Trifunctional NAD biosynthesis/regulator protein NadR

Contribute

Send feedback

Read comments (?) or add your own

P27278 (NADR_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 113. History...

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

Documents (3) |

Third-party data

text xml rdf/xml gff fasta

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

Names and origin

Protein names

Recommended name:
Trifunctional NAD biosynthesis/regulator protein NadR

Including the following 3 domains:

Transcriptional regulator NadR
Nicotinamide mononucleotide adenylyltransferase
Short name=NMN adenylyltransferase
Short name=NMN-AT
Short name=NMNAT
EC=2.7.7.1
Alternative name(s):
Nicotinamide ribonucleotide adenylyltransferase
Nicotinamide-nucleotide adenylyltransferase
Ribosylnicotinamide kinase
Short name=RNK
EC=2.7.1.22
Alternative name(s):
Nicotinamide riboside kinase
Short name=NRK
Short name=NmR-K

Gene names

Name:	nadR
Synonyms:	nadI
Ordered Locus Names:	b4390, JW5800

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	410 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	This enzyme has three activities: DNA binding, nicotinamide mononucleotide (NMN) adenylyltransferase and ribosylnicotinamide (RN) kinase. The DNA-binding domain binds to the nadB operator sequence in an NAD- and ATP-dependent manner. As NAD levels increase within the cell, the affinity of NadR for the nadB operator regions of nadA, nadB, and pncB increases, repressing the transcription of these genes. The RN kinase activity catalyzes the phosphorylation of RN to form nicotinamide ribonucleotide. The NMN adenylyltransferase activity catalyzes the transfer of the AMP moiety of ATP to nicotinamide ribonucleotide to form NAD⁺. The NMN adenylyltransferase domain also functions as the NAD and ATP sensor. Ref.6
Catalytic activity	ATP + nicotinamide ribonucleotide = diphosphate + NAD⁺. ATP + 1-(beta-D-ribofuranosyl)-nicotinamide = ADP + beta-nicotinamide D-ribonucleotide.
Enzyme regulation	Feed-back regulated by NAD. A high level of NAD causes NadR to lose enzymatic activity and repress several NAD synthetic genes; conversely, a low NAD level activates the assimilatory enzymatic activities and leads to derepression of biosynthetic genes By similarity.
Pathway	Cofactor biosynthesis; NAD(+) biosynthesis [regulation]. Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from nicotinamide D-ribonucleotide: step 1/1.
Subunit structure	Homotetramer By similarity.
Subcellular location	Cell membrane; Peripheral membrane protein. Cytoplasm By similarity.
Sequence similarities	In the central section; belongs to the bacterial NMN adenylyltransferase family. In the C-terminal section; belongs to the bacterial RNK family. Contains 1 HTH cro/C1-type DNA-binding domain.
Biophysicochemical properties	Kinetic parameters: K_M=0.7 mM for NMN Ref.6 K_M=1.7 µM for ATP pH dependence: Optimum pH is 8.6.
Sequence caution	The sequence AAA97286.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Pyridine nucleotide biosynthesis Transcription Transcription regulation
Cellular component	Cell membrane Cytoplasm Membrane
Ligand	ATP-binding DNA-binding NAD Nucleotide-binding
Molecular function	Kinase Repressor Transferase
Technical term	Complete proteome Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological_process	NAD biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway negative regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: InterPro transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transport Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW bacterial-type RNA polymerase core promoter proximal region sequence-specific DNA binding Inferred from direct assay Ref.6. Source: EcoCyc magnesium ion binding Inferred from direct assay Ref.6. Source: EcoCyc nicotinamide-nucleotide adenylyltransferase activity Inferred from direct assay Ref.6. Source: EcoCyc ribosylnicotinamide kinase 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 – 410

410

Trifunctional NAD biosynthesis/regulator protein NadR

PRO_0000149728

Regions

Domain

7 – 62

HTH cro/C1-type

DNA binding

18 – 37

H-T-H motif Probable

Nucleotide binding

70 – 73

NAD 1 By similarity

Nucleotide binding

144 – 157

NAD 1 By similarity

Nucleotide binding

177 – 179

NAD 1 By similarity

Nucleotide binding

204 – 206

NAD 1 By similarity

Nucleotide binding

259 – 261

NAD 2 By similarity

Nucleotide binding

294 – 297

NAD 2 By similarity

Region

63 – 229

167

Nicotinamide mononucleotide adenylyltransferase

Region

230 – 410

181

Ribosylnicotinamide kinase

Sites

Binding site

NAD 1 By similarity

Binding site

104

NAD 1 By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P27278 [UniParc].

