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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 PRU00886


View rule in raw text format (no links)
PURL: https://purl.expasy.org/prosite/rule/PRU00886
General rule information [?]

Accession PRU00886
Dates 04-JAN-2012 (Created)
19-NOV-2022 (Last updated, Version 7)
Data class Domain;
Predictors PROSITE; PS51553; GMPS_ATP_PPASE
Name GMP synthetase ATP pyrophosphatase (GMPS ATP-PPase) domain
Function The GMP synthetase ATP-PPase ATP-binding domain is a twisted, five- stranded parallel beta-sheet sandwiched between helical layers. It contains a glycine rich ATP-binding motif called the "P-loop motif" located after the first beta-strand
Scope(s) Bacteria
Archaea
Eukaryota
Example(s) Q8TYD7;

Propagated annotation [?]

Keywords [?]

ATP-binding
GMP biosynthesis
Nucleotide-binding
Purine biosynthesis

Gene Ontology [?]

GO:0005524; Molecular function:ATP binding
GO:0006177; Biological process:GMP biosynthetic process
GO:0000166; Molecular function:nucleotide binding
GO:0006164; Biological process:purine nucleotide biosynthetic process

Features [?]

From: PS51553
Key From To Description Tag Condition FTGroup
DOMAIN from to /note="GMPS ATP-PPase #"
BINDING 28 34 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"
/ligand_label="#"

Additional information [?]

Size range 172-208 amino acids
Related rules None
Fusion None
Repeats 1
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 [?]