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We are deeply saddened by the passing of Amos Bairoch (1957–2025), the creator of PROSITE. We wish to dedicate our latest paper, published shortly before his death, to him. He will always be a source of inspiration to us.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
Amos Bairoch

ProRule PRU00706


View rule in raw text format (no links)
PURL: https://purl.expasy.org/prosite/rule/PRU00706
General rule information [?]

Accession PRU00706
Dates 20-DEC-2023 (Created)
20-DEC-2023 (Last updated, Version 2)
Data class Domain;
Predictors PROSITE; PS51374; NDPK_LIKE
Name Nucleoside diphosphate kinase (NDK)-like domain
Function All Nme enzymes possess at least one nucleoside diphosphate kinase (NDK)-like domain of ~150 amino acids.
Scope(s) Bacteria
Eukaryota
Archaea
Viruses
Mimivirus bradfordmassiliense
Example(s) C3LT09;

Propagated annotation [?]

Identifier, protein and gene names [?]

case <FTGroup:1> and <FTTag:act_site>
Protein name + AltName: Full=Nucleoside diphosphate kinase;
                 Short=NDK;
                 Short=NDP kinase {ECO:0000255|HAMAP-Rule:MF_00451};
                 EC=2.7.4.6;
end case

Comments [?]

case <FTGroup:1> and <FTTag:act_site>
CATALYTIC ACTIVITYReaction=a 2'-deoxyribonucleoside 5'- diphosphate + ATP = a 2'-deoxyribonucleoside 5'-triphosphate + ADP; Xref=Rhea:RHEA:44640, ChEBI:CHEBI:30616, ChEBI:CHEBI:61560, ChEBI:CHEBI:73316, ChEBI:CHEBI:456216; EC=2.7.4.6;
CATALYTIC ACTIVITYReaction=a ribonucleoside 5'-diphosphate + ATP = a ribonucleoside 5'-triphosphate + ADP; Xref=Rhea:RHEA:18113, ChEBI:CHEBI:30616, ChEBI:CHEBI:57930, ChEBI:CHEBI:61557, ChEBI:CHEBI:456216; EC=2.7.4.6;
COFACTORName=Mg(2+); Xref=ChEBI:CHEBI:18420;
end case
SIMILARITYBelongs to the NDK family.

Keywords [?]


Gene Ontology [?]

GO:0004550; Molecular function:nucleoside diphosphate kinase activity
GO:0006241; Biological process:CTP biosynthetic process
GO:0005524; Molecular function:ATP binding
GO:0006228; Biological process:UTP biosynthetic process
GO:0006183; Biological process:GTP biosynthetic process
GO:0016310; Biological process:phosphorylation
GO:0046872; Molecular function:metal ion binding

Cross-references [?]

PROSITE PS00469; NDPK; 1;

Features [?]

From: PS51374
Key From To Description Tag Condition FTGroup
DOMAIN from to /note="NDPK-like #"
case <FTGroup:1>
ACT_SITE 114 114 /note="Pros-phosphohistidine intermediate" act_site H
end case
BINDING 8 8 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"
K 1
BINDING 56 56 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"
F 1
BINDING 84 84 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"
R 1
BINDING 90 90 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"
T 1
BINDING 101 101 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"
R 1
BINDING 111 111 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"
N 1

Additional information [?]

Size range 21-180 amino acids
Related rules None
Fusion None
Repeats 1-3
Topology Undefined

Copyright

PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.

UniProtKB rule member sequences [?]