AC   MF_00036;
DC   Protein; auto
c?   <OC:Bacteria>
TR   HAMAP; MF_00036_B; -; 1; level=0
c?   <OC:Archaea>
TR   HAMAP; MF_00036_A; -; 1; level=0
XX
Names: Ala_tRNA_synth
XX
ID   SYA
DE   RecName: Full=Alanine--tRNA ligase;
DE            EC=6.1.1.7;
DE   AltName: Full=Alanyl-tRNA synthetase;
DE            Short=AlaRS;
GN   Name=alaS;
XX
CC   -!- FUNCTION: Catalyzes the attachment of alanine to tRNA(Ala) in a two-
CC       step reaction: alanine is first activated by ATP to form Ala-AMP and
CC       then transferred to the acceptor end of tRNA(Ala). Also edits
CC       incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing
CC       domain.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-
CC         tRNA(Ala); Xref=Rhea:RHEA:12540, Rhea:RHEA-COMP:9657, Rhea:RHEA-
CC         COMP:9923, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57972,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78497, ChEBI:CHEBI:456215; EC=6.1.1.7;
case <FTGroup:1> or <FTGroup:2>
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC       Note=Binds 1 zinc ion per subunit.;
end case
case <OC:Enterobacterales>
CC   -!- SUBUNIT: Homotetramer.
end case
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- DOMAIN: Consists of three domains; the N-terminal catalytic domain, the
CC       editing domain and the C-terminal C-Ala domain. The editing domain
CC       removes incorrectly charged amino acids, while the C-Ala domain, along
CC       with tRNA(Ala), serves as a bridge to cooperatively bring together the
CC       editing and aminoacylation centers thus stimulating deacylation of
CC       misacylated tRNAs.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
XX
DR   Pfam; PF01411; tRNA-synt_2c; 1; trigger=no
DR   PRINTS; PR00980; TRNASYNTHALA; 1; trigger=no
DR   NCBIfam; TIGR03683; A-tRNA_syn_arch; 0-1; trigger=no
DR   NCBIfam; TIGR00344; AlaS; 1; trigger=no
DR   PROSITE; PS50860; AA_TRNA_LIGASE_II_ALA; 1; trigger=no
XX
case <FT:1>
KW   Acetylation
end case
KW   Cytoplasm
KW   Aminoacyl-tRNA synthetase
KW   Protein biosynthesis
KW   Ligase
KW   ATP-binding
KW   Nucleotide-binding
KW   RNA-binding
KW   tRNA-binding
case <FTGroup:1> or <FTGroup:2>
KW   Metal-binding
KW   Zinc
end case
XX
GO   GO:0004813; F:alanine-tRNA ligase activity
GO   GO:0005524; F:ATP binding
GO   GO:0006419; P:alanyl-tRNA aminoacylation
case <FTGroup:1> or <FTGroup:2>
GO   GO:0008270; F:zinc ion binding
end case
GO   GO:0005737; C:cytoplasm
XX
FT   From: SYA_ECOLI (P00957)
case <OC:Escherichia> or <OC:Shigella>
FT   MOD_RES         74
FT                   /note="N6-acetyllysine"
FT   Condition: K
end case
case <OC:Bacteria>
FT   BINDING         564
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   Group: 1; Condition: H
FT   BINDING         568
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   Group: 1; Condition: H
FT   BINDING         666
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   Group: 1; Condition: C
FT   BINDING         670
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   Group: 1; Condition: H
end case
FT   From: SYA_ARCFU (O28029)
case <OC:Archaea>
FT   BINDING         600
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   Group: 2; Condition: H
FT   BINDING         604
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   Group: 2; Condition: H
FT   BINDING         703
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   Group: 2; Condition: C
FT   BINDING         707
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   Group: 2; Condition: H
end case
XX
case <OC:Bacteria>
Size: 842-977;
end case
case <OC:Archaea>
Size: 870-932;
end case
Related: MF_03134!;
Template: P00957;
Scope:
 Bacteria
 Archaea
Fusion:
 Nter: None
 Cter: None
Duplicate: in LACP7
Plasmid: None
Comments: Zinc-binding shown for Archaea (ARCFU and PYRHO crystals), the
 residues are (mostly) conserved in bacteria and ECOLI is known to bind
 zinc. KORVE has an insert in the catalytic domain, BORAP, BORBU, BORGP,
 BORHD, TREDE, TREPA and the second copy of LACP7 are missing part of the
 catalytic domain and all of the C-Ala domain and are marked as atypical.
 In YERPA the C-Ala domain is replaced by an unrelated sequence and is also
 considered atypical. LACP3, LACPL, LEUCK, LEUMM, OENOB are missing one of
 the conserved zinc-binding residues and are atypical.
XX
# Revision 1.51 2023/06/01
//