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Annotation rule MF_00344
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General rule information [?]

Accession MF_00344
Dates 1-JUN-2001 (Created)
27-OCT-2018 (Last updated, Version 40)
Name GMP_synthase
Templates P04079 (GUAA_ECOLI); P9WMS7 (GUAA_MYCTU): [Recover all]

Propagated annotation [?]

Identifier, protein and gene names [?]

Protein name
RecName: Full=GMP synthase [glutamine-hydrolyzing];
AltName: Full=GMP synthetase;
AltName: Full=Glutamine amidotransferase;
Gene name

Comments [?]

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=;.
Pathway Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln route): step 1/1.
case <OC:Bacteria>
Subunit Homodimer.
end case

Keywords [?]

Gene Ontology [?]

GO:0005524; Molecular function: ATP binding.
GO:0003922; Molecular function: GMP synthase (glutamine-hydrolyzing) activity.
GO:0006177; Biological process: GMP biosynthetic process.

Cross-references [?]

Pfam PF00117; GATase; 1;
PF00958; GMP_synt_C; 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 [?]

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 [?]

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.