Last modified February 1, 1995. Version 2.
Checksum: BCBC26CD3ABA2F99
Show »

FASTA

410

47,346

        10         20         30         40         50         60 
MSSFDYLKTA IKQQGCTLQQ VADASGMTKG YLSQLLNAKI KSPSAQKLEA LHRFLGLEFP 

        70         80         90        100        110        120 
RQKKTIGVVF GKFYPLHTGH IYLIQRACSQ VDELHIIMGF DDTRDRALFE DSAMSQQPTV 

       130        140        150        160        170        180 
PDRLRWLLQT FKYQKNIRIH AFNEEGMEPY PHGWDVWSNG IKKFMAEKGI QPDLIYTSEE 

       190        200        210        220        230        240 
ADAPQYMEHL GIETVLVDPK RTFMSISGAQ IRENPFRYWE YIPTEVKPFF VRTVAILGGE 

       250        260        270        280        290        300 
SSGKSTLVNK LANIFNTTSA WEYGRDYVFS HLGGDEIALQ YSDYDKIALG HAQYIDFAVK 

       310        320        330        340        350        360 
YANKVAFIDT DFVTTQAFCK KYEGREHPFV QALIDEYRFD LVILLENNTP WVADGLRSLG 

       370        380        390        400        410 
SSVDRKEFQN LLVEMLEENN IEFVRVEEED YDSRFLRCVE LVREMMGEQR

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes." Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R. Nucleic Acids Res. 23:2105-2119(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[2]	"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.
[3]	"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.
[4]	"Mutational analysis of the Escherichia coli serB promoter region reveals transcriptional linkage to a downstream gene." Neuwald A.F., Berg D.E., Stauffer G.V. Gene 120:1-9(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-122. Strain: K12.
[5]	Rudd K.E. Unpublished observations (JUL-1992) Cited for: IDENTIFICATION.
[6]	"The Escherichia coli NadR regulator is endowed with nicotinamide mononucleotide adenylyltransferase activity." Raffaelli N., Lorenzi T., Mariani P.L., Emanuelli M., Amici A., Ruggieri S., Magni G. J. Bacteriol. 181:5509-5511(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS NMN ADENYLYLTRANSFERASE, BIOPHYSICOCHEMICAL PROPERTIES.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U14003 Genomic DNA. Translation: AAA97286.1. Different initiation. U00096 Genomic DNA. Translation: AAC77343.2. AP009048 Genomic DNA. Translation: BAE78379.1. X63155 Genomic DNA. No translation available.
PIR	S56614.
RefSeq	NP_418807.4. NC_000913.2. YP_492520.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P27278.
SMR	P27278. Positions 5-60, 63-349.
ModBase	Search...
Protein-protein interaction databases
STRING	511145.b4390.
Proteomic databases
PaxDb	P27278.
PRIDE	P27278.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC77343; AAC77343; b4390. BAE78379; BAE78379; BAE78379.
GeneID	12931806. 948911.
KEGG	ecj:Y75_p4274. eco:b4390.
PATRIC	32124396. VBIEscCol129921_4538.
Organism-specific databases
EchoBASE	EB1311.
EcoGene	EG11335. nadR.
Phylogenomic databases
eggNOG	COG3172.
HOGENOM	HOG000127874.
KO	K06211.
OMA	QAQYIDF.
ProtClustDB	PRK08099.
Enzyme and pathway databases
BioCyc	EcoCyc:PD04413. ECOL316407:JW5800-MONOMER. MetaCyc:PD04413.
UniPathway	UPA00253; UER00600. UPA00253.
Gene expression databases
Genevestigator	P27278.
Family and domain databases
Gene3D	1.10.260.40. 1 hit. 3.40.50.620. 1 hit.
InterPro	IPR016429. Bifunc_transcrip_reg_NadR. IPR004821. Cyt_trans-like. IPR001387. HTH. IPR010982. Lambda_DNA-bd_dom. IPR006417. NadR_NMN_Atrans. IPR027417. P-loop_NTPase. IPR014729. Rossmann-like_a/b/a_fold. [Graphical view]
Pfam	PF01381. HTH_3. 1 hit. [Graphical view]
PIRSF	PIRSF004776. NadR_NMNAT/RNK. 1 hit.
SMART	SM00530. HTH_XRE. 1 hit. [Graphical view]
SUPFAM	SSF47413. Lambda_like_DNA. 1 hit. SSF52540. SSF52540. 1 hit.
TIGRFAMs	TIGR00125. cyt_tran_rel. 1 hit. TIGR01526. nadR_NMN_Atrans. 1 hit.
PROSITE	PS50943. HTH_CROC1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NADR_ECOLI

Accession

Primary (citable) accession number: P27278
Secondary accession number(s): P76819, Q2M5S7

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	February 1, 1995
Last modified:	May 29, 2013
This is version 113 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

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

Including the following 3 domains:

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction 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

Entry information

Relevant documents