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UniProtKB - Q93K97 (ADPP_ECOLI)
Protein
ADP-ribose pyrophosphatase
Gene
nudF
Organism
Escherichia coli (strain K12)
Status
Functioni
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.
1 PublicationCatalytic activityi
- EC:3.6.1.131 Publication
Cofactori
Mg2+2 PublicationsNote: Binds 3 Mg2+ ions per subunit.2 Publications
Activity regulationi
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.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 56 | Substrate | 1 | |
Binding sitei | 79 | Substrate | 1 | |
Metal bindingi | 96 | Magnesium 1; via carbonyl oxygen | 1 | |
Binding sitei | 98 | Substrate; via amide nitrogen | 1 | |
Metal bindingi | 112 | Magnesium 2 | 1 | |
Metal bindingi | 112 | Magnesium 3 | 1 | |
Metal bindingi | 116 | Magnesium 1 | 1 | |
Metal bindingi | 116 | Magnesium 3 | 1 | |
Binding sitei | 139 | Substrate | 1 | |
Active sitei | 162 | Proton acceptorCurated | 1 | |
Metal bindingi | 164 | Magnesium 3 | 1 |
GO - Molecular functioni
- ADP-ribose diphosphatase activity Source: EcoCyc
- ADP-sugar diphosphatase activity Source: EcoCyc
- magnesium ion binding Source: EcoCyc
- pyrophosphatase activity Source: EcoCyc
GO - Biological processi
- nucleoside phosphate metabolic process Source: GO_Central
- response to heat Source: EcoCyc
- ribose phosphate metabolic process Source: GO_Central
Keywordsi
Molecular function | Hydrolase |
Ligand | Magnesium, Manganese, Metal-binding |
Enzyme and pathway databases
BioCyci | EcoCyc:EG12633-MONOMER |
BRENDAi | 3.6.1.13, 2026 |
Names & Taxonomyi
Protein namesi | Recommended 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 namesi | Name:nudF Synonyms:aspP, yqiE, yzzG Ordered Locus Names:b3034, JW3002 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000057042 | 1 – 209 | ADP-ribose pyrophosphataseAdd BLAST | 209 |
Proteomic databases
jPOSTi | Q93K97 |
PaxDbi | Q93K97 |
PRIDEi | Q93K97 |
Interactioni
Subunit structurei
Homodimer.
2 PublicationsBinary interactionsi
Q93K97
With | #Exp. | IntAct |
---|---|---|
sgbH [P37678] | 2 | EBI-562814,EBI-555448 |
Protein-protein interaction databases
BioGRIDi | 4263247, 23 interactors |
DIPi | DIP-36214N |
IntActi | Q93K97, 5 interactors |
STRINGi | 511145.b3034 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
AlphaFoldDBi | Q93K97 |
SMRi | Q93K97 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | Q93K97 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 55 – 193 | Nudix hydrolasePROSITE-ProRule annotationAdd BLAST | 139 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 28 – 29 | Substrate binding | 2 | |
Regioni | 51 – 52 | Substrate binding; shared with dimeric partner | 2 | |
Regioni | 133 – 135 | Substrate binding; shared with dimeric partner | 3 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 97 – 118 | Nudix boxAdd BLAST | 22 |
Sequence similaritiesi
Phylogenomic databases
eggNOGi | COG0494, Bacteria |
HOGENOMi | CLU_062658_6_1_6 |
InParanoidi | Q93K97 |
OMAi | TIIALQW |
PhylomeDBi | Q93K97 |
Family and domain databases
InterProi | View protein in InterPro IPR004385, NDP_pyrophosphatase IPR015797, NUDIX_hydrolase-like_dom_sf IPR020084, NUDIX_hydrolase_CS IPR000086, NUDIX_hydrolase_dom |
Pfami | View protein in Pfam PF00293, NUDIX, 1 hit |
SUPFAMi | SSF55811, SSF55811, 1 hit |
TIGRFAMsi | TIGR00052, TIGR00052, 1 hit |
PROSITEi | View protein in PROSITE PS51462, NUDIX, 1 hit PS00893, NUDIX_BOX, 1 hit |
i Sequence
Sequence statusi: Complete.
Q93K97-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MLKPDNLPVT FGKNDVEIIA RETLYRGFFS LDLYRFRHRL FNGQMSHEVR
60 70 80 90 100
REIFERGHAA VLLPFDPVRD EVVLIEQIRI AAYDTSETPW LLEMVAGMIE
110 120 130 140 150
EGESVEDVAR REAIEEAGLI VKRTKPVLSF LASPGGTSER SSIMVGEVDA
160 170 180 190 200
TTASGIHGLA DENEDIRVHV VSREQAYQWV EEGKIDNAAS VIALQWLQLH
HQALKNEWA
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 2 | L → V in CAC44036 (PubMed:11416161).Curated | 1 | |
Sequence conflicti | 6 | N → S in CAC44036 (PubMed:11416161).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | 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. |
PIRi | H65090 |
RefSeqi | NP_417506.1, NC_000913.3 WP_000917117.1, NZ_STEB01000001.1 |
Genome annotation databases
EnsemblBacteriai | AAC76070; AAC76070; b3034 BAE77090; BAE77090; BAE77090 |
GeneIDi | 66673067 947519 |
KEGGi | ecj:JW3002 eco:b3034 |
PATRICi | fig|1411691.4.peg.3697 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | 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. |
PIRi | H65090 |
RefSeqi | NP_417506.1, NC_000913.3 WP_000917117.1, NZ_STEB01000001.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB 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 | [»] | |
AlphaFoldDBi | Q93K97 | |||||
SMRi | Q93K97 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4263247, 23 interactors |
DIPi | DIP-36214N |
IntActi | Q93K97, 5 interactors |
STRINGi | 511145.b3034 |
Proteomic databases
jPOSTi | Q93K97 |
PaxDbi | Q93K97 |
PRIDEi | Q93K97 |
Genome annotation databases
EnsemblBacteriai | AAC76070; AAC76070; b3034 BAE77090; BAE77090; BAE77090 |
GeneIDi | 66673067 947519 |
KEGGi | ecj:JW3002 eco:b3034 |
PATRICi | fig|1411691.4.peg.3697 |
Phylogenomic databases
eggNOGi | COG0494, Bacteria |
HOGENOMi | CLU_062658_6_1_6 |
InParanoidi | Q93K97 |
OMAi | TIIALQW |
PhylomeDBi | Q93K97 |
Enzyme and pathway databases
BioCyci | EcoCyc:EG12633-MONOMER |
BRENDAi | 3.6.1.13, 2026 |
Miscellaneous databases
EvolutionaryTracei | Q93K97 |
PROi | PR:Q93K97 |
Family and domain databases
InterProi | View protein in InterPro IPR004385, NDP_pyrophosphatase IPR015797, NUDIX_hydrolase-like_dom_sf IPR020084, NUDIX_hydrolase_CS IPR000086, NUDIX_hydrolase_dom |
Pfami | View protein in Pfam PF00293, NUDIX, 1 hit |
SUPFAMi | SSF55811, SSF55811, 1 hit |
TIGRFAMsi | TIGR00052, TIGR00052, 1 hit |
PROSITEi | View protein in PROSITE PS51462, NUDIX, 1 hit PS00893, NUDIX_BOX, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | ADPP_ECOLI | |
Accessioni | Q93K97Primary (citable) accession number: Q93K97 Secondary accession number(s): P36651, P82969, Q2M9G6 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | April 13, 2004 |
Last sequence update: | April 13, 2004 | |
Last modified: | May 25, 2022 | |
This is version 154 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families