SYDN1_SYNAS
ID SYDN1_SYNAS Reviewed; 723 AA.
AC Q2LPW5;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Aspartate--tRNA(Asp/Asn) ligase 1 {ECO:0000255|HAMAP-Rule:MF_00044};
DE EC=6.1.1.23 {ECO:0000255|HAMAP-Rule:MF_00044};
DE AltName: Full=Aspartyl-tRNA synthetase 1 {ECO:0000255|HAMAP-Rule:MF_00044};
DE Short=AspRS 1 {ECO:0000255|HAMAP-Rule:MF_00044};
DE AltName: Full=Non-discriminating aspartyl-tRNA synthetase 1 {ECO:0000255|HAMAP-Rule:MF_00044};
DE Short=ND-AspRS 1 {ECO:0000255|HAMAP-Rule:MF_00044};
GN Name=aspS1 {ECO:0000255|HAMAP-Rule:MF_00044};
GN OrderedLocusNames=SYNAS_04480; ORFNames=SYN_02602;
OS Syntrophus aciditrophicus (strain SB).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophales; Syntrophaceae;
OC Syntrophus.
OX NCBI_TaxID=56780;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB;
RX PubMed=17442750; DOI=10.1073/pnas.0610456104;
RA McInerney M.J., Rohlin L., Mouttaki H., Kim U., Krupp R.S.,
RA Rios-Hernandez L., Sieber J., Struchtemeyer C.G., Bhattacharyya A.,
RA Campbell J.W., Gunsalus R.P.;
RT "The genome of Syntrophus aciditrophicus: life at the thermodynamic limit
RT of microbial growth.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:7600-7605(2007).
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; CP000252; ABC76327.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2LPW5; -.
DR SMR; Q2LPW5; -.
DR STRING; 56780.SYN_02602; -.
DR EnsemblBacteria; ABC76327; ABC76327; SYN_02602.
DR KEGG; sat:SYN_02602; -.
DR eggNOG; COG0173; Bacteria.
DR HOGENOM; CLU_014330_3_2_7; -.
DR OMA; DWPLLEW; -.
DR Proteomes; UP000001933; 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..723
FT /note="Aspartate--tRNA(Asp/Asn) ligase 1"
FT /id="PRO_0000235571"
FT REGION 230..233
FT /note="Aspartate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 206
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 252..254
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 252
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 261
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 481
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 516
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 523
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT BINDING 568..571
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT SITE 50
FT /note="Important for tRNA non-discrimination"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
FT SITE 103
FT /note="Important for tRNA non-discrimination"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00044"
SQ SEQUENCE 723 AA; 80508 MW; A62EAFBD7D3303FF CRC64;
MPNRGAHFSI SRRKDFLMDF SERVFCGHLT PDHTGRRVLL AGWVDAFRDH GGLLFIHLRD
RNGIIQIVFS PEAASADVYR QAASLRAEYC VAVQGEVRKR LPGTENPHIE TGDIEVFVSE
LTVLSESEAL PFAISDKAMV AGASSAGADH VNEDLRMQYR YLDIRRPAMQ KNLILRHRIS
QCVREFLDSR GFVEVETPVL TMSTPEGARD YLVPSRIHPR SFYALPQSPQ LFKQLLMIGG
MERYFQLARC FRDEDLRPNR QPEFTQLDIE ASFIDEEFLY ELIEELTVRM FAIGGIALSR
PFPRMTYAEA MDTTGSDRPD LRFGLRMADV TGVFSRTSYS IFKQILQRGG SIKGINIKGQ
SEKLSKNVLQ NEYAKEIAPS FGAKGMTWMR AEEGKLESNI VQFFSADELE ALKRVFQVED
GDVLIMVADP SCAIVNSALG QLRLHLGNRL GLIPEGVFYP VWITEFPLFE PTDEGGVTSS
HHPFTAPDRT DFDPGNIEEL LSLRSRAYDL VVNGEELGGG SIRINDREVQ RRIFAALGLT
EEDVKNKFGF FLRAFDFAAP PHGGLALGMD RVVSMILQTP SIREVIAFPK NRSAACPLTG
APSEVKREQL AELGLLNLGD KDVLPGDAEK EDRIDHLSWV SRIGIAEGER PVMESILAQA
EELAAQVGDL AGNEEPVRSV APVANRVREG LEAVRLSFSG TGRLLKNAPA VKGDYFKVAG
ILD
