AC   MF_00253;
DC   Protein; auto
c?   <OC:Bacteria>
TR   HAMAP; MF_00253_B; -; 1; level=0
c?   <OC:Archaea>
TR   HAMAP; MF_00253_A; -; 1; level=0
XX
Names: Gly_tRNA_synth
XX
ID   SYG
DE   RecName: Full=Glycine--tRNA ligase;
DE            EC=6.1.1.14;
DE   AltName: Full=Glycyl-tRNA synthetase;
DE            Short=GlyRS;
case <OC:Bacteria>
GN   Name=glyQS;
end case
case <OC:Archaea>
GN   Name=glyS;
end case
XX
CC   -!- FUNCTION: Catalyzes the attachment of glycine to tRNA(Gly).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + glycine + tRNA(Gly) = AMP + diphosphate + glycyl-
CC         tRNA(Gly); Xref=Rhea:RHEA:16013, Rhea:RHEA-COMP:9664, Rhea:RHEA-
CC         COMP:9683, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57305,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78522, ChEBI:CHEBI:456215;
CC         EC=6.1.1.14;
case <OC:Bacteria>
CC   -!- SUBUNIT: Homodimer.
end case
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
XX
DR   Pfam; PF00587; tRNA-synt_2b; 1; trigger=no
DR   PRINTS; PR01043; TRNASYNTHGLY; 1; trigger=no
DR   NCBIfam; TIGR00389; GlyS_dimeric; 1; trigger=no
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1; trigger=no
XX
KW   Cytoplasm
KW   Aminoacyl-tRNA synthetase
KW   Protein biosynthesis
KW   Ligase
KW   ATP-binding
KW   Nucleotide-binding
XX
GO   GO:0005524; F:ATP binding
GO   GO:0004820; F:glycine-tRNA ligase activity
GO   GO:0006426; P:glycyl-tRNA aminoacylation
GO   GO:0005737; C:cytoplasm
XX
FT   From: SYG_THET8 (P56206)
case <OC:Bacteria>
FT   BINDING         221..223
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: R-N-E
FT   BINDING         231..236
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: [FILV]-R-x(3)-[FL]
FT   BINDING         305..306
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: E-[CILV]
FT   BINDING         364..367
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: G-x(2)-R
FT   BINDING         236..240
FT                   /ligand="substrate"
FT   Condition: [FL]-x-Q-x-E
FT   BINDING         360..364
FT                   /ligand="substrate"
FT   Condition: E-x(3)-G
FT   BINDING         99
FT                   /ligand="substrate"
FT   Condition: [KR]
FT   BINDING         189
FT                   /ligand="substrate"
FT   Condition: E
end case
FT   From: SYG_METJA (Q57681)
case <OC:Archaea>
FT   BINDING         196..198
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: R-N-E
FT   BINDING         206..211
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: [FILV]-R-x(3)-F
FT   BINDING         328..329
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: E-[CILV]
FT   BINDING         451..454
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: G-x(2)-R
FT   BINDING         211..215
FT                   /ligand="substrate"
FT   Condition: F-x(3)-E
FT   BINDING         447..451
FT                   /ligand="substrate"
FT   Condition: E-x(3)-G
FT   BINDING         98
FT                   /ligand="substrate"
FT   Condition: R
FT   BINDING         164
FT                   /ligand="substrate"
FT   Condition: E
end case
XX
case <OC:Bacteria>
Size: 445-506;
end case
case <OC:Archaea>
Size: 565-583;
end case
Related: None;
Template: P56206;
Scope:
 Bacteria
 Archaea
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
XX
# Revision 1.31 2023/06/01
//