ID   SYA_BACC1               Reviewed;         880 AA.
AC   P61697;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2004, sequence version 1.
DT   04-NOV-2026, entry version 115.
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=BCE_4471;
OS   Bacillus cereus (strain ATCC 10987 / NRS 248).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae;
OC   Bacillus; Bacillus cereus group.
OX   NCBI_TaxID=222523;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10987 / NRS 248;
RX   PubMed=14960714; DOI=10.1093/nar/gkh258;
RA   Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L.,
RA   Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F.,
RA   Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.;
RT   "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic
RT   adaptations and a large plasmid related to Bacillus anthracis pXO1.";
RL   Nucleic Acids Res. 32:977-988(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; AE017194; AAS43372.1; -; Genomic_DNA.
DR   AlphaFoldDB; P61697; -.
DR   SMR; P61697; -.
DR   KEGG; bca:BCE_4471; -.
DR   HOGENOM; CLU_004485_1_1_9; -.
DR   OMA; AAAKWMY; -.
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:0140096; F:catalytic activity, acting on a protein; IEA:UniProtKB-ARBA.
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   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:000046; 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   NCBIfam; TIGR00344; alaS; 1.
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   PROSITE; PS50860; AA_TRNA_LIGASE_II_ALA; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Metal-binding;
KW   Nucleotide-binding; Protein biosynthesis; RNA-binding; tRNA-binding; Zinc.
FT   CHAIN           1..880
FT                   /note="Alanine--tRNA ligase"
FT                   /id="PRO_0000075051"
FT   BINDING         567
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT   BINDING         571
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT   BINDING         669
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT   BINDING         673
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
SQ   SEQUENCE   880 AA;  97414 MW;  8DF9F2B9531DB18F CRC64;
     MKQLTGAQIR QMFLDFFQEK GHAVEPSASL VPHEDPSLLW INSGVATLKK YFDGRVIPQN
     PRITNAQKSI RTNDIENVGK TARHHTFFEM LGNFSIGDYF KEEAITWAWE FLTSDKWIGF
     DKELLSVTIH PEDEEAFTIW NEKMGVPKER IIRLEENFWD IGEGPSGPNT EIFYDRGEAY
     GNDFSDPELY PGGENERYLE VWNLVFSQFN HNPDGSYTPL PKKNIDTGMG LERMTSIVQD
     VPTNFDTDLF MPMIGATETI SGEKYRNGDL EKDMAFKVIA DHIRTVTFAV GDGALPSNEG
     RGYVLRRLLR RAVRYSKKLN INRPFMFELV PVVGEVMKDF YPEVLEKKDF IAKVVKNEEE
     RFHETLHDGE AILAEVIAKA KEEKTTVISG VDAFRLYDTY GFPIELTEEY AEEAGMTVDH
     EGFENEMEKQ RERARAARQD VDSMQVQGGV LGEVKVASEF VGYGTVATES NVVALVKNGE
     YADSLQAGEE GQLMLDVTPF YAESGGQIAD RGYLLADGVK VLVKDVQKAP NGQNLHKVVV
     EEGTLTKDAA VKAIIDTKNR SSVVKNHTAT HLLHQALKDV LGTHVNQAGS LVTSERLRFD
     FSHFGQVQAD ELEKIERIVN EKIWESIDVE ISQKAIEEAK EMGAMALFGE KYGDVVRVVQ
     VGDYSLELCG GCHVDNTASI GIFKIVAESG IGAGTRRIEA VTGKSAYELM NDQVGLLKEA
     AGKMKTNPKD ILTRVDGLFA EVKQLQKENE SLAAKLSNIE AGNLTDSVMT VDGVNVLAAK
     VNVADMNNLR TMMDDLKNKL QSAVVVLASV NDDKVNILAG VTKDLISQGY HAGKLVKEVA
     SRCGGGGGGR PDMAQAGGKN PAQVEEALAF VQEYVKSVSK
//