AC   MF_03134;
DC   Protein; auto
c?   <OC:Eukaryota>
TR   HAMAP; MF_03134; -; 1; level=0
XX
Names: Ala_tRNA_synth_plantC
XX
ID   SYAP
DE   RecName: Full=Probable alanine--tRNA ligase, chloroplastic;
DE            EC=6.1.1.7;
DE   AltName: Full=Alanyl-tRNA synthetase;
DE            Short=AlaRS;
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 tRNA(Ala) via its editing 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;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC       Note=Binds 1 zinc ion per subunit.;
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast. Mitochondrion.
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; PF02272; DHHA1; 1; trigger=no
DR   Pfam; PF01411; tRNA-synt_2c; 1; trigger=no
DR   Pfam; PF07973; tRNA_SAD; 1; trigger=no
DR   PRINTS; PR00980; TRNASYNTHALA; 1; trigger=no
DR   NCBIfam; TIGR00344; AlaS; 1; trigger=no
DR   PROSITE; PS50860; AA_TRNA_LIGASE_II_ALA; 1; trigger=no
DR   General; TransitC; -; 0-1; trigger=yes
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KW   Aminoacyl-tRNA synthetase
KW   ATP-binding
KW   Ligase
KW   Nucleotide-binding
KW   Protein biosynthesis
KW   RNA-binding
KW   tRNA-binding
KW   Plastid
KW   Chloroplast
KW   Mitochondrion
case <FTGroup:1>
KW   Metal-binding
KW   Zinc
end case
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GO   GO:0004813; F:alanine-tRNA ligase activity
GO   GO:0005524; F:ATP binding
GO   GO:0008270; F:zinc ion binding
GO   GO:0006419; P:alanyl-tRNA aminoacylation
GO   GO:0009507; C:chloroplast
GO   GO:0005739; C:mitochondrion
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FT   From: SYAP_ARATH (Q9FFC7)
FT   BINDING         655
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   Group: 1; Condition: H
FT   BINDING         659
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   Group: 1; Condition: H
FT   BINDING         758
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   Group: 1; Condition: C
FT   BINDING         762
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   Group: 1; Condition: H
XX
Size: 815-996;
Related: MF_03133;
Template: Q9FFC7;
Scope:
 Eukaryota; Viridiplantae
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
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# Revision 1.9 2023/06/01
//