SYD_HAEI8
ID SYD_HAEI8 Reviewed; 588 AA.
AC Q4QNM1;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Aspartate--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00044};
DE EC=6.1.1.12 {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};
GN Name=aspS {ECO:0000255|HAMAP-Rule:MF_00044}; OrderedLocusNames=NTHI0435;
OS Haemophilus influenzae (strain 86-028NP).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=281310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=86-028NP;
RX PubMed=15968074; DOI=10.1128/jb.187.13.4627-4636.2005;
RA Harrison A., Dyer D.W., Gillaspy A., Ray W.C., Mungur R., Carson M.B.,
RA Zhong H., Gipson J., Gipson M., Johnson L.S., Lewis L., Bakaletz L.O.,
RA Munson R.S. Jr.;
RT "Genomic sequence of an otitis media isolate of nontypeable Haemophilus
RT influenzae: comparative study with H. influenzae serotype d, strain KW20.";
RL J. Bacteriol. 187:4627-4636(2005).
CC -!- FUNCTION: Catalyzes the attachment of L-aspartate to tRNA(Asp) in a
CC two-step reaction: L-aspartate is first activated by ATP to form Asp-
CC AMP and then transferred to the acceptor end of tRNA(Asp).
CC {ECO:0000255|HAMAP-Rule:MF_00044}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-
CC aspartyl-tRNA(Asp); Xref=Rhea:RHEA:19649, Rhea:RHEA-COMP:9660,
CC Rhea:RHEA-COMP:9678, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78516,
CC ChEBI:CHEBI:456215; EC=6.1.1.12; 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; CP000057; AAX87376.1; -; Genomic_DNA.
DR RefSeq; WP_011271986.1; NC_007146.2.
DR AlphaFoldDB; Q4QNM1; -.
DR SMR; Q4QNM1; -.
DR EnsemblBacteria; AAX87376; AAX87376; NTHI0435.
DR KEGG; hit:NTHI0435; -.
DR HOGENOM; CLU_014330_3_2_6; -.
DR OMA; YQLDVEM; -.
DR OrthoDB; 226836at2; -.
DR Proteomes; UP000002525; 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: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..588
FT /note="Aspartate--tRNA ligase"
FT /id="PRO_0000110881"
FT REGION 196..199
FT /note="Aspartate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 172
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 218..220
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 218
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 227
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 449
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"
SQ SEQUENCE 588 AA; 66714 MW; 4CAC2AC00B0A0200 CRC64;
MMRTHYCGAL NRNNIGQDVT LSGWVHRRRD LGGLIFIDMR DRDGIVQVCF DPKYQDALTA
AAGLRNEFCI QIKGEVIARP ENQINKNMAT GEVEVLAKEL RIYNASDVLP LDFNQNNTEE
QRLKYRYLDL RRPEMAQRLK TRAKITSFVR RFMDDNGFLD IETPMLTKAT PEGARDYLVP
SRVHKGKFYA LPQSPQLFKQ LLMMSGFDRY YQIVKCFRDE DLRADRQPEF TQIDVETSFL
TAPEVREIME RMVHDLWLDT IGVDLGKFPV MTWQEAMRRF GSDKPDLRNP LEMVDVADIV
KDVEFKVFNE PANNPNGRVA VIRVPNGAEI TRKQIDEYTQ FVGIYGAKGL AWAKVNDINA
GLEGVQSPIA KFLNEEVWKA LAERVNAQTG DILFFGADKW QTTTDAMGAL RLKLGCDLGL
TRLDEWQPLW VIDFPMFERD EEGNLAAMHH PFTSPKDFSP EQLEADPTSA VANAYDMVIN
GYEVGGGSVR IFDPKMQQTV FRILGIDEEQ QREKFGFLLD ALKFGTPPHA GLAFGLDRLT
MLLTGTENIR DVIAFPKTTA AACLMTEAPS FVNPQALEEL AISVVKAE
