ID SYL_ALKOO Reviewed; 802 AA.
AC A8MJY6;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 1.
DT 27-MAR-2024, entry version 88.
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}; OrderedLocusNames=Clos_2587;
OS Alkaliphilus oremlandii (strain OhILAs) (Clostridium oremlandii (strain
OS OhILAs)).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Alkaliphilus.
OX NCBI_TaxID=350688;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OhILAs;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Stolz J.F., Dawson A., Fisher E.,
RA Crable B., Perera E., Lisak J., Ranganathan M., Basu P., Richardson P.;
RT "Complete genome of Alkaliphilus oremlandii OhILAs.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP000853; ABW20118.1; -; Genomic_DNA.
DR AlphaFoldDB; A8MJY6; -.
DR SMR; A8MJY6; -.
DR STRING; 350688.Clos_2587; -.
DR KEGG; aoe:Clos_2587; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_9; -.
DR Proteomes; UP000000269; 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; 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; 1.
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..802
FT /note="Leucine--tRNA ligase"
FT /id="PRO_1000057340"
FT MOTIF 41..52
FT /note="'HIGH' region"
FT MOTIF 580..584
FT /note="'KMSKS' region"
FT BINDING 583
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 802 AA; 92499 MW; 96F021E311FB5EC5 CRC64;
MKQYNPKEIE SKWQNIWEER GVFHASNDKD KEKFYALIEF PYPSGQGLHV GHPRPYTALD
VVSRKRRLEG YNVLYPMGWD AFGLPTENYA IKNKIHPKVV TEQNVARFKK QLQGLGMSFD
WSREINTTDP EYYKWTQWIF LKLFEKGLAY KKEMSINWCT SCKVGLANEE VVNGGCERCG
AEVVRKQKNQ WMLKITEYAE RLINDLDLVD YIERVKIQQK NWIGKSEGME VDFEITGGKK
ITVYTTRPDT LFGSTYMVIS PEHPYIEELA AHIQNMDDLV HYREEAAKKS EFERTELVKD
KTGVKIEGIE ATNPATGKQI PIFISDYVMM SYGTGAIMAV PGHDTRDWEF AKKFNLPIVE
VVSGGNVDEA AYTDTEEGII VNSDFINGMQ VKEAKEKISS WLEEKGLGKR KVNYKLRDWV
FSRQRYWGEP IPLVHCDCCG WVPVPESQLP VLLPEVESYE PTDNGESPLA NLRDWVETTC
PKCGGKAERE TDTMPQWAGS SWYFLRYTDP HNNEELASKE NLDYWMPIDW YNGGMEHTTL
HLLYSRFWHK FLYDCGVVPS CEPYQKRTSH GMILGENNEK MSKSRGNVIN PDDIVTEFGA
DTLRLYEMFI GDFEKSVPWS QNGVKGCRRF LDRIWKLQEI LVDSQEMTKE LEGNIHKTIK
KVTEDYETLK FNTAVASMMA LINDFYDHGT VTKGDMKTLL TLLNPVAPHI TEELWEVLGF
EGHIYGTTWP IWDEAKTIDS VVEIPIQING KVKGQMVISV DFTADQVKEQ FRNDERLMAL
VEGKSIVKEI YVPGKIYNIV VK
//
