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Protein

NH(3)-dependent NAD(+) synthetase

Gene

nadE

Organism
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei55 – 551UniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi53 – 608ATPUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Ligandi

ATP-binding, NAD, Nucleotide-binding

Enzyme and pathway databases

BioCyciDRAD243230:GH46-2891-MONOMER.
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:DR_A0201
OrganismiDeinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Taxonomic identifieri243230 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciDeinococcalesDeinococcaceaeDeinococcus
Proteomesi
  • UP000002524 Componenti: Chromosome II

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 287287NH(3)-dependent NAD(+) synthetasePRO_0000152166Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi243230.DR_A0201.

Structurei

Secondary structure

1
287
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 1910Combined sources
Helixi27 – 4317Combined sources
Beta strandi49 – 535Combined sources
Helixi58 – 7619Combined sources
Beta strandi82 – 876Combined sources
Beta strandi90 – 923Combined sources
Helixi97 – 10610Combined sources
Beta strandi109 – 1135Combined sources
Helixi117 – 13115Combined sources
Helixi137 – 15923Combined sources
Beta strandi162 – 1643Combined sources
Helixi169 – 1746Combined sources
Turni179 – 1835Combined sources
Turni189 – 1924Combined sources
Helixi195 – 20410Combined sources
Helixi209 – 2113Combined sources
Helixi229 – 2335Combined sources
Helixi237 – 2448Combined sources
Helixi251 – 26313Combined sources
Helixi264 – 2674Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4Q16X-ray2.60A/B/C/D1-287[»]
ProteinModelPortaliQ9RYV5.
SMRiQ9RYV5. Positions 11-280.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the NAD synthetase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105C4K. Bacteria.
COG0171. LUCA.
HOGENOMiHOG000238070.
InParanoidiQ9RYV5.
KOiK01916.
OMAiDFVRGNI.
OrthoDBiEOG64JFM7.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
HAMAPiMF_00193. NadE.
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.

Q9RYV5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTPSPLPLSP LRSHIIRELH VQPDIDPGAE VERRVAFLCD YLQSTPTKGF
60 70 80 90 100
VLGISGGQDS TLAGRLCQLA VERRRSQGHG ATFLAVRLPY GVQADEADAQ
110 120 130 140 150
QALDFIQADR EVTVNIKEAA DASVAAAQAA LGSEVRDFVR GNVKARERMV
160 170 180 190 200
AQYALAGQEN LLVVGTDHAA EALTGFYTKY GDGGVDLTPL SGLTKRQGAQ
210 220 230 240 250
LLAHLGAPEG TWRKVPTADL EDDRPGLPDE VALGVTYAQI DAYLEGREVS
260 270 280
DEAAARLERL FLNSRHKRAL PVTPFDGWWQ PGEQKQS
Length:287
Mass (Da):31,077
Last modified:May 1, 2000 - v1
Checksum:i3258CD1549967F69
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE001825 Genomic DNA. Translation: AAF12179.1.
PIRiA75617.
RefSeqiNP_285524.1. NC_001264.1.
WP_010889460.1. NC_001264.1.

Genome annotation databases

EnsemblBacteriaiAAF12179; AAF12179; DR_A0201.
GeneIDi1797961.
KEGGidra:DR_A0201.
PATRICi21633442. VBIDeiRad64572_3090.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE001825 Genomic DNA. Translation: AAF12179.1.
PIRiA75617.
RefSeqiNP_285524.1. NC_001264.1.
WP_010889460.1. NC_001264.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4Q16X-ray2.60A/B/C/D1-287[»]
ProteinModelPortaliQ9RYV5.
SMRiQ9RYV5. Positions 11-280.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243230.DR_A0201.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAF12179; AAF12179; DR_A0201.
GeneIDi1797961.
KEGGidra:DR_A0201.
PATRICi21633442. VBIDeiRad64572_3090.

Phylogenomic databases

eggNOGiENOG4105C4K. Bacteria.
COG0171. LUCA.
HOGENOMiHOG000238070.
InParanoidiQ9RYV5.
KOiK01916.
OMAiDFVRGNI.
OrthoDBiEOG64JFM7.

Enzyme and pathway databases

UniPathwayiUPA00253; UER00333.
BioCyciDRAD243230:GH46-2891-MONOMER.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
HAMAPiMF_00193. NadE.
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...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422.

Entry informationi

Entry nameiNADE_DEIRA
AccessioniPrimary (citable) accession number: Q9RYV5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: May 1, 2000
Last modified: February 17, 2016
This is version 95 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.