ID   SYL1_RHIJ3              Reviewed;         838 AA.
AC   Q1MFI6;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   27-MAR-2024, entry version 108.
DE   RecName: Full=Leucine--tRNA ligase 1 {ECO:0000255|HAMAP-Rule:MF_00049};
DE            EC=6.1.1.4 {ECO:0000255|HAMAP-Rule:MF_00049};
DE   AltName: Full=Leucyl-tRNA synthetase 1 {ECO:0000255|HAMAP-Rule:MF_00049};
DE            Short=LeuRS 1 {ECO:0000255|HAMAP-Rule:MF_00049};
GN   Name=leuS1 {ECO:0000255|HAMAP-Rule:MF_00049};
GN   OrderedLocusNames=RL2798;
OS   Rhizobium johnstonii (strain DSM 114642 / LMG 32736 / 3841) (Rhizobium
OS   leguminosarum bv. viciae).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium;
OC   Rhizobium johnstonii.
OX   NCBI_TaxID=216596;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 114642 / LMG 32736 / 3841;
RX   PubMed=16640791; DOI=10.1186/gb-2006-7-4-r34;
RA   Young J.P.W., Crossman L.C., Johnston A.W.B., Thomson N.R., Ghazoui Z.F.,
RA   Hull K.H., Wexler M., Curson A.R.J., Todd J.D., Poole P.S., Mauchline T.H.,
RA   East A.K., Quail M.A., Churcher C., Arrowsmith C., Cherevach I.,
RA   Chillingworth T., Clarke K., Cronin A., Davis P., Fraser A., Hance Z.,
RA   Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA   Rabbinowitsch E., Sanders M., Simmonds M., Whitehead S., Parkhill J.;
RT   "The genome of Rhizobium leguminosarum has recognizable core and accessory
RT   components.";
RL   Genome Biol. 7:R34.1-R34.20(2006).
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; AM236080; CAK08288.1; -; Genomic_DNA.
DR   RefSeq; WP_011652325.1; NC_008380.1.
DR   AlphaFoldDB; Q1MFI6; -.
DR   SMR; Q1MFI6; -.
DR   EnsemblBacteria; CAK08288; CAK08288; RL2798.
DR   KEGG; rle:RL2798; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_5; -.
DR   Proteomes; UP000006575; 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; 3.40.50.620; 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.
FT   CHAIN           1..838
FT                   /note="Leucine--tRNA ligase 1"
FT                   /id="PRO_0000334802"
FT   MOTIF           40..51
FT                   /note="'HIGH' region"
FT   MOTIF           608..612
FT                   /note="'KMSKS' region"
FT   BINDING         611
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   838 AA;  94069 MW;  7C2AC9CEACE16F9F CRC64;
     MPYDPTKIEP KWQAYWAGHH IFRVEIDPAR PKFYALDMFP YPSGAGLHVG HPLGYTATDI
     MCRYKRMRGF NVLHPMGWDS FGLPAERHAM RTGVHPDITT KRNIETFRGQ VQRLGFSYDW
     SREFATTDPA YVRWTQWIFL KLFENGLAYQ AEVAVNWCPA QNAVLADEEV KDGRYVETGD
     PVIRRRMRQW MLRITAYADR LLQGLDGLDW PENLKAMQRN WIGRSEGAEI RFPLEHGKGV
     ITVFTTRPET LFGASYILLA PEHPAVAAIV EPEMSEAVAA YIAEAEGLEE TVRADAGREK
     TGVFTGAYAI NPANGARLPV WVADYVLAGY GTGALMAVPA HDARDYAFAH SHELPIIRVI
     DSEADIEKGA YEGEGAMVNS GFLSGLGSPE ARSAIVAWLQ ANGTGWPKVM YRLRDWLFSR
     QRYWGEPIPV LHLADGSVMP LPEECLPLLP PELDDYAPTP DGEPPLARAQ AWVETIVPGT
     DIPARRETNT MPQWAGSCWY YLRFLDPENT SEPVGREAER YWMPVDLYVG GAEHAVLHLL
     YARFWHKVLY DIGVVSTEEP FQRLFNQGMI LAHSYRDAAG RYYAPSSVVE EEGRWFAGSV
     EVQRAVEKMS KSQLNVVNPD DVVHQFGADA LRLYEMFMGP LDAAKPWQTA GVIGVRRFLE
     RAWRIVCDES DGLSPVVLEA APSPQLLRLR HQTVKTVTAD IEAIRFNTAV SRLMELANAL
     TAEAARPREV VETFVLLLAP FAPHIAEELW SKLGHGETLT WVSWPTFDPA LIEMETREYV
     VQINGKVRHR FEAAADLGEA LLAAARSEPS VMALLDGKTV VKEVLVPGRL VNFVVEDL
//