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.
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.
ProRule PRU00584
View rule in raw text format (no links)
PURL: https://purl.expasy.org/prosite/rule/PRU00584
General rule information
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| Accession | PRU00584 |
| Dates | 19-JAN-2007 (Created)
19-NOV-2022 (Last updated, Version 11) |
| Data class | Domain; |
| Predictors |
PROSITE; PS51255; ADPK |
Name | ADP-dependent kinase (ADPK) domain |
| Function | Archeal ADP-dependent glucokinases (ADPGKs) and phosphofructokinases (ADPPKKs) form an ADP-dependent kinase (ADPK) family, which was tentatively named the PFKC family. A ~460-residue ADPK domain is also found in a bifunctional ADP-dependent gluco/phosphofructo-kinase (ADP-GK/PFK) from Methanococcus jannaschii as well as in homologous hypothetical proteins present in several eukaryotes. |
| Scope(s) |
Eukaryota Archaea |
| Example(s) | Q9BRR6; |
Propagated annotation
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Identifier, protein and gene names
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| Protein name | + RecName: EC=2.7.1.-; |
Comments
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| case <FTGroup:1> | |
| COFACTOR | Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Note=Binds 1 Mg(2+) ion per subunit.; |
| end case | |
| PATHWAY | Carbohydrate degradation; glycolysis. |
Keywords
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| Glycolysis | |
| Kinase | |
| case <FTGroup:1> | |
| Magnesium | |
| Metal-binding | |
| end case | |
| Transferase | |
Gene Ontology
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| GO:0006096; Biological process:glycolytic process | |
| GO:0016301; Molecular function:kinase activity | |
| case <FTGroup:1> | |
| GO:0000287; Molecular function:magnesium ion binding | |
| end case | |
| GO:0016740; Molecular function:transferase activity | |
Features
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| From: PS51255 | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| DOMAIN | from | to | /note="ADPK #" | |||||||||
| ACT_SITE | 446 | 446 | /note="Proton acceptor" | D | ||||||||
| BINDING | 267 | 267 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" |
E | 1 | |||||||
| BINDING | 297 | 297 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" |
E | 1 | |||||||
| BINDING | 446 | 446 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" |
D | 1 | |||||||
Additional information
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| Size range | 440-485 amino acids |
| Related rules |
None |
| Fusion | None |
| Repeats | 1 |
| Topology | Undefined |
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
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- UniProtKB/Swiss-Prot sets
Archaea [14] Eukaryota [4] All [ 18 ]
- Retrieve set of proteins with 3D structure for this domain