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P83843 (ADPP_ECO57) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
ADP-ribose pyrophosphatase
EC=3.6.1.13
Alternative name(s):
ADP-ribose diphosphatase
ADP-ribose phosphohydrolase
Short name=ASPPase
Adenosine diphosphoribose pyrophosphatase
Short name=ADPR-PPase
Gene names
Name:nudF
Synonyms:aspP
Ordered Locus Names:Z4391, ECs3922
OrganismEscherichia coli O157:H7 [Complete proteome] [HAMAP]
Taxonomic identifier83334 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length209 AA.
Sequence statusComplete.
Protein existenceInferred 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.

Contains 1 nudix hydrolase domain.

Ontologies

Keywords
   LigandMagnesium
Metal-binding
   Molecular functionHydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Molecular functionADP-ribose diphosphatase activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 209209ADP-ribose pyrophosphatase
PRO_0000057044

Regions

Domain55 – 193139Nudix hydrolase
Region28 – 292Substrate binding By similarity
Region51 – 522Substrate binding; shared with dimeric partner By similarity
Region133 – 1353Substrate binding; shared with dimeric partner By similarity
Motif97 – 11822Nudix box

Sites

Active site1621Proton acceptor By similarity
Metal binding961Magnesium 1; via carbonyl oxygen By similarity
Metal binding1121Magnesium 2 By similarity
Metal binding1121Magnesium 3 By similarity
Metal binding1161Magnesium 1 By similarity
Metal binding1161Magnesium 3 By similarity
Metal binding1641Magnesium 3 By similarity
Binding site561Substrate By similarity
Binding site791Substrate By similarity
Binding site981Substrate; via amide nitrogen By similarity
Binding site1391Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
P83843 [UniParc].

Last modified April 13, 2004. Version 1.
Checksum: 2CF77EA9D63B9615

FASTA20923,667
        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

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE005174 Genomic DNA. Translation: AAG58173.1.
BA000007 Genomic DNA. Translation: BAB37345.1.
PIRA85964.
B91119.
RefSeqNP_289614.1. NC_002655.2.
NP_311949.1. NC_002695.1.

3D structure databases

ProteinModelPortalP83843.
SMRP83843. Positions 8-209.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000028358; EBESCP00000027251; EBESCG00000027409.
EBESCT00000058562; EBESCP00000056390; EBESCG00000057610.
GeneID916244.
961965.
GenomeReviewsGene locus Z4391 in contig AE005174_GR.
Gene locus ECs3922 in contig BA000007_GR.
KEGGece:Z4391.
ecs:ECs3922.
PATRIC18357335. VBIEscCol44059_3845.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000011193.
HOGENOMHBG692398.
OMALQWLELN.
ProtClustDBPRK10729.

Enzyme and pathway databases

BioCycECOL83334:ECS3922-MONOMER.

Family and domain databases

InterProIPR004385. NDP_pyrophosphatase.
IPR020084. NUDIX_hydrolase_CS.
IPR000086. NUDIX_hydrolase_dom.
IPR015797. NUDIX_hydrolase_dom-like.
[Graphical view]
Gene3DG3DSA:3.90.79.10. NUDIX_hydrolase. 1 hit.
KOK01515.
PfamPF00293. NUDIX. 1 hit.
[Graphical view]
SUPFAMSSF55811. NUDIX_hydrolase. 1 hit.
TIGRFAMsTIGR00052. TIGR00052. 1 hit.
PROSITEPS51462. NUDIX. 1 hit.
PS00893. NUDIX_BOX. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameADPP_ECO57
AccessionPrimary (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: January 25, 2012
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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