Reviewed, UniProtKB/Swiss-Prot A7ZMK7 (NADE_ECO24)

Names and origin

Protein names

Recommended name:
    NH(3)-dependent NAD(+) synthetase
    EC=6.3.1.5

Gene names

Name:	nadE
Ordered Locus Names:	EcE24377A_1961

Organism

Escherichia coli O139:H28 (strain E24377A / ETEC) [Complete proteome] [HAMAP]

Taxonomic identifier

331111 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	275 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	ATP + deamido-NAD+ + NH3 = AMP + diphosphate + NAD+. HAMAP MF_00193
Pathway	Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from deamido-NAD(+) (ammonia route): step 1/1. HAMAP MF_00193
Sequence similarities	Belongs to the NAD synthetase family.

Ontologies

Keywords
Ligand	ATP-binding NAD Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	NAD biosynthetic process Inferred from electronic annotation. Source: HAMAP
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 electronic annotation. Source: EC
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 MF_00193		PRO_1000077549
Regions
	Nucleotide binding	46 – 53	8	ATP By similarity
Sites
	Active site	48	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	A7ZMK7-1 [UniParc]. Last modified October 23, 2007. Version 1. Checksum: 38AD6EE7886A905A	FASTA	275	30,638
	10 20 30 40 50 60 MTLQQQIIKA LGAKPQINAE EEIRRSIDFL 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 QGKQLLAALG CPEHLYKKAP TADLEDDRPS LPDEVALGVT YDNIDDYLEG 250 260 270 KNVPEQVART IENWYLKTEH KRRPPITVFD DFWKK

References

[1]

"The pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates." Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J. J. Bacteriol. 190:6881-6893(2008) [PubMed: 18676672] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000800 Genomic DNA. Translation: ABV19336.1.
RefSeq	YP_001463036.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	A7ZMK7.
Genome annotation databases
GeneID	5586821.
GenomeReviews	Gene locus EcE24377A_1961 in contig CP000800_GR.
KEGG	ecw:EcE24377A_1961.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	ADLEEDR.
Family and domain databases
HAMAP	MF_00193. [Tree]
InterPro	IPR003694. NAD_synthase. IPR014729. Rossmann-like_a/b/a_fold. [Graphical view]
Gene3D	G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
Pfam	PF02540. NAD_synthase. 1 hit. [Graphical view]
TIGRFAMs	TIGR00552. nadE. 1 hit.
ProtoNet	Search...

Entry information

Entry name

NADE_ECO24

Accession

Primary (citable) accession number: A7ZMK7

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	October 23, 2007
Last modified:	November 3, 2009
This is version 15 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)