ID SYL_HYPNA Reviewed; 855 AA. AC Q0BWB5; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 1. DT 27-MAR-2024, entry version 124. DE RecName: Full=Leucine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00049}; DE EC=6.1.1.4 {ECO:0000255|HAMAP-Rule:MF_00049}; DE AltName: Full=Leucyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00049}; DE Short=LeuRS {ECO:0000255|HAMAP-Rule:MF_00049}; GN Name=leuS {ECO:0000255|HAMAP-Rule:MF_00049}; GN OrderedLocusNames=HNE_3557; OS Hyphomonas neptunium (strain ATCC 15444). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomonadales; OC Hyphomonadaceae; Hyphomonas. OX NCBI_TaxID=228405; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15444; RX PubMed=16980487; DOI=10.1128/jb.00111-06; RA Badger J.H., Hoover T.R., Brun Y.V., Weiner R.M., Laub M.T., Alexandre G., RA Mrazek J., Ren Q., Paulsen I.T., Nelson K.E., Khouri H.M., Radune D., RA Sosa J., Dodson R.J., Sullivan S.A., Rosovitz M.J., Madupu R., RA Brinkac L.M., Durkin A.S., Daugherty S.C., Kothari S.P., Giglio M.G., RA Zhou L., Haft D.H., Selengut J.D., Davidsen T.M., Yang Q., Zafar N., RA Ward N.L.; RT "Comparative genomic evidence for a close relationship between the RT dimorphic prosthecate bacteria Hyphomonas neptunium and Caulobacter RT crescentus."; RL J. Bacteriol. 188:6841-6850(2006). CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl- CC tRNA(Leu); Xref=Rhea:RHEA:11688, Rhea:RHEA-COMP:9613, Rhea:RHEA- CC COMP:9622, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57427, CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78494, ChEBI:CHEBI:456215; EC=6.1.1.4; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00049}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00049}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. CC {ECO:0000255|HAMAP-Rule:MF_00049}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000158; ABI77585.1; -; Genomic_DNA. DR RefSeq; WP_011648522.1; NC_008358.1. DR AlphaFoldDB; Q0BWB5; -. DR SMR; Q0BWB5; -. DR STRING; 228405.HNE_3557; -. DR KEGG; hne:HNE_3557; -. DR eggNOG; COG0495; Bacteria. DR HOGENOM; CLU_004427_0_0_5; -. DR Proteomes; UP000001959; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004823; F:leucine-tRNA ligase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006429; P:leucyl-tRNA aminoacylation; IEA:UniProtKB-UniRule. DR CDD; cd07958; Anticodon_Ia_Leu_BEm; 1. DR CDD; cd00812; LeuRS_core; 1. DR Gene3D; 2.20.28.290; -; 1. DR Gene3D; 3.10.20.590; -; 1. DR Gene3D; 3.40.50.620; HUPs; 2. DR HAMAP; MF_00049_B; Leu_tRNA_synth_B; 1. DR InterPro; IPR001412; aa-tRNA-synth_I_CS. DR InterPro; IPR002300; aa-tRNA-synth_Ia. DR InterPro; IPR002302; Leu-tRNA-ligase. DR InterPro; IPR025709; Leu_tRNA-synth_edit. DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd. DR InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd. DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit. DR NCBIfam; TIGR00396; leuS_bact; 1. DR PANTHER; PTHR43740:SF2; LEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1. DR PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 1. DR Pfam; PF08264; Anticodon_1; 1. DR Pfam; PF00133; tRNA-synt_1; 2. DR Pfam; PF13603; tRNA-synt_1_2; 1. DR Pfam; PF09334; tRNA-synt_1g; 1. DR PRINTS; PR00985; TRNASYNTHLEU. DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1. DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1. DR SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 1. DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; KW Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1..855 FT /note="Leucine--tRNA ligase" FT /id="PRO_0000334764" FT MOTIF 45..55 FT /note="'HIGH' region" FT MOTIF 619..623 FT /note="'KMSKS' region" FT BINDING 622 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049" SQ SEQUENCE 855 AA; 94333 MW; 40A93E3F4848CAFA CRC64; MATRYDPQSA EPRWRDAWEK ADIFRTKAPK DAPGAPKAFV LEMFPYPSGR LHMGHVRNYA MGDVVARHKR AKGYNVLHPM GWDAFGMPAE NAAMERKVHP GKWTYANIES MKAQFRKLGL SLDWSREFAT CDPDYYGAQQ ALFLKLMDKG LVYRKASKVN WDPVDNTVLA NEQVIDGRGW RSGAPVEQRE LTQWFFKITA YADDLLEAVQ KLERWPEKVR TMQANWIGRS EGLEMTFAFD GERPAGFEDG ISVFTTRPDT LFGASFVALS PDHPLTLQLA EKSDALQAFR AKCAQIGTSE EAIEKAEKLG FDTGLTVAHP FEPGRTVPVW VANFVLMGYG TGAIFGCPAH DQRDLDFARK FGLDVFPVVL PPGADAAAFE VGIEAYTGPG HIYKSGFLDG LSIDDAKRAA IAKIEAAGQG EGKVNYRLRD WGVSRQRYWG CPIPVVHCED CGVVGVPAAD LPVRLPEDVT FDVPGNPLDR HPDWKHVDCP KCGKPARRET DTLDTFVDSS WYYARFASVS DPEERAYWLP VDQYIGGVEH AVLHLLYSRF FSRAMRDVGE LDLPSGEPFA GLFTQGMVTH ETYRSEGGTW LEPSAVERKD GQVFEIATGK PVKVGAIEKM SKSKKNTVDP DAIVATYGAD VARWFVLSDS PPERDVEWTQ SGAEGAARFV QRVWSFVDSL PETGPFPAPG SDDVSTALRK SNHKAVAAID RAIEEFRFNS AIATIHEWVN ALKKTESDPA TLGARAEGAD MLARCLVPFM PHLAEACWER LGQTSLVSQA MWPKIDASLV VDDTVTLAVQ VNGKRRAEIT VAKDMAPDAV EAAAKALPDV ASFIAGKSVK KTIVVPGRIV NIVVA //