ID   SYDND_PSESM             Reviewed;         591 AA.
AC   Q87Y31;
DT   24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 122.
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=PSPTO_3981;
OS   Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=223283;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-871 / DC3000;
RX   PubMed=12928499; DOI=10.1073/pnas.1731982100;
RA   Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T.,
RA   Gwinn M.L., Dodson R.J., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA   Daugherty S.C., Brinkac L.M., Beanan M.J., Haft D.H., Nelson W.C.,
RA   Davidsen T.M., Zafar N., Zhou L., Liu J., Yuan Q., Khouri H.M.,
RA   Fedorova N.B., Tran B., Russell D., Berry K.J., Utterback T.R.,
RA   Van Aken S.E., Feldblyum T.V., D'Ascenzo M., Deng W.-L., Ramos A.R.,
RA   Alfano J.R., Cartinhour S., Chatterjee A.K., Delaney T.P., Lazarowitz S.G.,
RA   Martin G.B., Schneider D.J., Tang X., Bender C.L., White O., Fraser C.M.,
RA   Collmer A.;
RT   "The complete genome sequence of the Arabidopsis and tomato pathogen
RT   Pseudomonas syringae pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(2003).
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; AE016853; AAO57440.1; -; Genomic_DNA.
DR   RefSeq; NP_793745.1; NC_004578.1.
DR   RefSeq; WP_011104814.1; NC_004578.1.
DR   AlphaFoldDB; Q87Y31; -.
DR   SMR; Q87Y31; -.
DR   STRING; 223283.PSPTO_3981; -.
DR   PRIDE; Q87Y31; -.
DR   EnsemblBacteria; AAO57440; AAO57440; PSPTO_3981.
DR   GeneID; 1185657; -.
DR   KEGG; pst:PSPTO_3981; -.
DR   PATRIC; fig|223283.9.peg.4081; -.
DR   eggNOG; COG0173; Bacteria.
DR   HOGENOM; CLU_014330_3_2_6; -.
DR   OMA; YQLDVEM; -.
DR   OrthoDB; 226836at2; -.
DR   PhylomeDB; Q87Y31; -.
DR   Proteomes; UP000002515; Chromosome.
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; Reference proteome.
FT   CHAIN           1..591
FT                   /note="Aspartate--tRNA(Asp/Asn) ligase"
FT                   /id="PRO_0000110926"
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;  66352 MW;  4A841555305FBF36 CRC64;
     MMRSHYCGQL NESLEGQEIT LCGWVHRRRD HGGVIFLDIR DREGMAQVVF DPDRADSFAA
     ADRVRSEYVV KVVGKVRARP AGAVNANMAS GAIEVLGYEL EVLNESETPP FPLNEYSDVG
     EETRLRYRFI DLRRPEMAEK LRLRSRITTS IRRYLDENGF LDVETPILTR ATPEGARDYL
     VPSRTHPGSF FALPQSPQLF KQLLMVAGFD RYYQIAKCFR DEDLRADRQP EFTQIDIETS
     FLNEEDIIGL TEKMVRQLFK EVLNVEFGDF PHMTFEEAMR RYGSDKPDLR NPLELVDVAD
     QLNAVEFKVF SGPANDPKGR VAALRVPGAA SMARSQIDDY TKFVSIYGAK GLAYIKVNER
     AKGPEGLQSP IVKFIPEENL NVILDRVGAV DGDIVFFGAD KFKVVSEALG ALRIKIGNDL
     KLHTCEWAPM WVVDFPMFEE NDDGSFSALH HPFTAPKCTP EELEANPATA LSRAYDMVLN
     GTELGGGSIR IHRKEMQQAV FRLLGIAEDE QQEKFGFLLD ALKYGAPPHG GLAFGLDRLV
     MLMTGAQSIR EVIAFPKTQS AADVMTQAPG VVDAKALREL HIRLREQPKA E