Q8U4I9 (NADE_PYRFU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Gene names

Name:	nadE
Ordered Locus Names:	PF0098

Organism

Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)

Taxonomic identifier

186497 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus

Protein attributes

Sequence length	257 AA.
Sequence status	Complete.
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 Reference proteome
Gene Ontology (GO)
Biological process	NAD biosynthetic process Inferred from electronic annotation. Source: InterPro
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW 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 – 257	257	NH(3)-dependent NAD(+) synthetase HAMAP MF_00193		PRO_0000152231
Regions
	Nucleotide binding	28 – 35	8	ATP By similarity
Sites
	Active site	30	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8U4I9 [UniParc]. Last modified June 1, 2002. Version 1. Checksum: 45BCEC8D1643DD41	FASTA	257	28,891
	10 20 30 40 50 60 MRRLNFEKVV TRLVEFIKEN AKQGVVIGIS GGVDSATVAY LATKALGKDK ILGLIMPYYE 70 80 90 100 110 120 NKDVEDAKLV AENLGIRYKI INIKPIVDTI QSSLDVALDR KSLGNIMARV RMVLLYSYAN 130 140 150 160 170 180 SLGRLVLGTS NRSEFLTGYF TKWGDGASDY APLINIYKTE VWEVARIIGV PQSIVEKKPS 190 200 210 220 230 240 AGLWEGQTDE DELGISYKLL DELLWRLVDL KMSKEEIANE LNVSEEIVEH VEKLVKNSEH 250 KRRLPIGPKV DDLIIEP

References

[1]	"Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences." Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M., DiRuggiero J., Robb F.T. Genetics 152:1299-1305(1999) [PubMed: 10430560] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE009950 Genomic DNA. Translation: AAL80222.1.
RefSeq	NP_577827.1. NC_003413.1.
3D structure databases
ProteinModelPortal	Q8U4I9.
SMR	Q8U4I9. Positions 1-255.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBPYRT00000005428; EBPYRP00000005289; EBPYRG00000005427.
GeneID	1467927.
GenomeReviews	Gene locus PF0098 in contig AE009950_GR.
KEGG	pfu:PF0098.
NMPDR	fig|186497.1.peg.98.
Phylogenomic databases
GeneTree	EBGT00050000022961.
HOGENOM	HBG351567.
OMA	DGAVDCH.
PhylomeDB	Q8U4I9.
ProtClustDB	PRK13980.
Family and domain databases
HAMAP	MF_00193. NadE. [Tree]
InterPro	IPR022310. NAD/GMP_synthase. IPR003694. NAD_synthase. IPR022926. NH(3)-dep_NAD(+)_synth. IPR014729. Rossmann-like_a/b/a_fold. [Graphical view]
Gene3D	G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
KO	K01916.
Pfam	PF02540. NAD_synthase. 1 hit. [Graphical view]
TIGRFAMs	TIGR00552. NadE. 1 hit.
ProtoNet	Search...

Entry information

Entry name

NADE_PYRFU

Accession

Primary (citable) accession number: Q8U4I9

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 15, 2002
Last sequence update:	June 1, 2002
Last modified:	December 14, 2011
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program