SYDND_DEIRA
ID SYDND_DEIRA Reviewed; 435 AA.
AC Q9RVH4;
DT 11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Aspartate--tRNA(Asp/Asn) ligase {ECO:0000255|HAMAP-Rule:MF_02075};
DE EC=6.1.1.23 {ECO:0000255|HAMAP-Rule:MF_02075};
DE AltName: Full=Aspartyl-tRNA synthetase 2;
DE Short=AspRS2;
DE AltName: Full=Non-discriminating aspartyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02075};
DE Short=ND-AspRS {ECO:0000255|HAMAP-Rule:MF_02075};
GN Name=aspS2; OrderedLocusNames=DR_1055;
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
RN [2]
RP FUNCTION AS A NON-DISCRIMINATING ASPRS, AND GENE NAME.
RX PubMed=9789001; DOI=10.1073/pnas.95.22.12838;
RA Curnow A.W., Tumbula D.L., Pelaschier J.T., Min B., Soll D.;
RT "Glutamyl-tRNA(Gln) amidotransferase in Deinococcus radiodurans may be
RT confined to asparagine biosynthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:12838-12843(1998).
RN [3]
RP FUNCTION AS A NON-DISCRIMINATING ASPRS, CATALYTIC ACTIVITY, SUBSTRATE
RP SPECIFICITY, KINETIC PARAMETERS, MUTAGENESIS OF HIS-28 AND PRO-77, AND
RP DISCRIMINATION SITE.
RX PubMed=15781458; DOI=10.1074/jbc.m500874200;
RA Feng L., Yuan J., Toogood H., Tumbula-Hansen D., Soll D.;
RT "Aspartyl-tRNA synthetase requires a conserved proline in the anticodon-
RT binding loop for tRNA(Asn) recognition in vivo.";
RL J. Biol. Chem. 280:20638-20641(2005).
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). Is slightly more efficient at aminoacylating
CC tRNA(Asn) over tRNA(Asp). {ECO:0000269|PubMed:15781458,
CC ECO:0000269|PubMed:9789001}.
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_02075, ECO:0000269|PubMed:15781458};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.8 uM for tRNA(Asp) {ECO:0000269|PubMed:15781458};
CC KM=2.0 uM for tRNA(Asn) {ECO:0000269|PubMed:15781458};
CC Note=kcat is 0.15 sec(-1) for tRNA(Asp) aspartylation and 0.51 sec(-
CC 1) for tRNA(Asn) aspartylation.;
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02075}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02075}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC Type 2 subfamily. {ECO:0000255|HAMAP-Rule:MF_02075}.
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DR EMBL; AE000513; AAF10623.1; -; Genomic_DNA.
DR PIR; H75443; H75443.
DR RefSeq; NP_294779.1; NC_001263.1.
DR RefSeq; WP_010887698.1; NZ_CP015081.1.
DR AlphaFoldDB; Q9RVH4; -.
DR SMR; Q9RVH4; -.
DR STRING; 243230.DR_1055; -.
DR EnsemblBacteria; AAF10623; AAF10623; DR_1055.
DR KEGG; dra:DR_1055; -.
DR PATRIC; fig|243230.17.peg.1250; -.
DR eggNOG; COG0017; Bacteria.
DR HOGENOM; CLU_004553_2_1_0; -.
DR InParanoid; Q9RVH4; -.
DR OMA; WVHEIRD; -.
DR OrthoDB; 1138123at2; -.
DR BioCyc; MetaCyc:MON-14054; -.
DR Proteomes; UP000002524; Chromosome I.
DR GO; GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004815; F:aspartate-tRNA ligase activity; IBA:GO_Central.
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:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0006422; P:aspartyl-tRNA aminoacylation; IBA:GO_Central.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR HAMAP; MF_02075; Asp_tRNA_synth_type2; 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; IPR004523; Asp-tRNA_synthase_2.
DR InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004365; NA-bd_OB_tRNA.
DR PANTHER; PTHR43450; PTHR43450; 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; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00458; aspS_nondisc; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 1: Evidence at protein level;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..435
FT /note="Aspartate--tRNA(Asp/Asn) ligase"
FT /id="PRO_0000429272"
FT REGION 185..188
FT /note="Aspartate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02075"
FT BINDING 163
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02075"
FT BINDING 206..208
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02075"
FT BINDING 206
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02075"
FT BINDING 214..216
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02075"
FT BINDING 358
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02075"
FT BINDING 361
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02075"
FT BINDING 365
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02075"
FT BINDING 406..409
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02075"
FT SITE 77
FT /note="Important for tRNA non-discrimination"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02075"
FT MUTAGEN 28
FT /note="H->Q: Enhances enzyme specificity for tRNA(Asp) over
FT tRNA(Asn)."
FT /evidence="ECO:0000269|PubMed:15781458"
FT MUTAGEN 77
FT /note="P->C,I,L,F,S,V: Seems not to be able to charge
FT tRNA(Asn) in vivo, but Asp-tRNA(Asp) formation is not
FT affected."
FT /evidence="ECO:0000269|PubMed:15781458"
FT MUTAGEN 77
FT /note="P->K: Enhances enzyme specificity for tRNA(Asp) over
FT tRNA(Asn), by decreasing the ability to form Asp-tRNA(Asn)
FT and increasing the efficiency of Asp-tRNA(Asp) synthesis in
FT vitro. Seems not to be able to charge tRNA(Asn) in vivo."
FT /evidence="ECO:0000269|PubMed:15781458"
SQ SEQUENCE 435 AA; 48231 MW; 8429EA90841D304D CRC64;
MTSPLKRTLT RELPQHEGQT VKLQGFVHAR RDLGGVQFLV LRDVTGVTQC VGSGLTLPLA
ESSVEVVGKV KAHPKAPGGF EVQVEDFRVI SAATEATPVE IPKMEWNVNP ETMLDYRVVT
VRGLKERAAL KVQAELVDAF RAHLRGEGFT EISTPKIVSA GAEGGANLFP IDYFGHPAYL
AQSPQLYKQI MVGVFERVFE VAAVYRAEEH ATSRHLNEYL SLDVEMGFIE DEEDVMGLEN
RLLASIMERL RATSQAEFEL LGATIPDVPA HIPRITLMDA RQLVTEKYGH PVGGKDLDPE
AERLLSQHFA ETEGSDFVFV TKYPRAARPF YAHPELNEDG SVNGEVTRGF DLLFRGIEIT
SGGQRIHDYG MLMDSIAAYK LKPESLEGYT EVFKYGMPPH GGFAIGAERL TAKLLGIANV
RYARAFPRDR HRLTP
