ID   SYL_PHEZH               Reviewed;         867 AA.
AC   B4RCZ4;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=PHZ_c3517;
OS   Phenylobacterium zucineum (strain HLK1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Phenylobacterium.
OX   NCBI_TaxID=450851;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HLK1;
RX   PubMed=18700039; DOI=10.1186/1471-2164-9-386;
RA   Luo Y., Xu X., Ding Z., Liu Z., Zhang B., Yan Z., Sun J., Hu S., Hu X.;
RT   "Complete genome of Phenylobacterium zucineum - a novel facultative
RT   intracellular bacterium isolated from human erythroleukemia cell line
RT   K562.";
RL   BMC Genomics 9:386-386(2008).
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; CP000747; ACG79926.1; -; Genomic_DNA.
DR   RefSeq; WP_012524064.1; NC_011144.1.
DR   AlphaFoldDB; B4RCZ4; -.
DR   SMR; B4RCZ4; -.
DR   STRING; 450851.PHZ_c3517; -.
DR   EnsemblBacteria; ACG79926; ACG79926; PHZ_c3517.
DR   KEGG; pzu:PHZ_c3517; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_5; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000001868; 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..867
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000199218"
FT   MOTIF           43..53
FT                   /note="'HIGH' region"
FT   MOTIF           627..631
FT                   /note="'KMSKS' region"
FT   BINDING         630
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   867 AA;  96158 MW;  A803FE1B482BC32A CRC64;
     MAATRYNPKE TEPKWRKRWD EAQAFRAVEA PGKRKYYVLE MFPYPSGRLH MGHVRNYALG
     DVIARYKRAQ DFSVLHPMGW DAFGLPAENA AMERGVDPKA WTYDNIARMR AELKELGLSI
     DWSREFATCD VEYYGQQQAL FLELFERGLV YRKESVVNWD PVDQTVLANE QVVDGKGWRS
     GAPVEKRKLA QWFLKITQYA DQLVDDLKTL DRWPEKVRVM QENWIGRSKG ARLRFRFAGQ
     PPAGHEAGVE VYTTRPDTLF GASFVGVAPD HPLAQAVAAA NPEAAAFIEK CRHGAVSEAE
     IETAEKEGFD TGLKVKHPFD PSWELPVWIA NFILMDYGTG AIFGCPAHDQ RDLDFARKYG
     LPVKPVVLPP EEAQAEAIVQ KLLNEAYTGP GRIINSGFLD GLDVEAAKAA AIARIEEQGD
     GQGATVYRLR DWGVSRQRAW GCPIPVVHCQ ACGVVPVRRS DLPLTHPADI EFGKAGNALE
     RHPTWKHTTC PGCGGPATRE TDTLDTFVDS SWYFARFANP GAEAPIDKAA ADYWLPVDQY
     IGGVEHAVLH LLYARFITKA LADVGMLSVR EPFAGLFTQG MVTHETYRKQ SGEWVEPKEV
     EVTAEGKTRR ARLVGSGEPV VIGDVEKMSK SKKNTVAPEE IFDVYGVDAA RLFVLSDSPP
     ERDAQWSTSG VQGAWRFVNR VWDEFDASEE PVPGTEEAVT GVATDNLRRQ HAKTVKAVTE
     AIEGFRFNSA IAHLYSFLNV LKAERPQGRA GALAHAHRAA LRDFALLIAP FTPHLAEECW
     ARIGGQGLVV EAPWPTYDPA LTQDAVKVLP VQVNGKRRGE ISAPAGAEPA EVEQLVLADP
     EIKARLEGLT IRKIIVVKDR IVNIVAA