Reviewed, UniProtKB/Swiss-Prot P83843 (ADPP_ECO57)

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
Ordered Locus Names:	Z4391, ECs3922

Organism

Escherichia coli O157:H7 [Complete proteome] [HAMAP]

Taxonomic identifier

83334 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	209 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

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 By similarity.
Catalytic activity	ADP-ribose + H2O = AMP + D-ribose 5-phosphate.
Cofactor	Binds 3 magnesium ions per subunit By similarity.
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 By similarity.
Subunit structure	Homodimer By similarity.
Sequence similarities	Belongs to the Nudix hydrolase family. NudF subfamily.

Ontologies

Keywords
Ligand	Magnesium Metal-binding Zinc
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Molecular function	ADP-ribose diphosphatase activity Inferred from electronic annotation. Source: EC magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 209	209	ADP-ribose pyrophosphatase		PRO_0000057044
Regions
	Motif	97 – 118	22	Nudix box
Sites
	Active site	162	1	Proton acceptor By similarity
	Metal binding	112	1	Magnesium 1 By similarity
	Metal binding	112	1	Magnesium 2 By similarity
	Metal binding	116	1	Magnesium 1 By similarity
	Metal binding	116	1	Magnesium 3 By similarity
	Metal binding	164	1	Magnesium 1 By similarity

Sequences

	Sequence		Length	Mass (Da)
	P83843-1 [UniParc]. Last modified April 13, 2004. Version 1. Checksum: 2CF77EA9D63B9615	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

References

[1]

"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7." Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R. Nature 409:529-533(2001) [PubMed: 11206551] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.

[2]

"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12." Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. , Kuhara S., Shiba T., Hattori M., Shinagawa H. DNA Res. 8:11-22(2001) [PubMed: 11258796] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE005174 Genomic DNA. Translation: AAG58173.1. BA000007 Genomic DNA. Translation: BAB37345.1.
PIR	A85964. B91119.
RefSeq	NP_289614.1. NP_311949.1.
3D structure databases
SMR	P83843. Positions 8-209.
ModBase	Search...
Genome annotation databases
GeneID	916244. 961965.
GenomeReviews	Gene locus Z4391 in contig AE005174_GR. Gene locus ECs3922 in contig BA000007_GR.
KEGG	ece:Z4391. ecs:ECs3922.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P83843.
OMA	P83843. YFPSPGG.
Enzyme and pathway databases
BioCyc	ECOL83334:ECS3922-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...

Entry information

Entry name

ADPP_ECO57

Accession

Primary (citable) accession number: P83843
Secondary accession number(s): P36651

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 13, 2004
Last sequence update:	April 13, 2004
Last modified:	June 16, 2009
This is version 34 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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