ID   SYL_HYPNA               Reviewed;         855 AA.
AC   Q0BWB5;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 117.
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=HNE_3557;
OS   Hyphomonas neptunium (strain ATCC 15444).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomonadales;
OC   Hyphomonadaceae; Hyphomonas.
OX   NCBI_TaxID=228405;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15444;
RX   PubMed=16980487; DOI=10.1128/jb.00111-06;
RA   Badger J.H., Hoover T.R., Brun Y.V., Weiner R.M., Laub M.T., Alexandre G.,
RA   Mrazek J., Ren Q., Paulsen I.T., Nelson K.E., Khouri H.M., Radune D.,
RA   Sosa J., Dodson R.J., Sullivan S.A., Rosovitz M.J., Madupu R.,
RA   Brinkac L.M., Durkin A.S., Daugherty S.C., Kothari S.P., Giglio M.G.,
RA   Zhou L., Haft D.H., Selengut J.D., Davidsen T.M., Yang Q., Zafar N.,
RA   Ward N.L.;
RT   "Comparative genomic evidence for a close relationship between the
RT   dimorphic prosthecate bacteria Hyphomonas neptunium and Caulobacter
RT   crescentus.";
RL   J. Bacteriol. 188:6841-6850(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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000158; ABI77585.1; -; Genomic_DNA.
DR   RefSeq; WP_011648522.1; NC_008358.1.
DR   AlphaFoldDB; Q0BWB5; -.
DR   SMR; Q0BWB5; -.
DR   STRING; 228405.HNE_3557; -.
DR   PRIDE; Q0BWB5; -.
DR   EnsemblBacteria; ABI77585; ABI77585; HNE_3557.
DR   KEGG; hne:HNE_3557; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_5; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000001959; 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; 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; 3.
DR   Pfam; PF13603; tRNA-synt_1_2; 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..855
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000334764"
FT   MOTIF           45..55
FT                   /note="'HIGH' region"
FT   MOTIF           619..623
FT                   /note="'KMSKS' region"
FT   BINDING         622
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   855 AA;  94333 MW;  40A93E3F4848CAFA CRC64;
     MATRYDPQSA EPRWRDAWEK ADIFRTKAPK DAPGAPKAFV LEMFPYPSGR LHMGHVRNYA
     MGDVVARHKR AKGYNVLHPM GWDAFGMPAE NAAMERKVHP GKWTYANIES MKAQFRKLGL
     SLDWSREFAT CDPDYYGAQQ ALFLKLMDKG LVYRKASKVN WDPVDNTVLA NEQVIDGRGW
     RSGAPVEQRE LTQWFFKITA YADDLLEAVQ KLERWPEKVR TMQANWIGRS EGLEMTFAFD
     GERPAGFEDG ISVFTTRPDT LFGASFVALS PDHPLTLQLA EKSDALQAFR AKCAQIGTSE
     EAIEKAEKLG FDTGLTVAHP FEPGRTVPVW VANFVLMGYG TGAIFGCPAH DQRDLDFARK
     FGLDVFPVVL PPGADAAAFE VGIEAYTGPG HIYKSGFLDG LSIDDAKRAA IAKIEAAGQG
     EGKVNYRLRD WGVSRQRYWG CPIPVVHCED CGVVGVPAAD LPVRLPEDVT FDVPGNPLDR
     HPDWKHVDCP KCGKPARRET DTLDTFVDSS WYYARFASVS DPEERAYWLP VDQYIGGVEH
     AVLHLLYSRF FSRAMRDVGE LDLPSGEPFA GLFTQGMVTH ETYRSEGGTW LEPSAVERKD
     GQVFEIATGK PVKVGAIEKM SKSKKNTVDP DAIVATYGAD VARWFVLSDS PPERDVEWTQ
     SGAEGAARFV QRVWSFVDSL PETGPFPAPG SDDVSTALRK SNHKAVAAID RAIEEFRFNS
     AIATIHEWVN ALKKTESDPA TLGARAEGAD MLARCLVPFM PHLAEACWER LGQTSLVSQA
     MWPKIDASLV VDDTVTLAVQ VNGKRRAEIT VAKDMAPDAV EAAAKALPDV ASFIAGKSVK
     KTIVVPGRIV NIVVA