ADP-ribose pyrophosphatase - Escherichia coli (strain K12)

Contribute

Send feedback

Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q93K97 (ADPP_ECOLI)

Last modified June 16, 2009. Version 63. History...

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

Documents (3) |

Third-party data |

Customize display

text xml rdf/xml gff fasta

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein names

Recommended name:
    ADP-ribose pyrophosphatase
    EC=3.6.1.13
Alternative name(s):
    ADP-ribose diphosphatase
    Adenosine diphosphoribose pyrophosphatase
      Short name=ADPR-PPase
    ADP-ribose phosphohydrolase
      Short name=ASPPase

Gene names

Name:	nudF
Synonyms:	aspP, yqiE, yzzG
Ordered Locus Names:	b3034, JW3002

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Hide | Top

Protein attributes

Sequence length	209 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

Hide | Top

General annotation (Comments)

Function	Acts on ADP-mannose and ADP-glucose as well as ADP-ribose. Prevents glycogen biosynthesis. The reaction catalyzed by this enzyme is a limiting step of the gluconeogenic process. Ref.1
Catalytic activity	ADP-ribose + H₂O = AMP + D-ribose 5-phosphate.
Cofactor	Binds 3 magnesium ions per subunit.
Enzyme regulation	Inhibited by phosphorylated compounds such as AMP, ADP, ATP, 3-phosphoglyceric acid and PPi. Not inhibited by orthophosphate. Activity is high in cells grown in low glucose concentrations and decreases dramatically as glucose concentration increases.
Subunit structure	Homodimer.
Sequence similarities	Belongs to the Nudix hydrolase family. NudF subfamily.

Hide | Top

Ontologies

Keywords
Ligand	Magnesium Manganese Metal-binding Zinc
Molecular function	Hydrolase
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Cellular component	cytosol Inferred from direct assay. Source: UniProtKB
Molecular function	ADP-ribose diphosphatase activity Inferred from electronic annotation. Source: EC magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Hide | Top

Binary interactions

With	Entry	#Exp.	IntAct	Notes
sgbH	P37678	1	EBI-562814,EBI-555448

Hide | Top

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 209

209

ADP-ribose pyrophosphatase

PRO_0000057042

Regions

Motif

97 – 118

Nudix box

Sites

Active site

162

Proton acceptor

Metal binding

112

Magnesium 1

Metal binding

112

Magnesium 2

Metal binding

116

Magnesium 1

Metal binding

116

Magnesium 3

Metal binding

164

Magnesium 1

Experimental info

Sequence conflict

L → V in CAC44036. Ref.1

Sequence conflict

N → S in CAC44036. Ref.1

Secondary structure

209

Helix Strand Turn

Details...

Hide | Top

Sequences

Sequence

Length

Mass (Da)

Tools

Q93K97-1 [UniParc].

Last modified April 13, 2004. Version 2.
Checksum: 2CF77EA9D63B9615
Show »

FASTA

209

23,667

        10         20         30         40         50         60 
MLKPDNLPVT FGKNDVEIIA RETLYRGFFS LDLYRFRHRL FNGQMSHEVR REIFERGHAA 

        70         80         90        100        110        120 
VLLPFDPVRD EVVLIEQIRI AAYDTSETPW LLEMVAGMIE EGESVEDVAR REAIEEAGLI 

       130        140        150        160        170        180 
VKRTKPVLSF LASPGGTSER SSIMVGEVDA TTASGIHGLA DENEDIRVHV VSREQAYQWV 

