013
This is version 127 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

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·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents