ID   SYDND_CERS5             Reviewed;         591 AA.
AC   A4WPF7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 95.
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=Rsph17025_0365;
OS   Cereibacter sphaeroides (strain ATCC 17025 / ATH 2.4.3) (Rhodobacter
OS   sphaeroides).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Cereibacter.
OX   NCBI_TaxID=349102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17025 / ATH 2.4.3;
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   Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Richardson P., Mackenzie C., Choudhary M.,
RA   Donohue T.J., Kaplan S.;
RT   "Complete sequence of chromosome of Rhodobacter sphaeroides ATCC 17025.";
RL   Submitted (APR-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; CP000661; ABP69271.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4WPF7; -.
DR   SMR; A4WPF7; -.
DR   STRING; 349102.Rsph17025_0365; -.
DR   PRIDE; A4WPF7; -.
DR   EnsemblBacteria; ABP69271; ABP69271; Rsph17025_0365.
DR   KEGG; rsq:Rsph17025_0365; -.
DR   eggNOG; COG0173; Bacteria.
DR   HOGENOM; CLU_014330_3_2_5; -.
DR   OMA; YQLDVEM; -.
DR   OrthoDB; 226836at2; -.
DR   BioCyc; RSPH349102:G1G8M-372-MON; -.
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_1000006743"
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         453
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT   BINDING         486
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT   BINDING         493
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT   BINDING         538..541
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT   SITE            33
FT                   /note="Important for tRNA non-discrimination"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
SQ   SEQUENCE   591 AA;  66275 MW;  27284BD0D699FA2E CRC64;
     MHAYRSHTCA ELNAGHVGQE VRLSGWVHRV RDHGGVLFID LRDHYGITQV IADADSPAFA
     ELETVRAEWV IRIEGRVKGR DAALVNPKLA TGEIEVYATG LTVLGAADEL PMPVFGEVDY
     PEETRLTYRF LDLRREKLHA NMMLRSNVVR SLRNRMWDAG FNEFQTPIIT ASSPEGARDF
     LVPSRLHPGK FYALPQAPQQ FKQLIMVAGF DRYFQIAPCF RDEDPRADRS PTDFYQLDVE
     MSFVEQEDVF RAVQPVIRGI FEEFGGGRRV DADWPRIAYR DAMLWYGSDK PDLRNPIKMQ
     VVSEHFRGSG FAIFAKLLEN EGTEIRAIPA PTGGSRKFCD RMNAFAQSQG LPGMGYIFWR
     KGDDGAMEAA GPLAKNIGPE RTEAIRQQLG LGEGDAAFFL GGKPETFEAV AGRARNEIGR
     ELGLTEENCF RFAWIVDFPM YEKDDEGKVD FSHNPFSMPQ GGMAALEGDP LKVLAYQYDL
     ACNGYELISG GIRNHKPEIM FKAFELAGYP ASEVEKRFGG MVKAFRYGAP PHGGCAAGID
     RIVMLLADEA NIREVIMFPM NQRAEDLLMG APSEPTNEQL RELRLRVVPK D