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}; 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
//
