SYA_LACJO
ID SYA_LACJO Reviewed; 882 AA.
AC P61702;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 1.
DT 03-AUG-2022, entry version 116.
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}; OrderedLocusNames=LJ_0474;
OS Lactobacillus johnsonii (strain CNCM I-12250 / La1 / NCC 533).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=257314;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CNCM I-1225 / La1 / NCC 533;
RX PubMed=14983040; DOI=10.1073/pnas.0307327101;
RA Pridmore R.D., Berger B., Desiere F., Vilanova D., Barretto C.,
RA Pittet A.-C., Zwahlen M.-C., Rouvet M., Altermann E., Barrangou R.,
RA Mollet B., Mercenier A., Klaenhammer T., Arigoni F., Schell M.A.;
RT "The genome sequence of the probiotic intestinal bacterium Lactobacillus
RT johnsonii NCC 533.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:2512-2517(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=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 Evidence={ECO:0000255|HAMAP-Rule:MF_00036};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-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; AE017198; AAS08466.1; -; Genomic_DNA.
DR RefSeq; WP_011161609.1; NC_005362.1.
DR AlphaFoldDB; P61702; -.
DR SMR; P61702; -.
DR STRING; 257314.LJ_0474; -.
DR EnsemblBacteria; AAS08466; AAS08466; LJ_0474.
DR KEGG; ljo:LJ_0474; -.
DR PATRIC; fig|257314.6.peg.501; -.
DR eggNOG; COG0013; Bacteria.
DR HOGENOM; CLU_004485_1_1_9; -.
DR OMA; YHHTMFE; -.
DR Proteomes; UP000000581; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004813; F:alanine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006419; P:alanyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.930.10; -; 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 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; SSF101353; SSF101353; 1.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF55186; SSF55186; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00344; alaS; 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; Reference proteome; RNA-binding;
KW tRNA-binding; Zinc.
FT CHAIN 1..882
FT /note="Alanine--tRNA ligase"
FT /id="PRO_0000075129"
FT BINDING 568
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT BINDING 572
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 882 AA; 98403 MW; 60586CEABFE704DA CRC64;
MKQLTSSQVR QMFLDFFKEH GHMVMQSASL IPQDDPTLLW INSGVATMKK YFDGSVVPKN
HRITSSQKSI RTNDIENVGK TARHQTFFEM LGNFSVGDYF KKEVIPWAWE FLTSPKWLGL
DPDKLYVTVY PKDTEAYHMW HDVVGLPEDH IVKLEDNFWD IGEGPCGPDS EIFYDRGQEN
NDVAEDDPEN FPGGENARYL EIWNIVFSQF NHLPNGKYVD QPHKNIDTGM GLERVVSIIQ
DAPTNFETDL FMPIIKETEK LSDGKKYAAN KEDDVAFKII ADHVRAVSFA IADGALPSNS
GRGYVLRRLI RRADLNGQRL GIKGAFLYKL VPVVGEIMKS HYPEVVDQQA FIQKVIKNEE
ERFQVTLSSG LNLLDNIIAE AKKSDDKTIS GKDAFKLFDT YGFPYELTFE AAQDAGLKID
KKGFDEEMKA QKERARKARG NLQSMGSQDV TLMNIKDKSE FEYGTLEEKH AKLIDIVVDD
KLVDKADGEH ATLIFDKTPF YAERGGQVAD HGEILNQNGE LVARVTDVQH APNDQNLHFV
DVILPLEKGQ EYVLKVDQKR RRGLKHNHTA THLLHAALRE VLGTHTHQAG SLVEPDYLRF
DFTSLEPMTK KEIASVEKLV NEKIWEEIPV KTTVTDPDTG LKMGALALFG EKYGDTVRVV
QIDDFSTEFC GGTHCENTDQ IGMLKIVSES AVGAGTRRII AVTGPEAYKY VTDRDEILKE
VQDEVKATKA EDVVNKISSI EDDLRASQKE AEQLKAQINK AKAGDLFNDI KQVKDLTVIA
AQADVEGMND LRELADNWKS SNKSDVLVLA AEVNGKANMV ISLDDKAIKA GLKAGDLIKT
AAPIFGGGGG GRPNMAQAGG KNPAGLKDAI AKVLQEVEEK QN
