SYN_LACDA
ID SYN_LACDA Reviewed; 432 AA.
AC P54262; P77878; Q1G9Z5;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Asparagine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00534};
DE EC=6.1.1.22 {ECO:0000255|HAMAP-Rule:MF_00534};
DE AltName: Full=Asparaginyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00534};
DE Short=AsnRS {ECO:0000255|HAMAP-Rule:MF_00534};
GN Name=asnS1 {ECO:0000255|HAMAP-Rule:MF_00534}; Synonyms=asnS, asnSa;
GN OrderedLocusNames=Ldb1004;
GN and
GN Name=asnS2 {ECO:0000255|HAMAP-Rule:MF_00534}; Synonyms=asnSb;
GN OrderedLocusNames=Ldb1195;
OS Lactobacillus delbrueckii subsp. bulgaricus (strain ATCC 11842 / DSM 20081
OS / BCRC 10696 / JCM 1002 / NBRC 13953 / NCIMB 11778 / NCTC 12712 / WDCM
OS 00102 / Lb 14).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=390333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8636057; DOI=10.1128/jb.178.8.2459-2461.1996;
RA Kim S.I., Germond J.-E., Pridmore D., Soell D.;
RT "Lactobacillus bulgaricus asparagine synthetase and asparaginyl-tRNA
RT synthetase: coregulation by transcription antitermination?";
RL J. Bacteriol. 178:2459-2461(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8758990; DOI=10.1093/nar/24.14.2648;
RA Kim S.I., Nalaskowska M., Germond J.-E., Pridmore D., Soell D.;
RT "Asn-tRNA in Lactobacillus bulgaricus is formed by asparaginylation of tRNA
RT and not by transamidation of Asp-tRNA.";
RL Nucleic Acids Res. 24:2648-2651(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11842 / DSM 20081 / BCRC 10696 / JCM 1002 / NBRC 13953 / NCIMB
RC 11778 / NCTC 12712 / WDCM 00102 / Lb 14;
RX PubMed=16754859; DOI=10.1073/pnas.0603024103;
RA van de Guchte M., Penaud S., Grimaldi C., Barbe V., Bryson K., Nicolas P.,
RA Robert C., Oztas S., Mangenot S., Couloux A., Loux V., Dervyn R., Bossy R.,
RA Bolotin A., Batto J.-M., Walunas T., Gibrat J.-F., Bessieres P.,
RA Weissenbach J., Ehrlich S.D., Maguin E.;
RT "The complete genome sequence of Lactobacillus bulgaricus reveals extensive
RT and ongoing reductive evolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:9274-9279(2006).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-asparagine + tRNA(Asn) = AMP + diphosphate + H(+) + L-
CC asparaginyl-tRNA(Asn); Xref=Rhea:RHEA:11180, Rhea:RHEA-COMP:9659,
CC Rhea:RHEA-COMP:9674, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58048, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78515, ChEBI:CHEBI:456215; EC=6.1.1.22;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00534};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00534}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00534}.
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DR EMBL; X89438; CAA61603.1; -; Genomic_DNA.
DR EMBL; X89439; CAA61604.1; -; Genomic_DNA.
DR EMBL; CR954253; CAI97806.1; -; Genomic_DNA.
DR EMBL; CR954253; CAI97997.1; -; Genomic_DNA.
DR PIR; S71072; S71072.
DR PIR; S71074; S71074.
DR RefSeq; WP_011543871.1; NC_008054.1.
DR AlphaFoldDB; P54262; -.
DR SMR; P54262; -.
DR STRING; 390333.Ldb1004; -.
DR EnsemblBacteria; CAI97806; CAI97806; Ldb1004.
DR EnsemblBacteria; CAI97997; CAI97997; Ldb1195.
DR KEGG; ldb:Ldb1004; -.
DR KEGG; ldb:Ldb1195; -.
DR PATRIC; fig|390333.7.peg.1065; -.
DR eggNOG; COG0017; Bacteria.
DR HOGENOM; CLU_004553_2_0_9; -.
DR OMA; DNMDLAE; -.
DR BioCyc; LDEL390333:LDB_RS04395-MON; -.
DR BioCyc; LDEL390333:LDB_RS05130-MON; -.
DR Proteomes; UP000001259; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004816; F:asparagine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006421; P:asparaginyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR HAMAP; MF_00534; Asn_tRNA_synth; 1.
DR InterPro; IPR004364; Aa-tRNA-synt_II.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004522; Asn-tRNA-ligase.
DR InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004365; NA-bd_OB_tRNA.
DR Pfam; PF00152; tRNA-synt_2; 1.
DR Pfam; PF01336; tRNA_anti-codon; 1.
DR PRINTS; PR01042; TRNASYNTHASP.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00457; asnS; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..432
FT /note="Asparagine--tRNA ligase"
FT /id="PRO_0000176415"
FT CONFLICT 266
FT /note="V -> L (in Ref. 1; CAA61604)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 432 AA; 50001 MW; EB6377372532B8B8 CRC64;
MTELISIRES SKHVDEEVRM HVWLTDKRSS GKIVFLQLRD GTAFFQGVVR KNDVSEEVFE
AAKGLRQEAS FYLTGTIHED ARSHFGYEIQ ISDLEVVSNN EGYPITNKEH GIDFLLDHRH
LWLRSRRPFA IMQIRNRIFK ATVDFFENEG FVKFDAPLLM HSAPEGTTEL FHIDYFNHDA
YLSQSGQLYG EVGAEAFGKI FTFGPTFRAE ASKTRRHLTE FWMMEPEMAW MHQDESLDLQ
ERFLSYVVGQ VLEHCEYELS ILGRDVDKLR PAAEGNYTRL SYDDAVKMLQ EAGKDFKWGD
DFGAPDEAFL SEQFDRPFFI VNYPVAIKPF YMKKNPENPL TYLCADVEAP EGYGEIMGGS
EREADYDTLK AQIEEAGLNL DDYSWYLDLR KYGSVPHSGF GMGFERVIAW ICKLDHVREA
VPFPRMINRM QP
