ID   SYA_OENOB               Reviewed;         885 AA.
AC   Q04EQ9;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=Alanine--tRNA ligase;
DE            EC=6.1.1.7;
DE   AltName: Full=Alanyl-tRNA synthetase;
DE            Short=AlaRS;
GN   Name=alaS; OrderedLocusNames=OEOE_1167;
OS   Oenococcus oeni (strain ATCC BAA-331 / PSU-1).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Oenococcus.
OX   NCBI_TaxID=203123;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-331 / PSU-1;
RX   PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA   Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V.,
RA   Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA   Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA   Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA   Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA   Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA   Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R.,
RA   O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T.,
RA   Richardson P., Kozyavkin S., Weimer B.C., Mills D.A.;
RT   "Comparative genomics of the lactic acid bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
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 (By similarity). {ECO:0000250}.
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; CP000411; ABJ57063.1; -; Genomic_DNA.
DR   RefSeq; WP_011677637.1; NC_008528.1.
DR   AlphaFoldDB; Q04EQ9; -.
DR   SMR; Q04EQ9; -.
DR   STRING; 203123.OEOE_1167; -.
DR   EnsemblBacteria; ABJ57063; ABJ57063; OEOE_1167.
DR   KEGG; ooe:OEOE_1167; -.
DR   PATRIC; fig|203123.7.peg.1192; -.
DR   eggNOG; COG0013; Bacteria.
DR   HOGENOM; CLU_004485_1_1_9; -.
DR   OMA; YHHTMFE; -.
DR   OrthoDB; 91428at2; -.
DR   Proteomes; UP000000774; 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: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;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome; RNA-binding;
KW   tRNA-binding.
FT   CHAIN           1..885
FT                   /note="Alanine--tRNA ligase"
FT                   /id="PRO_0000347707"
SQ   SEQUENCE   885 AA;  98215 MW;  805DAFEB97C1AD67 CRC64;
     MKKLNSAQIR QMFLDFFQSK GHKIEPSQSL IPQDDPSLLW INSGVATLKK YFDGSVIPDN
     PRITNAQKSI RTNDIENVGH TARHHTFFEM LGNFSVGDYF KKEAIPWAWE LLTSPEWYGI
     EPEKLFITYY PRDTETKELW ESQADFVAGH TIPQDDNFWD IGEGPSGPDT EVFFDRGPKF
     QNLPDNDPEM YPGGENERYL EIWNIVFSQF NHLPGLTDNS KYPELPHKNI DTGMGLERVV
     SIFENAPTNF ETDLFLPIIR KVEQLSGKRY GKIKDEDVSF KVITDHIRAV TFAISDGALP
     GNTGRGYVIR RLLRRAVMHG RKLEIEKPFL TQLVPIVGKI MEAYYPEILE NEDKIIPVIQ
     SEEGRFNKTL TAGLNLLDDL IEKAHKDNAT QISGKDAFKL FDTYGFPLES TEEQAADAGL
     TVDTTSFDKE MKDQQNRART AQGKLKTFGF QDEALMSLKV PSVYVGWKQS SVDDAKIAAI
     IVDDQQVDDA KAGQKALLIF DKTPFYAEMG GQVADQGTVQ AANGKVLAQV TDVQNAPNKQ
     HIHTAKLISD LKIGQKVNLR LDMHRHVAVS KNHTATHLLD QALRNVIAGN IHQAGSLVEP
     DYLRFDFTHQ GPVPTETLDR IEDLVNQKIA DALPVSWIET DIESAKKLGA VAVFGEKYGK
     KVRVVSIGDF NKEFDGGTHA KNTSELGLFK IVSESGIGAG TRRIEAVTGQ SAFKMLKNHE
     KLLKKAAEFL SAQKLADVPD KIVDLQNNLK NVQKQVESLS DKAANVAADK IFEKTLEAGK
     YSYIAAQIDN QTVDGLRKIV DEWRQRAVSD LIIIATNNNG KALLVAASAK PNEVKAGNVV
     KAISPKIQGG GGGRPDFAQA GGKNPAGIAN ALASVSEYLE SLDQR