ID C4LCB2_TOLAT Unreviewed; 861 AA. AC C4LCB2; DT 07-JUL-2009, integrated into UniProtKB/TrEMBL. DT 07-JUL-2009, sequence version 1. DT 18-JUN-2025, entry version 103. DE RecName: Full=Leucine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00049}; DE EC=6.1.1.4 {ECO:0000256|HAMAP-Rule:MF_00049}; DE AltName: Full=Leucyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00049}; DE Short=LeuRS {ECO:0000256|HAMAP-Rule:MF_00049}; GN Name=leuS {ECO:0000256|HAMAP-Rule:MF_00049}; GN OrderedLocusNames=Tola_2823 {ECO:0000313|EMBL:ACQ94416.1}; OS Tolumonas auensis (strain DSM 9187 / NBRC 110442 / TA 4). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Aeromonadales; Aeromonadaceae; Tolumonas. OX NCBI_TaxID=595494 {ECO:0000313|EMBL:ACQ94416.1, ECO:0000313|Proteomes:UP000009073}; RN [1] {ECO:0000313|Proteomes:UP000009073} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 9187 / TA4 {ECO:0000313|Proteomes:UP000009073}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D., RA Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C., RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Spring S., RA Beller H.; RT "Complete sequence of Tolumonas auensis DSM 9187."; RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ACQ94416.1, ECO:0000313|Proteomes:UP000009073} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 9187 / TA4 {ECO:0000313|Proteomes:UP000009073}; RX PubMed=22180815; DOI=10.4056/sigs.2184986; RA Chertkov O., Copeland A., Lucas S., Lapidus A., Berry K.W., Detter J.C., RA Del Rio T.G., Hammon N., Dalin E., Tice H., Pitluck S., Richardson P., RA Bruce D., Goodwin L., Han C., Tapia R., Saunders E., Schmutz J., RA Brettin T., Larimer F., Land M., Hauser L., Spring S., Rohde M., RA Kyrpides N.C., Ivanova N., Goker M., Beller H.R., Klenk H.P., Woyke T.; RT "Complete genome sequence of Tolumonas auensis type strain (TA 4)."; RL Stand. Genomic Sci. 5:112-120(2011). CC -!- CATALYTIC ACTIVITY: CC Reaction=tRNA(Leu) + L-leucine + ATP = L-leucyl-tRNA(Leu) + AMP + CC diphosphate; 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:0000256|ARBA:ARBA00047469, ECO:0000256|HAMAP- CC Rule:MF_00049}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00049}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|HAMAP-Rule:MF_00049, CC ECO:0000256|RuleBase:RU363035}. 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; CP001616; ACQ94416.1; -; Genomic_DNA. DR AlphaFoldDB; C4LCB2; -. DR STRING; 595494.Tola_2823; -. DR KEGG; tau:Tola_2823; -. DR eggNOG; COG0495; Bacteria. DR HOGENOM; CLU_004427_0_0_6; -. DR Proteomes; UP000009073; Chromosome. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0002161; F:aminoacyl-tRNA deacylase 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 FunFam; 1.10.730.10:FF:000002; Leucine--tRNA ligase; 1. DR FunFam; 2.20.28.290:FF:000001; Leucine--tRNA ligase; 1. DR FunFam; 3.10.20.590:FF:000001; Leucine--tRNA ligase; 1. DR FunFam; 3.40.50.620:FF:000003; Leucine--tRNA ligase; 1. DR FunFam; 3.40.50.620:FF:000124; Leucine--tRNA ligase; 1. DR FunFam; 3.90.740.10:FF:000012; Leucine--tRNA ligase; 1. DR Gene3D; 2.20.28.290; -; 1. DR Gene3D; 3.10.20.590; -; 1. DR Gene3D; 3.40.50.620; HUPs; 2. DR Gene3D; 1.10.730.10; Isoleucyl-tRNA Synthetase, Domain 1; 1. DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1. 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 {ECO:0000256|ARBA:ARBA00023146, KW ECO:0000256|HAMAP-Rule:MF_00049}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_00049}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00049}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00049}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00049}; KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP- KW Rule:MF_00049}; Reference proteome {ECO:0000313|Proteomes:UP000009073}. FT DOMAIN 42..183 FT /note="Methionyl/Leucyl tRNA synthetase" FT /evidence="ECO:0000259|Pfam:PF09334" FT DOMAIN 224..406 FT /note="Leucyl-tRNA synthetase editing" FT /evidence="ECO:0000259|Pfam:PF13603" FT DOMAIN 420..575 FT /note="Aminoacyl-tRNA synthetase class Ia" FT /evidence="ECO:0000259|Pfam:PF00133" FT DOMAIN 620..654 FT /note="Aminoacyl-tRNA synthetase class Ia" FT /evidence="ECO:0000259|Pfam:PF00133" FT DOMAIN 701..824 FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase FT anticodon-binding" FT /evidence="ECO:0000259|Pfam:PF08264" FT MOTIF 45..55 FT /note="'HIGH' region" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049" FT MOTIF 621..625 FT /note="'KMSKS' region" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049" FT BINDING 624 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049" SQ SEQUENCE 861 AA; 97335 MW; 7182C3BC2D0B2E61 CRC64; MSVMQEQYNP QSLEPEVQRH WDKQQTFKAF EKVDKEKFYC LSMFPYPSGR LHMGHVRNYT IGDVISRYQR LNGKNVLQPI GWDAFGLPAE NAAIKNNSAP AKWTYENIEY MKGQLKMLGL SYDWDRELAT CTPQYYRWEQ WFFTELYKKG LVYKKTSSVN WCPNDQTVLA NEQVQDGCCW RCDTPVEQKE IPQWFVKITA YAEELLTDLD KLDGWPEMVK TMQRNWIGRS EGLTMTFHVE NSEQSFDIYT TRPDTLMGVT YVAVAAAHPL AKQAAENNAA LADFLEECKN TKVAEAELAT MEKKGMATGL YALHPLDGRR VPIMVANFVL MDYGTGAVMA VPAHDQRDFE FAHKYGLEIR AVIAAEDGSA PDISAAAYTE KGVLFNSGEF DGLDFKQAFD AICTKLESQG LGKRTVNFRL RDWGVSRQRY WGAPIPMLTL EDGTVVPAPA DQLPVILPED VVMDGVQSPI KADPEWAKTT YNGQPALRET DTFDTFMESS WYFARYCCPD YEQGMLDTDR ANHWLPVDQY IGGIEHACMH LLYARFFHKL LRDSGMVKSD EPFTRLLCQG MVLADAFYYT EHGARVWVSP TDVKVERDEK GRIIKAVDNE GREVIHAGMT KMSKSKNNGI DPQLMVERYG ADTVRLFMMF ASPADMTLEW QESGVDGAQR FLKRLWKAVA EHTAKGAAPE LDVASLSNEQ KTLRRELHKT IAKFSDDIGR RQTFNTAIAA VMELMNRVAK APQESDQDRA LVQEVLTNVV LMLYPITPHV CFHLWQALGN ADIDQAAWPV ADAAAMVEDE KLVVVQVNGK VRGKLTVAAD ATQEQVQALA MQDHTVAKFT ADLTVRKVIY VPGKLLNIVV G //