ID   SYDND_PSEP1             Reviewed;         591 AA.
AC   A5VZU3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 90.
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}; OrderedLocusNames=Pput_1242;
OS   Pseudomonas putida (strain ATCC 700007 / DSM 6899 / BCRC 17059 / F1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=351746;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700007 / DSM 6899 / BCRC 17059 / F1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Lykidis A., Parales R., Richardson P.;
RT   "Complete sequence of Pseudomonas putida F1.";
RL   Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
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=ATP + L-aspartate + tRNA(Asx) = AMP + diphosphate + L-
CC         aspartyl-tRNA(Asx); Xref=Rhea:RHEA:18349, Rhea:RHEA-COMP:9710,
CC         Rhea:RHEA-COMP:9711, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78516,
CC         ChEBI:CHEBI:456215; EC=6.1.1.23; Evidence={ECO:0000255|HAMAP-
CC         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}.
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DR   EMBL; CP000712; ABQ77403.1; -; Genomic_DNA.
DR   RefSeq; WP_004575741.1; NC_009512.1.
DR   AlphaFoldDB; A5VZU3; -.
DR   SMR; A5VZU3; -.
DR   STRING; 351746.Pput_1242; -.
DR   PRIDE; A5VZU3; -.
DR   EnsemblBacteria; ABQ77403; ABQ77403; Pput_1242.
DR   KEGG; ppf:Pput_1242; -.
DR   eggNOG; COG0173; Bacteria.
DR   HOGENOM; CLU_014330_3_2_6; -.
DR   OMA; YQLDVEM; -.
DR   OrthoDB; 226836at2; -.
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   Gene3D; 2.40.50.140; -; 1.
DR   Gene3D; 3.30.1360.30; -; 1.
DR   Gene3D; 3.30.930.10; -; 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; IPR002312; Asp/Asn-tRNA-synth_IIb.
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   PANTHER; PTHR22594:SF5; PTHR22594:SF5; 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; SSF50249; SSF50249; 1.
DR   SUPFAM; SSF55261; SSF55261; 1.
DR   SUPFAM; SSF55681; SSF55681; 1.
DR   TIGRFAMs; TIGR00459; aspS_bact; 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..591
FT                   /note="Aspartate--tRNA(Asp/Asn) ligase"
FT                   /id="PRO_1000006731"
FT   REGION          198..201
FT                   /note="Aspartate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT   BINDING         174
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT   BINDING         220..222
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT   BINDING         220
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT   BINDING         229
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   591 AA;  66568 MW;  B823515D39E52E0F CRC64;
     MMRSHYCGQL NESLDGQEVT LCGWVHRRRD HGGVIFLDIR DREGMAQVVF DPDRAETFAA
     ADRVRSEYVV QITGKVRKRP EGAVNANMAS GAIEILGYQL NVLNEAETPP FPLNEYSDVG
     EETRLRYRFI DLRRPEMADK LRLRSRITSS IRRFLDENGF LDVETPILTR ATPEGARDYL
     VPSRTHAGSF FALPQSPQLF KQLLMVAGFD RYYQIAKCFR DEDLRADRQP EFTQIDIETS
     FLDESEIMGL TESMIRKLFK EVLDLEFGEF PHMTFEEAMR RYGSDKPDLR IPLELVDVAD
     QLKDVDFKVF AGPANDPKCR VTALRLPGGA SMPRSKIDEY TKFVGIYGAK GLAYIKVNER
     AKGVEGLQSP IVKNIPEANL NNILDRVGAV DGDIVFFGAD KFKVVSEALG ALRIRLGHDF
     ELLTCEWAPM WVVDFPMFEE NEDGSFTALH HPFTAPKCTP EELEANPATA LSRAYDMVLN
     GTELGGGSIR IHRKEMQQAV FRLLGIEAEE QEEKFGFLLD ALKFGAPPHG GLAFGLDRLV
     MLMTGAQSIR EVIAFPKTQS AACVMTQAPG MVDAKALREL HIRLREQTKV E