ID   SYL_ALBFT               Reviewed;         892 AA.
AC   Q220P5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 99.
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=Rfer_0758;
OS   Albidiferax ferrireducens (strain ATCC BAA-621 / DSM 15236 / T118)
OS   (Rhodoferax ferrireducens).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Rhodoferax.
OX   NCBI_TaxID=338969;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-621 / DSM 15236 / T118;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA   Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of chromosome of Rhodoferax ferrireducens DSM 15236.";
RL   Submitted (FEB-2006) 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; CP000267; ABD68508.1; -; Genomic_DNA.
DR   RefSeq; WP_011463081.1; NC_007908.1.
DR   AlphaFoldDB; Q220P5; -.
DR   SMR; Q220P5; -.
DR   STRING; 338969.Rfer_0758; -.
DR   EnsemblBacteria; ABD68508; ABD68508; Rfer_0758.
DR   KEGG; rfr:Rfer_0758; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_4; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000008332; 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   Gene3D; 3.40.50.620; -; 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   PANTHER; PTHR43740; PTHR43740; 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; SSF47323; 1.
DR   SUPFAM; SSF50677; SSF50677; 1.
DR   TIGRFAMs; TIGR00396; leuS_bact; 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..892
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009408"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT   MOTIF           640..644
FT                   /note="'KMSKS' region"
FT   BINDING         643
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   892 AA;  99291 MW;  1C6F17513F50E8A6 CRC64;
     MQEKYTPLDV EQAAQSHWTA MDAYRVTEDS SKKKFYACSM LPYPSGKLHM GHVRNYTIND
     MLTRYLRMNG YNVLMPMGWD AFGLPAENAA LKNGVPPAQW TFENIAYMKQ QMQAMGLAID
     WSREVATCDP SYYKWNQWLF LKMLDKGIAY RKTQVVNWDP VDQTVLANEQ VIDGKGWRTG
     ATVEKREIPG YYLKITDYAE ELLGQVQTGL PGWPERVKLM QENWIGKSEG VRFAFTHDIR
     DASGALIDDG RMYVFTTRPD TIKGVTFCAV APEHPLALHA ARGNPALAAF IEECKTGGTT
     EAELATQEKK GLDTGLIVTH PLTQLPVAVW VGNYVLMSYG DGAVMGVPAH DERDFAFAKK
     YGLPIKQVVQ VDGEQFDYDQ WQDWYADKQR GVAINSGSFS GMSFKQAVEA VAHKLAALGL
     GEKKTTWRLR DWGVSRQRYW GTPIPIIHCP EHGAVPVPEK DLPVVLPQDC VPDGSGNPLH
     KHEGFHAGVV CPICGVAARR ETDTMDTFVD SSWYFMRYCD PKNEKAMVGE GAAYWMPMDQ
     YIGGIEHAIL HLLYARFWTK VMRDLGLVKV DEPFTKLLTQ GMVLNHIYSR KGENGAKDYF
     WPNDVENVSD ETGKVVAAKL KVAVGNLPAG TLVDYEGIGT MSKSKNNGVD PQDLIERYGA
     DTARLYTMFT APPEATLEWN DAAVEGSYRF LRRVWNFGIK LSTIDMIAVD ESTTGATALN
     DINFSKEAKV LRLEIHTVLK QVDYDYQRMQ YNTVVSGAMK MINALENFKA TDSGGAQVAL
     IEGFGILLRC LYPATPHIAH SLWQGLGYAG TLGDLLDAPW PQVDELALLQ DEVELMLQIN
     GKLRGAIVVS AGASKVEIEL AAIDSEVFRK LANGATPKKV IVVPGRLVNL VV