ID A0A0K0Y7P4_9RHOB Unreviewed; 617 AA.
AC A0A0K0Y7P4;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Aspartate--tRNA(Asp/Asn) ligase {ECO:0000256|HAMAP-Rule:MF_00044};
DE EC=6.1.1.23 {ECO:0000256|HAMAP-Rule:MF_00044};
DE AltName: Full=Aspartyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00044};
DE Short=AspRS {ECO:0000256|HAMAP-Rule:MF_00044};
DE AltName: Full=Non-discriminating aspartyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00044};
DE Short=ND-AspRS {ECO:0000256|HAMAP-Rule:MF_00044};
GN Name=aspS {ECO:0000256|HAMAP-Rule:MF_00044,
GN ECO:0000313|EMBL:AKS46906.1};
GN ORFNames=OSB_23700 {ECO:0000313|EMBL:AKS46906.1}, SAMN05444287_2030
GN {ECO:0000313|EMBL:SIO23449.1};
OS Octadecabacter temperatus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Octadecabacter.
OX NCBI_TaxID=1458307 {ECO:0000313|EMBL:AKS46906.1, ECO:0000313|Proteomes:UP000067444};
RN [1] {ECO:0000313|EMBL:AKS46906.1, ECO:0000313|Proteomes:UP000067444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB1 {ECO:0000313|EMBL:AKS46906.1,
RC ECO:0000313|Proteomes:UP000067444};
RX PubMed=26358607;
RA Voget S., Billerbeck S., Simon M., Daniel R.;
RT "Closed Genome Sequence of Octadecabacter temperatus SB1, the First
RT Mesophilic Species of the Genus Octadecabacter.";
RL Genome Announc. 3:e01051-15(2015).
RN [2] {ECO:0000313|Proteomes:UP000184809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26878 {ECO:0000313|Proteomes:UP000184809};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:SIO23449.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 26878 {ECO:0000313|EMBL:SIO23449.1};
RA Varghese N., Submissions S.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|HAMAP-
CC Rule:MF_00044};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00044}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00044}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC Type 1 subfamily. {ECO:0000256|ARBA:ARBA00006303, ECO:0000256|HAMAP-
CC Rule:MF_00044}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00044}.
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DR EMBL; CP012160; AKS46906.1; -; Genomic_DNA.
DR EMBL; FSRP01000001; SIO23449.1; -; Genomic_DNA.
DR RefSeq; WP_049835170.1; NZ_FSRP01000001.1.
DR AlphaFoldDB; A0A0K0Y7P4; -.
DR STRING; 1458307.OSB_23700; -.
DR KEGG; otm:OSB_23700; -.
DR PATRIC; fig|1458307.3.peg.2389; -.
DR OrthoDB; 9802326at2; -.
DR Proteomes; UP000067444; Chromosome.
DR Proteomes; UP000184809; Unassembled WGS sequence.
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 CDD; cd04317; EcAspRS_like_N; 1.
DR Gene3D; 3.30.1360.30; GAD-like domain; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 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; IPR047089; Asp-tRNA-ligase_1_N.
DR InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb.
DR InterPro; IPR004115; GAD-like_sf.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004365; NA-bd_OB_tRNA.
DR NCBIfam; TIGR00459; aspS_bact; 1.
DR PANTHER; PTHR22594:SF5; ASPARTATE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR22594; ASPARTYL/LYSYL-TRNA SYNTHETASE; 1.
DR Pfam; PF00152; tRNA-synt_2; 1.
DR Pfam; PF01336; tRNA_anti-codon; 1.
DR PRINTS; PR01042; TRNASYNTHASP.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF55261; GAD domain-like; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_00044};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00044}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00044};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00044};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00044};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00044}; Reference proteome {ECO:0000313|Proteomes:UP000067444}.
FT DOMAIN 142..584
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 199..202
FT /note="Aspartate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
FT BINDING 175
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
FT BINDING 221..223
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
FT BINDING 221
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
FT BINDING 478
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
FT BINDING 511
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
FT BINDING 518
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
FT BINDING 563..566
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
FT SITE 33
FT /note="Important for tRNA non-discrimination"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00044"
SQ SEQUENCE 617 AA; 69624 MW; D23DAD858CB0AEC1 CRC64;
MHAYRSHSCA ELNKDNVGEN VRLSGWVHRI RDHGGLLFID LRDHYGITQV MADPDSPVFK
DIEKVRSEWC IRIDGNVMAR DESLVNDKLP TGEIEVFIRD IEVLGAANEL PLMVFGDQEY
PEDTRLKYRY LDLRREKMQD NMKLRSDVVS SMRKRMWDKG FREFQTPIIT ASSPEGARDF
LVPSRLHPGK FYALPQAPQQ FKQLIMVSGY DKYFQIAPCF RDEDPRADRS PTDFYQLDLE
MSFVEQQDVF DTIQPVITGI FEEFGKGRKV DQTWEQISYR DAALWYGSDK PDLRNPIKMQ
VVSEHFKDSG FAIFAKLLEQ EGTEVRAIPA PTGGGRKFCD RMNVFAQKEG LPGMGYIFWR
KQSADSIAQE RGITVKEVNA LIKSGEIVLG DEAAGPLAKN IGPERTEAIR QQLGLGVGDA
AFFLGGKPKA FESVAGKARQ VIGDELGLTD TNRFAFAWIV DFPIYERDEE TGKVDFEHNP
FSMPQGGMAA LDGDPEDVLG YQYDLACNGY ELVSGAIRNH RPEIMFKAFE IAGYGKDEVE
KRFGGMVNAF QYGAPPHGGC AAGVDRIVML LADADNLRDV IMFPMNQRAE DVMMGAPNLP
MNEQLRELSL RVVPQES
//
