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Protein

NH(3)-dependent NAD(+) synthetase

Gene

nadE

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

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
Active sitei52UniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi50 – 57ATPUniRule annotation8

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Ligandi

ATP-binding, NAD, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00253; UER00333.

Names & Taxonomyi

Protein namesi
Recommended name:
NH(3)-dependent NAD(+) synthetaseUniRule annotation (EC:6.3.1.5UniRule annotation)
Gene namesi
Name:nadEUniRule annotation
Ordered Locus Names:PA4920
OrganismiPseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Taxonomic identifieri208964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
Proteomesi
  • UP000002438 Componenti: Chromosome

Organism-specific databases

PseudoCAPiPA4920.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001521851 – 275NH(3)-dependent NAD(+) synthetaseAdd BLAST275

Proteomic databases

PaxDbiQ9HUP3.
PRIDEiQ9HUP3.

Interactioni

Protein-protein interaction databases

STRINGi208964.PA4920.

Structurei

Secondary structure

1275
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi1 – 11Combined sources11
Helixi21 – 42Combined sources22
Beta strandi46 – 51Combined sources6
Helixi55 – 75Combined sources21
Beta strandi81 – 86Combined sources6
Helixi92 – 105Combined sources14
Beta strandi108 – 112Combined sources5
Helixi116 – 123Combined sources8
Helixi127 – 129Combined sources3
Helixi134 – 160Combined sources27
Beta strandi162 – 165Combined sources4
Helixi170 – 175Combined sources6
Turni180 – 184Combined sources5
Turni190 – 193Combined sources4
Helixi196 – 205Combined sources10
Helixi210 – 213Combined sources4
Helixi238 – 245Combined sources8
Helixi252 – 264Combined sources13
Helixi266 – 269Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4XFDX-ray1.55A1-275[»]
5F23X-ray1.50A1-275[»]
ProteinModelPortaliQ9HUP3.
SMRiQ9HUP3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the NAD synthetase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4107RA1. Bacteria.
COG0171. LUCA.
HOGENOMiHOG000238070.
InParanoidiQ9HUP3.
KOiK01916.
OMAiAKIIEGW.
PhylomeDBiQ9HUP3.

Family and domain databases

CDDicd00553. NAD_synthase. 1 hit.
Gene3Di3.40.50.620. 1 hit.
HAMAPiMF_00193. NadE. 1 hit.
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.

Q9HUP3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQQIQRDIAQ ALQVQPPFQS EADVQAQIAR RIAFIQQCLK DSGLKTLVLG
60 70 80 90 100
ISGGVDSLTA GLLAQRAVEQ LREQTGDQAY RFIAVRLPYQ VQQDEADAQA
110 120 130 140 150
SLATIRADEE QTVNIGPSVK ALAEQLEALE GLEPAKSDFV IGNIKARIRM
160 170 180 190 200
VAQYAIAGAR GGLVIGTDHA AEAVMGFFTK FGDGACDLAP LSGLAKHQVR
210 220 230 240 250
ALARALGAPE NLVEKIPTAD LEDLRPGHPD EASHGVTYAE IDAFLHGQPL
260 270
REEAARVIVD TYHKTQHKRE LPKAP
Length:275
Mass (Da):29,697
Last modified:March 1, 2001 - v1
Checksum:i4CD3AE92F3FC2146
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE004091 Genomic DNA. Translation: AAG08305.1.
PIRiF83030.
RefSeqiNP_253607.1. NC_002516.2.
WP_003099998.1. NZ_ASJY01000787.1.

Genome annotation databases

EnsemblBacteriaiAAG08305; AAG08305; PA4920.
GeneIDi882213.
KEGGipae:PA4920.
PATRICi19844644. VBIPseAer58763_5153.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE004091 Genomic DNA. Translation: AAG08305.1.
PIRiF83030.
RefSeqiNP_253607.1. NC_002516.2.
WP_003099998.1. NZ_ASJY01000787.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4XFDX-ray1.55A1-275[»]
5F23X-ray1.50A1-275[»]
ProteinModelPortaliQ9HUP3.
SMRiQ9HUP3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi208964.PA4920.

Proteomic databases

PaxDbiQ9HUP3.
PRIDEiQ9HUP3.

Protocols and materials databases

DNASUi882213.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAG08305; AAG08305; PA4920.
GeneIDi882213.
KEGGipae:PA4920.
PATRICi19844644. VBIPseAer58763_5153.

Organism-specific databases

PseudoCAPiPA4920.

Phylogenomic databases

eggNOGiENOG4107RA1. Bacteria.
COG0171. LUCA.
HOGENOMiHOG000238070.
InParanoidiQ9HUP3.
KOiK01916.
OMAiAKIIEGW.
PhylomeDBiQ9HUP3.

Enzyme and pathway databases

UniPathwayiUPA00253; UER00333.

Family and domain databases

CDDicd00553. NAD_synthase. 1 hit.
Gene3Di3.40.50.620. 1 hit.
HAMAPiMF_00193. NadE. 1 hit.
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...

Entry informationi

Entry nameiNADE_PSEAE
AccessioniPrimary (citable) accession number: Q9HUP3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: March 1, 2001
Last modified: November 2, 2016
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.