ID   SYL_HERAR               Reviewed;         881 AA.
AC   A4G8E6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 101.
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=HEAR2661;
OS   Herminiimonas arsenicoxydans.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Herminiimonas.
OX   NCBI_TaxID=204773;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ULPAs1;
RX   PubMed=17432936; DOI=10.1371/journal.pgen.0030053;
RA   Muller D., Medigue C., Koechler S., Barbe V., Barakat M., Talla E.,
RA   Bonnefoy V., Krin E., Arsene-Ploetze F., Carapito C., Chandler M.,
RA   Cournoyer B., Cruveiller S., Dossat C., Duval S., Heymann M., Leize E.,
RA   Lieutaud A., Lievremont D., Makita Y., Mangenot S., Nitschke W., Ortet P.,
RA   Perdrial N., Schoepp B., Siguier P., Simeonova D.D., Rouy Z., Segurens B.,
RA   Turlin E., Vallenet D., van Dorsselaer A., Weiss S., Weissenbach J.,
RA   Lett M.-C., Danchin A., Bertin P.N.;
RT   "A tale of two oxidation states: bacterial colonization of arsenic-rich
RT   environments.";
RL   PLoS Genet. 3:518-530(2007).
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; CU207211; CAL62783.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4G8E6; -.
DR   SMR; A4G8E6; -.
DR   STRING; 204773.HEAR2661; -.
DR   KEGG; har:HEAR2661; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_4; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000006697; 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   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..881
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009353"
FT   MOTIF           48..58
FT                   /note="'HIGH' region"
FT   MOTIF           638..642
FT                   /note="'KMSKS' region"
FT   BINDING         641
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   881 AA;  99183 MW;  643783A2A205F7A7 CRC64;
     MQDKYSPADV EKSAHDHWQA TDAYKAVEHA KDKNGKDKKK FYACSMLPYP SGKLHMGHVR
     NYTINDVMYR YLRMNGYNVL MPMGWDAFGM PAENAAMANN VPPAQWTYAN IEHMKTQMAS
     MGLAIDWSRE MTACKPEYYK WNQWMFLKML EKGIIYKKTG SVNWDPIDQT VLANEQVIDG
     RGWRSGALIE KREIPMYYAR ITDYAEELLD HVEHKLPGWP ERVRTMQANW IGKSTGVRFA
     FTHDIKDDDK LINDGKLWVF TTRADTIKGV TFCAVAAEHP LATFAAKSNP ELAEFIAECK
     LGSVIEADMA TMEKKGMPTG LFVKHPLTGS LVEVWVGNYV LITYGDGAVM GVPAHDERDF
     AFAQKYVLPI HQVIDVEGKT FSEVTWHDWY ADKENGRCIN SGKYDGLNYQ QAVNTIAADL
     EELGLGEKKI TYRLRDWGIS RQRYWGTPIP MINCADCGAV PVPEKDLPVV LPEDCVPDGS
     GNPLNKHEAF LKCDCPKCGK PARRETDTMD TFVDSSWYYM RYCSPNSNDA MVDSRNDYWM
     PMDQYIGGIE HAVLHLLYAR FWTKVMRDFG LVKFDEPFTN LLTQGMVLNE TYYREDASGK
     KTWFNPADVQ LELDDKGRPV SAILNNDRQP VEIGGTEKMS KSKNNGIDPQ AQIDQYGADT
     ARLFTMFASP PEQTLEWSGA GVEGANRFLR RVWTYAYNQS ARIAAATASD FSKLSDAQKT
     LRREVHKILQ QADNDYKRIQ YNTVVSAGMK MLNTLEGAKL DESAASNAVI AEGLSIFLRI
     LNPVAPHITH VLWQELGFAK VHGDILDAAW PQVDAGALEQ AEIEMMIQVN GKLRGSIVVA
     KDADKATIEA TALANEAVRK FIEGTPKKII VVPGKLVNIV A
//