ID SYDND_ACIBS Reviewed; 592 AA. AC B0VRC7; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 08-APR-2008, sequence version 1. DT 10-JUN-2026, entry version 105. DE RecName: Full=Aspartate--tRNA(Asp/Asn) ligase {ECO:0000255|HAMAP-Rule:MF_00044}; DE EC=6.1.1.23 {ECO:0000255|HAMAP-Rule:MF_00044}; DE AltName: Full=Aspartyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00044}; DE Short=AspRS {ECO:0000255|HAMAP-Rule:MF_00044}; DE AltName: Full=Non-discriminating aspartyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00044}; DE Short=ND-AspRS {ECO:0000255|HAMAP-Rule:MF_00044}; GN Name=aspS {ECO:0000255|HAMAP-Rule:MF_00044}; GN OrderedLocusNames=ABSDF0538; OS Acinetobacter baumannii (strain SDF). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Moraxellales; Moraxellaceae; Acinetobacter; OC Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=509170; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SDF; RX PubMed=18350144; DOI=10.1371/journal.pone.0001805; RA Vallenet D., Nordmann P., Barbe V., Poirel L., Mangenot S., Bataille E., RA Dossat C., Gas S., Kreimeyer A., Lenoble P., Oztas S., Poulain J., RA Segurens B., Robert C., Abergel C., Claverie J.-M., Raoult D., Medigue C., RA Weissenbach J., Cruveiller S.; RT "Comparative analysis of Acinetobacters: three genomes for three RT lifestyles."; RL PLoS ONE 3:E1805-E1805(2008). CC -!- FUNCTION: Aspartyl-tRNA synthetase with relaxed tRNA specificity since CC it is able to aspartylate not only its cognate tRNA(Asp) but also CC tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first CC activated by ATP to form Asp-AMP and then transferred to the acceptor CC end of tRNA(Asp/Asn). {ECO:0000255|HAMAP-Rule:MF_00044}. CC -!- CATALYTIC ACTIVITY: CC Reaction=tRNA(Asx) + L-aspartate + ATP = L-aspartyl-tRNA(Asx) + AMP + CC diphosphate; Xref=Rhea:RHEA:18349, Rhea:RHEA-COMP:9710, Rhea:RHEA- CC COMP:9711, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78516, ChEBI:CHEBI:456215; CC EC=6.1.1.23; Evidence={ECO:0000255|HAMAP-Rule:MF_00044}; CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00044}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00044}. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. CC Type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_00044}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CU468230; CAO99921.1; -; Genomic_DNA. DR AlphaFoldDB; B0VRC7; -. DR SMR; B0VRC7; -. DR KEGG; abm:ABSDF0538; -. DR HOGENOM; CLU_014330_3_2_6; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004815; F:aspartate-tRNA ligase activity; IEA:UniProtKB-UniRule. DR GO; GO:0050560; F:aspartate-tRNA(Asn) ligase activity; IEA:UniProtKB-EC. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0006422; P:aspartyl-tRNA aminoacylation; IEA:UniProtKB-UniRule. DR CDD; cd00777; AspRS_core; 1. DR CDD; cd04317; EcAspRS_like_N; 1. DR Gene3D; 3.30.930.10; Bira Bifunctional Protein, Domain 2; 1. DR Gene3D; 3.30.1360.30; GAD-like domain; 1. DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1. DR HAMAP; MF_00044; Asp_tRNA_synth_type1; 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; IPR004524; Asp-tRNA-ligase_1. DR InterPro; IPR047089; Asp-tRNA-ligase_1_N. DR InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb. DR InterPro; IPR047090; AspRS_core. DR InterPro; IPR004115; GAD-like_sf. DR InterPro; IPR029351; GAD_dom. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR004365; NA-bd_OB_tRNA. DR NCBIfam; TIGR00459; aspS_bact; 1. DR NCBIfam; NF001750; PRK00476.1; 1. DR PANTHER; PTHR22594:SF5; ASPARTATE--TRNA LIGASE, MITOCHONDRIAL; 1. DR PANTHER; PTHR22594; ASPARTYL/LYSYL-TRNA SYNTHETASE; 1. DR Pfam; PF02938; GAD; 1. DR Pfam; PF00152; tRNA-synt_2; 1. DR Pfam; PF01336; tRNA_anti-codon; 1. DR PRINTS; PR01042; TRNASYNTHASP. DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1. DR SUPFAM; SSF55261; GAD domain-like; 1. DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 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. FT CHAIN 1..592 FT /note="Aspartate--tRNA(Asp/Asn) ligase" FT /id="PRO_1000090948" FT REGION 199..202 FT /note="Aspartate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044" FT BINDING 175 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044" FT BINDING 221..223 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044" FT BINDING 221 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044" FT BINDING 230 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044" FT BINDING 450 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044" FT BINDING 483 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044" FT BINDING 490 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044" FT BINDING 535..538 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044" FT SITE 31 FT /note="Important for tRNA non-discrimination" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044" FT SITE 82 FT /note="Important for tRNA non-discrimination" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044" SQ SEQUENCE 592 AA; 66623 MW; F53C46D58B017C0A CRC64; MMRTHYCGSL TEAQIDQTVT LCGWVHRRRD HGGVIFLDMR DRDGLVQVVI DPDTPEAFAT ADKARSEYVL KITGRVRRRY EGTENPNMVS GQIEVLGKEI EVLAASETPP FPLNDDTINV SEEHRLKYRF LDIRRPEMLD RLRFRSKVTN LIRNYLDDHG FLDVETPILT RATPEGARDY LVPSRVQNGS FYALPQSPQL FKQLLMVGGI DRYYQIAKCF RDEDLRADRQ PEFTQIDIET SFLNDDDIMD LMEGMTVKLF NDLLGVKFEK FRRMPYSEAM RDYASDKPDL RIPLKLVDVA DLMQEVEFKV FAGPAKDPKG RIAALRVPGA GSLTRSQIDE YTKFVGIYGA KGLAYIKVNE IEKGIEGLQS PIVKFIEPIV MQLLERVGAE NGDIVFFGAD KAKIVNDAMG ALRVKIGHDL NLATCEWAPL WVVDFPMFEE ADDGKWTSVH HPFTLPKSSV EDVKSNPGEA LSVAYDMVLN GTEVGGGSLR IYTLEMQKAI FEALGISDEE AEEKFSFLLN ALRYGAPPHG GLAFGLDRLV MLMTGATSIR DVIAFPKTKT AECPLTQAPA PVEANQLRDL GIRLREQQKK EA //