AC MF_02213; DC Protein; auto TR HAMAP; MF_02213; -; 1; level=0 XX Names: Lipid_II_synth_GatD XX ID GATD DE RecName: Full=Lipid II isoglutaminyl synthase (glutamine-hydrolyzing) subunit GatD; DE EC=6.3.5.13; DE AltName: Full=Lipid II isoglutaminyl synthase glutaminase subunit; DE EC=3.5.1.2; GN Name=gatD; XX CC -!- FUNCTION: The lipid II isoglutaminyl synthase complex catalyzes the CC formation of alpha-D-isoglutamine in the cell wall lipid II stem CC peptide. The GatD subunit catalyzes the hydrolysis of glutamine to CC glutamate and ammonia. The resulting ammonia molecule is channeled to CC the active site of MurT. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys- CC D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate + H2O + L- CC glutamine = ADP + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-D- CC isoglutaminyl-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl CC diphosphate + H(+) + L-glutamate + phosphate; Xref=Rhea:RHEA:57928, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58359, CC ChEBI:CHEBI:60033, ChEBI:CHEBI:62233, ChEBI:CHEBI:456216; CC EC=6.3.5.13; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + L-glutamine = L-glutamate + NH4(+); CC Xref=Rhea:RHEA:15889, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, CC ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; EC=3.5.1.2; CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC -!- SUBUNIT: Forms a heterodimer with MurT. CC -!- SIMILARITY: Belongs to the CobB/CobQ family. GatD subfamily. XX DR PROSITE; PS51274; GATASE_COBBQ; 1; trigger=yes DR Pfam; PF07685; GATase_3; 1; trigger=no XX KW Cell shape KW Cell wall biogenesis/degradation KW Glutamine amidotransferase KW Hydrolase KW Ligase KW Peptidoglycan synthesis XX GO GO:0140282; F:carbon-nitrogen ligase activity on lipid II GO GO:0004359; F:glutaminase activity GO GO:0009252; P:peptidoglycan biosynthetic process XX FT From: GATD_STAAC (A0A0H2WZ38) FT ACT_SITE 94 FT /note="Nucleophile" FT Condition: C FT ACT_SITE 189 FT Condition: H FT BINDING 128 FT /ligand="substrate" FT Condition: R XX Size: 210-390; Related: None; Template: A0A0H2WZ38; A0A0H3JN63; Q8DNZ8; Scope: Bacteria Archaea Fusion: Nter: None Cter: None Duplicate: None Plasmid: None Comments: None XX # Revision 1.5 2022/05/14 //