SYDND_CHLTR
ID SYDND_CHLTR Reviewed; 582 AA.
AC O84546;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 138.
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=CT_542;
OS Chlamydia trachomatis (strain D/UW-3/Cx).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=272561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D/UW-3/Cx;
RX PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT trachomatis.";
RL Science 282:754-759(1998).
RN [2]
RP FUNCTION AS A NON-DISCRIMINATING ASPRS, CATALYTIC ACTIVITY, SUBSTRATE
RP SPECIFICITY, AND KINETIC PARAMETERS.
RC STRAIN=D/UW-3/Cx;
RX PubMed=11585842; DOI=10.1074/jbc.m109494200;
RA Raczniak G., Becker H.D., Min B., Soll D.;
RT "A single amidotransferase forms asparaginyl-tRNA and glutaminyl-tRNA in
RT Chlamydia trachomatis.";
RL J. Biol. Chem. 276:45862-45867(2001).
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 ECO:0000269|PubMed:11585842}.
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, ECO:0000269|PubMed:11585842};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.95 uM for tRNA(Asp) {ECO:0000269|PubMed:11585842};
CC KM=2.76 uM for tRNA(Asn) {ECO:0000269|PubMed:11585842};
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; AE001273; AAC68144.1; -; Genomic_DNA.
DR PIR; G71500; G71500.
DR RefSeq; NP_220057.1; NC_000117.1.
DR RefSeq; WP_009871906.1; NC_000117.1.
DR AlphaFoldDB; O84546; -.
DR SMR; O84546; -.
DR STRING; 813.O172_02980; -.
DR EnsemblBacteria; AAC68144; AAC68144; CT_542.
DR GeneID; 884319; -.
DR KEGG; ctr:CT_542; -.
DR PATRIC; fig|272561.5.peg.587; -.
DR HOGENOM; CLU_014330_3_2_0; -.
DR InParanoid; O84546; -.
DR OMA; YQLDVEM; -.
DR SABIO-RK; O84546; -.
DR Proteomes; UP000000431; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006422; P:aspartyl-tRNA aminoacylation; IBA:GO_Central.
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 1: Evidence at protein level;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..582
FT /note="Aspartate--tRNA(Asp/Asn) ligase"
FT /id="PRO_0000110856"
FT REGION 201..204
FT /note="Aspartate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 177
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 223..225
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 223
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 232
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 447
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 481
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 488
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 533..536
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT SITE 32
FT /note="Important for tRNA non-discrimination"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT SITE 84
FT /note="Important for tRNA non-discrimination"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
SQ SEQUENCE 582 AA; 66227 MW; E8D2EBB2785EFABA CRC64;
MKYRTHKCNE LSLDHVGEHV RLSGWVHRYR NHGGVVFIDL RDCFGITQIV CRQEENPELH
QLMDQVRSEW VLCVEGLVCA RLEGMENPNL VTGSIEVEVS SLEVLSRAQN LPFSISDEHI
NVNEELRLTY RYLDMRRGDI LDRLMCRHKV MLACRQYLDE QGFTEVVTPI LGKSTPEGAR
DYLVPSRIYP GNFYALPQSP QLFKQILMVG GLDRYFQIAT CFRDEDLRAD RQPEFTQIDM
EMSFGGPEDL FPVVEELVAR LFAVKGIELK APFLRMTYQE AKDSYGTDKP DLRFGLRLKN
CCEYARKFTF SIFLDQLAYG GTVKGFCVPG GADMSRKQLD IYTDFVKRYG AMGLVWIKKQ
DGGVSSNVAK FASEDVFQEM FEAFEAKDQD ILLLIAAPEA VANQALDHLR RLIARERQLY
DSTQYNFVWI TDFPLFAKEE GELCPEHHPF TAPLDEDISL LDSDPFAVRS SSYDLVLNGY
EIASGSQRIH NPDLQNKIFA LLKLSQESVK EKFGFFIDAL SFGTPPHLGI ALGLDRIMMV
LTGAETIREV IAFPKTQKAG DLMMSAPSEI LPIQLKELGL KL
