PRU00886

Accession	PRU00886
Dates	4-JAN-2012 (Created) 19-NOV-2022 (Last updated, Version 6)

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

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.

ATP-binding
GMP biosynthesis
Nucleotide-binding
Purine biosynthesis

From: PS51553

Key

From

To

Description

Tag

Condition

FTGroup

DOMAIN

from

to

GMPS ATP-PPase #

BINDING

28

34

/ligand="ATP" /ligand_id="ChEBI:CHEBI:30616" /ligand_label="#

Size range	172-208 amino acids
Related rules	None
Repeats	1
Topology	Undefined
Example	Q8TYD7 (GUAAB_METKA)
Scope	Bacteria Archaea Eukaryota
Comments	None

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.

View rule in raw text format (no links)

• UniProtKB/Swiss-Prot sets
  

  Archaea	[37]
  Bacteria	[567]
  Eukaryota	[21]
  All	[ 625 ]

  
  
• Retrieve set of proteins with 3D structure for this domain