HAMAP rule MF_00344
General rule information
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Accession | MF_00344 |
Dates | 1-JUN-2001 (Created)
1-JUN-2023 (Last updated, Version 44) |
Name | GMP_synthase |
Scope(s) |
Bacteria Archaea |
Template(s) | P04079 (GUAA_ECOLI); P9WMS7 (GUAA_MYCTU); [ Recover all ] |
Triggered by |
HAMAP; MF_00344 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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Identifier | GUAA |
Protein name | RecName: Full=GMP synthase [glutamine-hydrolyzing]; EC=6.3.5.2; AltName: Full=GMP synthetase; AltName: Full=Glutamine amidotransferase; |
Gene name | Name=guaA; |
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. |
case <OC:Bacteria> | |
SUBUNIT | Homodimer. |
end case |
Keywords
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ATP-binding |
Glutamine amidotransferase |
GMP biosynthesis |
Ligase |
Nucleotide-binding |
Purine biosynthesis |
Gene Ontology
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GO:0005524; Molecular function:ATP binding |
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; |
Pfam | PF00958; GMP_synt_C; 1; |
PRINTS | PR00096; GATASE; 1; |
NCBIfam | TIGR00884; GuaA_Cterm; 1; |
NCBIfam | TIGR00888; GuaA_Nterm; 1; |
PROSITE | PS51273; GATASE_TYPE_1; 1; |
PROSITE | PS51553; GMPS_ATP_PPASE; 1; |
Features
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From: GUAA_ECOLI (P04079) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
ACT_SITE | 86 | 86 | /note="Nucleophile" | C | ||||||||
ACT_SITE | 181 | 181 | H | |||||||||
ACT_SITE | 183 | 183 | E |
Additional information
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Size range | 501-551 amino acids |
Related rules |
MF_00345 MF_01510 |
Fusion | Nter: None Cter: None |
Comments | Active site is not conserved in HALH5; CHLPN and the second copy in BACTN have an internal deletion; weird inserts in HELHP, LEPIC and LEPIN; longer N-terminus in RHOBA; all these sequences are not included in alignment and not taken into account in size range. 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. |