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| Annotation rule MF_00344 |
General rule information
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| Accession | MF_00344 |
| Dates | 1-JUN-2001 (Created) 18-NOV-2019 (Last updated, Version 41) |
| Name | GMP_synthase |
| Scope | Bacteria
Archaea |
| Templates | P04079 (GUAA_ECOLI); P9WMS7 (GUAA_MYCTU): [Recover all] |
| Triggered by |
Propagated annotation
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Identifier, protein and gene names
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| Identifier |
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| Protein name |
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| Gene name |
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Comments
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| Function | Catalyzes the synthesis of GMP from XMP. |
| Catalytic activity | RHEA:11680: ATP + H2O + L-glutamine + XMP = AMP + diphosphate + GMP + 2 H(+) + L-glutamate
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
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.
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; |
| PF00958; GMP_synt_C; 1; | |
| PRINTS | PR00096; GATASE; 1; |
| TIGRFAMs | TIGR00884; GuaA_Cterm; 1; |
| TIGR00888; GuaA_Nterm; 1; | |
| PROSITE | PS51273; GATASE_TYPE_1; 1; trigger=PRU00605; |
| PS51553; GMPS_ATP_PPASE; 1; trigger=PRU00886; |
Features
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| From: GUAA_ECOLI (P04079) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| ACT_SITE | 86 | 86 | 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 (GUAAB); MF_01510 (GUAAA) |
| Fusion | None |
| Comments | Active site is not conserved in BACHD; 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. |