HAMAP rule MF_01510
General rule information
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| Accession | MF_01510 |
| Dates | 11-FEB-2004 (Created)
1-JUN-2023 (Last updated, Version 24) |
| Name | GMP_synthase_A |
| Scope(s) |
Archaea |
| Template(s) | P04079 (GUAA_ECOLI); [ Recover all ] |
| Triggered by |
HAMAP; MF_01510 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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| Identifier | GUAAA |
| Protein name | RecName: Full=GMP synthase [glutamine-hydrolyzing] subunit A; EC=6.3.5.2; AltName: Full=Glutamine amidotransferase; |
| Gene name | Name=guaAA; |
Comments
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| FUNCTION | Catalyzes the synthesis of GMP from XMP. |
| CATALYTIC ACTIVITY | Reaction=ATP + H2O + L-glutamine + XMP = AMP + diphosphate + GMP + 2 H(+) + L-glutamate; Xref=Rhea:RHEA:11680, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57464, ChEBI:CHEBI:58115, ChEBI:CHEBI:58359, ChEBI:CHEBI:456215; EC=6.3.5.2; |
| PATHWAY | Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln route): step 1/1. |
| SUBUNIT | Heterodimer composed of a glutamine amidotransferase subunit (A) and a GMP-binding subunit (B). |
Keywords
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| ATP-binding |
| GMP biosynthesis |
| Glutamine amidotransferase |
| Ligase |
| Nucleotide-binding |
| Purine biosynthesis |
Gene Ontology
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| GO:0003922; Molecular function:GMP synthase (glutamine-hydrolyzing) activity |
| GO:0006177; Biological process:GMP biosynthetic process |
Cross-references
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| Pfam | PF00117; GATase; 1; |
| PRINTS | PR00096; GATASE; 1; |
| NCBIfam | TIGR00888; GuaA_Nterm; 1; |
| PROSITE | PS51273; GATASE_TYPE_1; 1; |
Features
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| From: GUAAA_METJA (Q58970) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| ACT_SITE | 76 | 76 | /note="Nucleophile" | C | ||||||||
| ACT_SITE | 163 | 163 | H | |||||||||
| ACT_SITE | 165 | 165 | E | |||||||||
Additional information
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| Size range | 181-202 amino acids |
| Related rules |
MF_00344 |
| Fusion | Nter: None Cter: None |
| Comments | Sequences from AERPE and PYRAE are like that of Eubacteria composed of two domains, while other archaea have separate proteins that correspond to each domain |