ID   SYL_PORG3               Reviewed;         925 AA.
AC   B2RIZ3;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 90.
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=PGN_0819;
OS   Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM
OS   12257 / NCTC 11834 / 2561).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC   Porphyromonas.
OX   NCBI_TaxID=431947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561;
RX   PubMed=18524787; DOI=10.1093/dnares/dsn013;
RA   Naito M., Hirakawa H., Yamashita A., Ohara N., Shoji M., Yukitake H.,
RA   Nakayama K., Toh H., Yoshimura F., Kuhara S., Hattori M., Hayashi T.,
RA   Nakayama K.;
RT   "Determination of the genome sequence of Porphyromonas gingivalis strain
RT   ATCC 33277 and genomic comparison with strain W83 revealed extensive genome
RT   rearrangements in P. gingivalis.";
RL   DNA Res. 15:215-225(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; AP009380; BAG33338.1; -; Genomic_DNA.
DR   RefSeq; WP_012457800.1; NZ_CP025930.1.
DR   AlphaFoldDB; B2RIZ3; -.
DR   SMR; B2RIZ3; -.
DR   STRING; 431947.PGN_0819; -.
DR   EnsemblBacteria; BAG33338; BAG33338; PGN_0819.
DR   GeneID; 29256038; -.
DR   KEGG; pgn:PGN_0819; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_10; -.
DR   OMA; TFMVLAP; -.
DR   BioCyc; PGIN431947:G1G2V-897-MON; -.
DR   Proteomes; UP000008842; 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; -; 3.
DR   HAMAP; MF_00049_B; Leu_tRNA_synth_B; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
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   PANTHER; PTHR43740; PTHR43740; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF13603; tRNA-synt_1_2; 1.
DR   Pfam; PF09334; tRNA-synt_1g; 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.
FT   CHAIN           1..925
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000091343"
FT   MOTIF           40..51
FT                   /note="'HIGH' region"
FT   MOTIF           700..704
FT                   /note="'KMSKS' region"
FT   BINDING         703
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   925 AA;  106051 MW;  D1E774CE15ABA339 CRC64;
     MEYNFQEIEK RVQGQWRKDK VYRVAEDTSK KPFYVLDMFP YPSGAGLHVG HPLGYIASDI
     FSRYKRLRGF NVLHPMGYDA FGLPAEQYAI QTGQHPEKTT EENTARYREQ LDKIGFSYDW
     EREIRTCDPN YYKWTQWAFL KMFDSYYCNQ AQQARPISEL IEVFARQGNE GLNVACGEGV
     RFTAEEWTAM SEKEQQEILM NYRLAYLGDT MVNWCPALGT VLANDEVKDG VSERGGHPVE
     QKKMRQWCLR VSAYAERLLH DLETLDWTES LKETQRNWIG RSEGAEMEFR LAGKDCTFTI
     FTTRADTIFG VTFMVLAPES ELVEEVTTEE QRAAVETYLT ETKRRTERER ISDKRVSGVF
     SGSYAINPLT GKEIPIWISD YVLAGYGTGA IMAVPAHDTR DFAFARHFDL PIVQVVVPEG
     ETATDPATWE DAKDSKSGIM VNSDFLNGLS VEDAIAQTKE YIREKHLGCV KVNYRLRDAI
     FSRQRYWGEP FPIYYKEGMP HALDEDRLPL RLPEVDKFLP TESGEPPLGR ATGWHTAEGY
     PYELSTMPGF AGSSAYYLRY MDPQNDTALV SRSANEYWRH VDLYIGGTEH ATGHLIYSRF
     WNKFLFDLGI VCEAEPFRKL VNQGMIQGRS NFVYRIKNTN TFVSYGLREQ YEVTPLHVDV
     NIVSNDQLDI DRFRAWRPEY ASAEFILEDG KYICGWAIEK MSKSMFNVVN PDDIIARYGA
     DTLRLYEMFL GPLEQSKPWD TNGIDGVHRF LKKFWALYYN ADGIRVTDTA PTKEELKSLH
     KLIKKVGQDI ESFSFNTSIP AFMICVNELT AAKTTSRAIL CPLLTVLSPF APHITEWLWQ
     ELGVEGSIVT ATWPEYNEEY LVESCVRYPV SFNGKVRFNI ELPADMSKKD VEQAALTAPE
     AARWLEGKSP KKVIVVPGRI VNVVV