SYDND_HELMI
ID SYDND_HELMI Reviewed; 605 AA.
AC B0TF89;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=Helmi_17810;
GN ORFNames=HM1_1848;
OS Heliobacterium modesticaldum (strain ATCC 51547 / Ice1).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Heliobacteriaceae;
OC Heliomicrobium.
OX NCBI_TaxID=498761;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51547 / Ice1;
RX PubMed=18441057; DOI=10.1128/jb.00299-08;
RA Sattley W.M., Madigan M.T., Swingley W.D., Cheung P.C., Clocksin K.M.,
RA Conrad A.L., Dejesa L.C., Honchak B.M., Jung D.O., Karbach L.E.,
RA Kurdoglu A., Lahiri S., Mastrian S.D., Page L.E., Taylor H.L., Wang Z.T.,
RA Raymond J., Chen M., Blankenship R.E., Touchman J.W.;
RT "The genome of Heliobacterium modesticaldum, a phototrophic representative
RT of the Firmicutes containing the simplest photosynthetic apparatus.";
RL J. Bacteriol. 190:4687-4696(2008).
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; CP000930; ABZ84406.1; -; Genomic_DNA.
DR AlphaFoldDB; B0TF89; -.
DR SMR; B0TF89; -.
DR STRING; 498761.HM1_1848; -.
DR EnsemblBacteria; ABZ84406; ABZ84406; HM1_1848.
DR KEGG; hmo:HM1_1848; -.
DR eggNOG; COG0173; Bacteria.
DR HOGENOM; CLU_014330_3_2_9; -.
DR OMA; YQLDVEM; -.
DR Proteomes; UP000008550; 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..605
FT /note="Aspartate--tRNA(Asp/Asn) ligase"
FT /id="PRO_1000198994"
FT REGION 207..210
FT /note="Aspartate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 183
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 229..231
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 229
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 238
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 456
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 490
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 497
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 542..545
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT SITE 39
FT /note="Important for tRNA non-discrimination"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT SITE 91
FT /note="Important for tRNA non-discrimination"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
SQ SEQUENCE 605 AA; 68460 MW; 17CD816C531916C8 CRC64;
MMIDMFTGLK RSHRGGDLRI DHAGQTVTLM GWVQRRRDHG GLIFVDLRDR SGLVQVVFSP
EVGKEAFTKA EDVRNEYVLA VTGDVRPRPE GTVNANLPSG QIDVYARQLW VLNSAKTPPF
YIEDGVDVDE TVRLKYRYLD LRRPEMQRNL IIRHKTAKAM RDFLDRNGFL EIETPMLTKS
TPEGAREFMV PSRIHPGEFF VLPQSPQLYK QILMVAGMER YFQIVRCFRD EDLRADRQPE
FTQLDIEMSF TQMDDLLTLM EEMVAHIFKE ALGKEISTPF RRIPYAEAMG RFGSDKPDLR
FGLELIDLTE TVKDVEFKVF ASVVKGGGEV KAINAKGCAH FSRKEIDDLT KGVAVYGAKG
LAYIQMTEEG PKSPIAKFFT DEQLNAVLDR LGAEKGDLLL FVADKPSVVA ASLGFLRQEL
ARRLNLIDSE KLEFAWVVDF PLVEYDPEEK RYNAIHHPFT APKDEDLDLL DKEPGKVRAK
AYDLVLNGVE LGGGSLRIYR RDIQEKMFAI LGLTAEEAYQ KFGFLLDAFD YGTPPHGGIA
FGLDRMIMLM TGRDTIRDVI AFPKTQSASD MMVDAPSAVT PRQLKELHIK LDLPVKAPKA
EPAKK