       190        200 
EEGKIDNAAS VIALQWLQLH HQALKNEWA

« Hide

Hide | Top

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Adenosine diphosphate sugar pyrophosphatase prevents glycogen biosynthesis in Escherichia coli." Moreno-Bruna B., Baroja-Fernandez E., Munoz F.J., Bastarrica-Berasategui A., Zandueta-Criado A., Rodriguez-Lopez M., Lasa I., Akazawa T., Pozueta-Romero J. Proc. Natl. Acad. Sci. U.S.A. 98:8128-8132(2001) [PubMed: 11416161] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-15, FUNCTION. Strain: BL21.
[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: 9278503] [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: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"Identification of the cpdA gene encoding cyclic 3',5'-adenosine monophosphate phosphodiesterase in Escherichia coli." Imamura R., Yamanaka K., Ogura T., Hiraga S., Fujita N., Ishihama A., Niki H. J. Biol. Chem. 271:25423-25429(1996) [PubMed: 8810311] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 98-209. Strain: K12.
[5]	"Studies on the ADP-ribose pyrophosphatase subfamily of the nudix hydrolases and tentative identification of trgB, a gene associated with tellurite resistance." Dunn C.A., O'Handley S.F., Frick D.N., Bessman M.J. J. Biol. Chem. 274:32318-32324(1999) [PubMed: 10542272] [Abstract] Cited for: CHARACTERIZATION. Strain: K12 / MG1655 / ATCC 47076.
[6]	"The structure of ADP-ribose pyrophosphatase reveals the structural basis for the versatility of the Nudix family." Gabelli S.B., Bianchet M.A., Bessman M.J., Amzel L.M. Nat. Struct. Biol. 8:467-472(2001) [PubMed: 11323725] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF NATIVE ENZYME, COMPLEX WITH ADP-RIBOSE, COMPLEX WITH GADOLINIUM.
[7]	"Mechanism of the Escherichia coli ADP-ribose pyrophosphatase, a Nudix hydrolase." Gabelli S.B., Bianchet M.A., Ohnishi Y., Ichikawa Y., Bessman M.J., Amzel L.M. Biochemistry 41:9279-9285(2002) [PubMed: 12135348] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.07 ANGSTROMS), CATALYTIC MECHANISM.

Hide | Top

Cross-references

Sequence databases

AJ298136 Genomic DNA. Translation: CAC44036.1.
U28377 Genomic DNA. Translation: AAA69202.1.
U00096 Genomic DNA. Translation: AAC76070.1.
AP009048 Genomic DNA. Translation: BAE77090.1.
D16557 Genomic DNA. No translation available.

PIR

H65090.

RefSeq

AP_003584.1.
NP_417506.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1G0S	X-ray	1.90	A/B	1-209	[»]
1G9Q	X-ray	2.30	A/B	1-209	[»]
1GA7	X-ray	2.71	A/B	1-209	[»]
1KHZ	X-ray	2.04	A/B	1-209	[»]
1VIQ	X-ray	2.40	A/B/C	2-209	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

Q93K97. 5 interactions.

Genome annotation databases

GeneID

947519.

GenomeReviews

Gene locus JW3002 in contig AP009048_GR.
Gene locus b3034 in contig U00096_GR.

KEGG

ecj:JW3002.
eco:b3034.

Organism-specific databases

EcoGene

EG12184. nudF.

CMR

Search...

Phylogenomic databases

HOGENOM

Q93K97.

OMA

Q93K97. YFPSPGG.

Enzyme and pathway databases

BioCyc

EcoCyc:EG12633-MON.
MetaCyc:EG12633-MON.

Family and domain databases

InterPro

IPR004385. NDP_pyrophos.
IPR000086. NUDIX_hydrolase_core.
[Graphical view]

Gene3D

G3DSA:3.90.79.10. NUDIX_hydrolase. 1 hit.

Pfam

PF00293. NUDIX. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00052. NDP_pyrophos. 1 hit.

PROSITE

PS00893. NUDIX. 1 hit.
[Graphical view]

ProtoNet

Search...

Hide | Top

Entry information

Entry name

ADPP_ECOLI

Accession

Primary (citable) accession number: Q93K97
Secondary accession number(s): P36651, P82969, Q2M9G6

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 13, 2004
Last sequence update:	April 13, 2004
Last modified:	June 16, 2009
This is version 63 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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

Hide | Top

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents