SYA_LEUMM
ID SYA_LEUMM Reviewed; 893 AA.
AC Q03YQ2;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 25-MAY-2022, entry version 95.
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=LEUM_0556;
OS Leuconostoc mesenteroides subsp. mesenteroides (strain ATCC 8293 / DSM
OS 20343 / BCRC 11652 / CCM 1803 / JCM 6124 / NCDO 523 / NBRC 100496 / NCIMB
OS 8023 / NCTC 12954 / NRRL B-1118 / 37Y).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Leuconostoc.
OX NCBI_TaxID=203120;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8293 / DSM 20343 / BCRC 11652 / CCM 1803 / JCM 6124 / NCDO 523
RC / NBRC 100496 / NCIMB 8023 / NCTC 12954 / NRRL B-1118 / 37Y;
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; CP000414; ABJ61670.1; -; Genomic_DNA.
DR RefSeq; WP_011679382.1; NC_008531.1.
DR AlphaFoldDB; Q03YQ2; -.
DR SMR; Q03YQ2; -.
DR STRING; 203120.LEUM_0556; -.
DR EnsemblBacteria; ABJ61670; ABJ61670; LEUM_0556.
DR KEGG; lme:LEUM_0556; -.
DR eggNOG; COG0013; Bacteria.
DR HOGENOM; CLU_004485_1_1_9; -.
DR OMA; YHHTMFE; -.
DR OrthoDB; 91428at2; -.
DR Proteomes; UP000000362; 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; RNA-binding; tRNA-binding.
FT CHAIN 1..893
FT /note="Alanine--tRNA ligase"
FT /id="PRO_0000347661"
SQ SEQUENCE 893 AA; 97903 MW; CE915BA26DA283F9 CRC64;
MKDLSSAEIR QMFLDFFASK GHEVVPSKNL IPQDDPTLLW INSGVATLKK YFDGTVVPNN
PRITNSQKAI RTNDIENVGK TARHHTLFEM MGNFSIGDYF KEQAIPWAWE LLTSPEWYGL
DAEKLYVTVY PKDQEARKIW EEKTSLPDGH IYEVEDNFWD IGEGPSGPDS EIFFDRGSSF
QDLPDDDPEM YPGGENERYL EIWNLVFSQF NHLPGLTDNS QYPELPHKNI DTGMGLERVV
SVFQNGRTNF DTDLFLPIIR ATEKLSNQFT YDDSQDSEVN TSFKVIADHI RAITFAIGDG
ALPSNEGRGY VIRRLLRRAV LHGQKLGIKG QFLTNLVPIV GDIMESYYPE VKANTAKIQK
TVAAEEKRFN ATLTGGLSLL NDVIKEAKKT GQTQISGADA FKLSDTYGFP LELTQEQAED
AGLTVDVDRY NDELQAQRVR ARAARSNTKS MGVQNAVLTD LRVDSKYVGW SQTEVNHAEI
VAIIGEDEQG VDALLDNADV DATVQVAFDV TPFYAEMGGQ VPDFGDVLNT NGDVIAHVTD
VQTAPNGQHI HTVDVISSFT LGDKVDLKVD MARHIAVSKN HTATHMLDQS LRNVLGGDVH
QAGSLVEPEY LRFDFNNEGP VSSEDLDKIE SMMNQEIAKN LPVTWLETDI ESAKKLGAVA
VFGEKYGDQV RVVSIGDFNK EFDGGTHANS TAELGLFKIV SESGIGAGVR RIEAVTGLQA
LSQYKAQEKA LKEIATALKA QKLTDAPEKV YDLQADLRTV QRHAESLEAK LANATAGEIF
NDVKTVNGHT YITAQLQVSG MDGLRQVADN WKENYPSDVL VLATVADEKV SLIVAAAPDA
NQSGIKAGEL IKSIAPHIGG GGGGRPDMAQ AGGKKPAGIP DAFAAVSAFL ADK
