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HAMAP rule MF_00036

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General rule information [?]

Accession MF_00036
Dates 1-JUN-2001 (Created)
1-JUN-2023 (Last updated, Version 51)
Name Ala_tRNA_synth
Scope(s) Bacteria
Template(s) P00957 (SYA_ECOLI); [ Recover all ]
Triggered by
case c? <OC:Bacteria>
HAMAP; MF_00036_B (Get profile general information and statistics)
end case
case c? <OC:Archaea>
HAMAP; MF_00036_A (Get profile general information and statistics)
end case

Propagated annotation [?]

Identifier, protein and gene names [?]

Identifier SYA
Protein name RecName: Full=Alanine--tRNA ligase;
AltName: Full=Alanyl-tRNA synthetase;
Gene name Name=alaS;

Comments [?]

FUNCTIONCatalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.
CATALYTIC ACTIVITY Reaction=ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl- tRNA(Ala); Xref=Rhea:RHEA:12540, Rhea:RHEA-COMP:9657, Rhea:RHEA- COMP:9923, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57972, ChEBI:CHEBI:78442, ChEBI:CHEBI:78497, ChEBI:CHEBI:456215; EC=;
case <FTGroup:1> or <FTGroup:2>
COFACTOR Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 1 zinc ion per subunit.;
end case
case <OC:Enterobacterales>
end case
DOMAINConsists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs.
SIMILARITYBelongs to the class-II aminoacyl-tRNA synthetase family.

Keywords [?]

Gene Ontology [?]

GO:0004813; Molecular function:alanine-tRNA ligase activity
GO:0005524; Molecular function:ATP binding
GO:0006419; Biological process:alanyl-tRNA aminoacylation
case <FTGroup:1> or <FTGroup:2>
GO:0008270; Molecular function:zinc ion binding
end case
GO:0005737; Cellular component:cytoplasm

Cross-references [?]

Pfam PF01411; tRNA-synt_2c; 1;
NCBIfam TIGR03683; A-tRNA_syn_arch; 0-1;
NCBIfam TIGR00344; AlaS; 1;

Features [?]

From: SYA_ECOLI (P00957)
Key From To Description Tag Condition FTGroup
case <OC:Escherichia> or <OC:Shigella>
MOD_RES 74 74 /note="N6-acetyllysine" K
end case
case <OC:Bacteria>
BINDING 564 564 /ligand="Zn(2+)"
H 1
BINDING 568 568 /ligand="Zn(2+)"
H 1
BINDING 666 666 /ligand="Zn(2+)"
C 1
BINDING 670 670 /ligand="Zn(2+)"
H 1
end case
From: SYA_ARCFU (O28029)
Key From To Description Tag Condition FTGroup
case <OC:Archaea>
BINDING 600 600 /ligand="Zn(2+)"
H 2
BINDING 604 604 /ligand="Zn(2+)"
H 2
BINDING 703 703 /ligand="Zn(2+)"
C 2
BINDING 707 707 /ligand="Zn(2+)"
H 2
end case

Additional information [?]

Size range 870-932 amino acids
Related rules MF_03134
Fusion Nter: None Cter: 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.

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