ID   SYA_ACIAD               Reviewed;         878 AA.
AC   Q6FCT2;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   04-NOV-2026, entry version 134.
DE   RecName: Full=Alanine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00036};
DE            EC=6.1.1.7 {ECO:0000255|HAMAP-Rule:MF_00036};
DE   AltName: Full=Alanyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00036};
DE            Short=AlaRS {ECO:0000255|HAMAP-Rule:MF_00036};
GN   Name=alaS {ECO:0000255|HAMAP-Rule:MF_00036};
GN   OrderedLocusNames=ACIAD1253;
OS   Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Moraxellales; Moraxellaceae; Acinetobacter.
OX   NCBI_TaxID=62977;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33305 / BD413 / ADP1;
RX   PubMed=15514110; DOI=10.1093/nar/gkh910;
RA   Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA   Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA   Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT   "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT   a versatile and naturally transformation competent bacterium.";
RL   Nucleic Acids Res. 32:5766-5779(2004).
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. {ECO:0000255|HAMAP-Rule:MF_00036}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=tRNA(Ala) + L-alanine + ATP = L-alanyl-tRNA(Ala) + AMP +
CC         diphosphate; 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         Evidence={ECO:0000255|HAMAP-Rule:MF_00036};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00036};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00036};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00036}.
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. {ECO:0000255|HAMAP-Rule:MF_00036}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00036}.
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DR   EMBL; CR543861; CAG68127.1; -; Genomic_DNA.
DR   RefSeq; WP_004925983.1; NC_005966.1.
DR   SMR; Q6FCT2; -.
DR   STRING; 202950.GCA_001485005_01018; -.
DR   GeneID; 45233677; -.
DR   KEGG; aci:ACIAD1253; -.
DR   eggNOG; COG0013; Bacteria.
DR   HOGENOM; CLU_004485_1_1_6; -.
DR   OMA; AAAKWMY; -.
DR   OrthoDB; 9803884at2; -.
DR   BioCyc; ASP62977:ACIAD_RS05770-MONOMER; -.
DR   CDD; cd00673; AlaRS_core; 1.
DR   FunFam; 2.40.30.130:FF:000001; Alanine--tRNA ligase; 1.
DR   FunFam; 3.10.310.40:FF:000001; Alanine--tRNA ligase; 1.
DR   FunFam; 3.30.930.10:FF:000004; Alanine--tRNA ligase; 1.
DR   FunFam; 3.30.980.10:FF:000004; Alanine--tRNA ligase, cytoplasmic; 1.
DR   Gene3D; 2.40.30.130; -; 1.
DR   Gene3D; 3.10.310.40; -; 1.
DR   Gene3D; 3.30.54.20; -; 1.
DR   Gene3D; 6.10.250.550; -; 1.
DR   Gene3D; 3.30.930.10; Bira Bifunctional Protein, Domain 2; 1.
DR   Gene3D; 3.30.980.10; Threonyl-trna Synthetase, Chain A, domain 2; 1.
DR   HAMAP; MF_00036_B; Ala_tRNA_synth_B; 1.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR002318; Ala-tRNA-lgiase_IIc.
DR   InterPro; IPR018162; Ala-tRNA-ligase_IIc_anticod-bd.
DR   InterPro; IPR018165; Ala-tRNA-synth_IIc_core.
DR   InterPro; IPR018164; Ala-tRNA-synth_IIc_N.
DR   InterPro; IPR023033; Ala_tRNA_ligase_euk/bac.
DR   InterPro; IPR003156; DHHA1_dom.
DR   InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   InterPro; IPR012947; tRNA_SAD.
DR   PANTHER; PTHR11777:SF9; ALANINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR   PANTHER; PTHR11777; ALANYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF02272; DHHA1; 1.
DR   Pfam; PF01411; tRNA-synt_2c; 1.
DR   Pfam; PF07973; tRNA_SAD; 1.
DR   PRINTS; PR00980; TRNASYNTHALA.
DR   SMART; SM00863; tRNA_SAD; 1.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   SUPFAM; SSF101353; Putative anticodon-binding domain of alanyl-tRNA synthetase (AlaRS); 1.
DR   SUPFAM; SSF55186; ThrRS/AlaRS common domain; 1.
DR   SUPFAM; SSF50447; Translation proteins; 1.
DR   NCBIfam; TIGR00344; alaS; 1.
DR   PROSITE; PS50860; AA_TRNA_LIGASE_II_ALA; 1.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0004813; F:alanine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0002161; F:aminoacyl-tRNA deacylase activity; IEA:TreeGrafter.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006419; P:alanyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; IEA:TreeGrafter.
DR   Proteomes; UP000000430; Chromosome.
DR   AlphaFoldDB; Q6FCT2; -.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Metal-binding;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome; RNA-binding;
KW   tRNA-binding; Zinc.
FT   CHAIN           1..878
FT                   /note="Alanine--tRNA ligase"
FT                   /id="PRO_0000075043"
FT   BINDING         562
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT   BINDING         566
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT   BINDING         670
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT   BINDING         674
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
SQ   SEQUENCE   878 AA;  96691 MW;  2594DCD48229355A CRC64;
     MTSAEIREAF LRYFESQGHT RVASSSLVPA NDPTLLFTNA GMNQFKDCFL GLEKRDYVRA
     TTSQKCVRAG GKHNDLDNVG YTARHHTFFE MLGNFSFGDY FKRDALTFAW DFLTSEQWLG
     LPKDKLYVTV YHTDDEAYDI WNKEIGLAAD RIIRIGDNKG EKYASDNFWA MGDTGPCGPC
     SEIFFDHGDH IWGGLPGTPE EDGDRFIEIW NNVFMQFNRT ADGVLHPLPA PSVDTGMGLE
     RISAVLQHVN SNYDIDLFQH LIKSACEIIN VKDEGQPSLR VVADHARSCC FLIADGVNPS
     NEGRGYVLRR IIRRAVRHGN KLGATGTFFY KMLQPLIDVM GDAYPELKND QARIEATLIR
     EEEQFAKTLE QGLKLLEGEL TQLSGKVIPG ETVFKLYDTY GFPTDLTADI ARERDLEIDE
     VGFEREMEAQ RRRARDAGKF AVDYNSIVKV EGETQFDGYH ATAGQGEIVA IYKDGEQVDE
     VVEGDEALIV LNQTPFYAES GGQIGDTGLF KNDTGIFEVQ DTKKSGGAFV HQGIVTMGSL
     KAAQHVDAIV KADIRAATAR NHSATHLLHA ALRQILGTHV QQKGSLVASD ILRFDFANDQ
     PVSFEQLQEI ERLVNAEVIA NSAVTTELLD IESAKAKGAM MLFGEKYGDE VRVLSMGSVI
     DEHNFSIELC GGIHVQRTGD IGLFKIISEG GVAAGIRRIE AVTGTKALEV VQKADADIQH
     INSLLKAQKD QTVERVQAAV EQTSALHKQI EQLNQKLANF QAAELLSQVQ NIAGRSTLIT
     TVQNIDAKSL RNLHDSVKSK LEDAVIVLAG LEGDKISLIA SVAKQYTAHL KAGDIIKHLA
     TELGGKGGGK PDLAQGGAPL NEKFEHVIAA LPAWLEQH
//