ID   SYL_PSYIN               Reviewed;         859 AA.
AC   A1SU60;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, 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=Ping_1191;
OS   Psychromonas ingrahamii (strain 37).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Psychromonadaceae; Psychromonas.
OX   NCBI_TaxID=357804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=37;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Staley J.,
RA   Richardson P.;
RT   "Complete sequence of Psychromonas ingrahamii 37.";
RL   Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000510; ABM03025.1; -; Genomic_DNA.
DR   RefSeq; WP_011769588.1; NC_008709.1.
DR   AlphaFoldDB; A1SU60; -.
DR   SMR; A1SU60; -.
DR   STRING; 357804.Ping_1191; -.
DR   EnsemblBacteria; ABM03025; ABM03025; Ping_1191.
DR   KEGG; pin:Ping_1191; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_6; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000000639; 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..859
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009402"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT   MOTIF           618..622
FT                   /note="'KMSKS' region"
FT   BINDING         621
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   859 AA;  96995 MW;  B0636E5861FFDE2E CRC64;
     MQELYNPKEI EKKFQTNWDE NQSFKATEDP SKEKYYCLSM FPYPSGKLHM GHVRNYTIGD
     VISRYQRMQG KNVMQPMGWD AFGLPAENAA IKNNTAPAGW TYENIAYMKT QLKQLGFGYD
     WSRELATCQP EYYRWEQWFF TKLVEKDLVY KKMATVNWDP VDQTVLANEQ VIDGRGWRSG
     ALVEQKEIPQ WFIKITAYAQ ELLDDLDKLD EWPEQVRTMQ RNWIGRSEGV EMDFKVSGKE
     ESFSVYTTRP DTVMGVTYVA VAAQHPLALE AAKNNPTLAA FCKKCKNVKL AEAEIATMAK
     EGVDTGFKAI HPISGLEVPI WTANFVLMGY GSGAVMSVPA HDQRDYEFAK KYDLTIKAVI
     KPANTDLDIS VEAYTEKGVC FDSGEFDGLD FSAAFDAVET KLVAENKGKR QVNFRLRDWG
     VSRQRYWGTP IPMLNLEDGS VVPVPENELP VILPEDVQMN GIVSPIKADP DWAKTTYNGQ
     PATHETDTFD TFMESSWYYA RYCSPQSDDA MLDPEKANYW LPVDQYIGGI EHAILHLLYS
     RFFHKLLRDF GLVDCDEPYK KLLTQGMVLA DAYYYEDAKG GKVWIAPTDV ETETDEKGKV
     ISAATKDGQT VIYDGMSKMS KSKNNGVDPQ VMIDKYGADS VRLFMMFAAP ADQTLEWSDS
     ALEGSLRFLK RLWKIAFDHL ALGAVADLDL KSHTEAQKTL RRELHKTIAK VTDDIGRRQT
     FNTAIASVME LMNKLTKTAT KTEQDRAILQ EALLAITKLL APITPHICAE LFEVLGQTEE
     ILNAPWPTVD ESALVEDSKL IVVQVNGKLR AKLTVAADAQ QETVQAIAME NENVSKFTDG
     KTIRKIIFVP GKLLNIVAN