AC   MF_00344;
DC   Protein; auto
TR   HAMAP; MF_00344; -; 1; level=0
XX
Names: GMP_synthase
XX
ID   GUAA
DE   RecName: Full=GMP synthase [glutamine-hydrolyzing];
DE            EC=6.3.5.2;
DE   AltName: Full=GMP synthetase;
DE   AltName: Full=Glutamine amidotransferase;
GN   Name=guaA;
XX
CC   -!- FUNCTION: Catalyzes the synthesis of GMP from XMP.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + L-glutamine + XMP = AMP + diphosphate + GMP + 2
CC         H(+) + L-glutamate; Xref=Rhea:RHEA:11680, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57464, ChEBI:CHEBI:58115,
CC         ChEBI:CHEBI:58359, ChEBI:CHEBI:456215; EC=6.3.5.2;
CC   -!- PATHWAY: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln
CC       route): step 1/1.
case <OC:Bacteria>
CC   -!- SUBUNIT: Homodimer.
end case
XX
DR   Pfam; PF00117; GATase; 1; trigger=no
DR   Pfam; PF00958; GMP_synt_C; 1; trigger=no
DR   PRINTS; PR00096; GATASE; 1; trigger=no
DR   NCBIfam; TIGR00884; GuaA_Cterm; 1; trigger=no
DR   NCBIfam; TIGR00888; GuaA_Nterm; 1; trigger=no
DR   PROSITE; PS51273; GATASE_TYPE_1; 1; trigger=yes
DR   PROSITE; PS51553; GMPS_ATP_PPASE; 1; trigger=yes
XX
KW   ATP-binding
KW   Glutamine amidotransferase
KW   GMP biosynthesis
KW   Ligase
KW   Nucleotide-binding
KW   Purine biosynthesis
XX
GO   GO:0005524; F:ATP binding
GO   GO:0003922; F:GMP synthase (glutamine-hydrolyzing) activity
GO   GO:0006177; P:GMP biosynthetic process
XX
FT   From: GUAA_ECOLI (P04079)
FT   ACT_SITE        86
FT                   /note="Nucleophile"
FT   Condition: C
FT   ACT_SITE        181
FT   Condition: H
FT   ACT_SITE        183
FT   Condition: E
XX
Size: 501-551;
Related: MF_00345; MF_01510;
Template: P04079; P9WMS7;
Scope:
 Bacteria
 Archaea
Fusion:
 Nter: None
 Cter: None
Duplicate: in BACTN
Plasmid: in BORBU
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.
XX
# Revision 1.44 2023/06/01
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