SYL_SYNWW
ID SYL_SYNWW Reviewed; 824 AA.
AC Q0AWK4;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 103.
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=Swol_1599;
OS Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Syntrophomonadaceae;
OC Syntrophomonas.
OX NCBI_TaxID=335541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2245B / Goettingen;
RX PubMed=21966920; DOI=10.1111/j.1462-2920.2010.02237.x;
RA Sieber J.R., Sims D.R., Han C., Kim E., Lykidis A., Lapidus A.L.,
RA McDonnald E., Rohlin L., Culley D.E., Gunsalus R., McInerney M.J.;
RT "The genome of Syntrophomonas wolfei: new insights into syntrophic
RT metabolism and biohydrogen production.";
RL Environ. Microbiol. 12:2289-2301(2010).
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; CP000448; ABI68900.1; -; Genomic_DNA.
DR RefSeq; WP_011640998.1; NC_008346.1.
DR AlphaFoldDB; Q0AWK4; -.
DR SMR; Q0AWK4; -.
DR STRING; 335541.Swol_1599; -.
DR PRIDE; Q0AWK4; -.
DR EnsemblBacteria; ABI68900; ABI68900; Swol_1599.
DR KEGG; swo:Swol_1599; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_9; -.
DR OMA; TFMVLAP; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000001968; 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; 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; 2.
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; 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..824
FT /note="Leucine--tRNA ligase"
FT /id="PRO_0000334833"
FT MOTIF 42..52
FT /note="'HIGH' region"
FT MOTIF 581..585
FT /note="'KMSKS' region"
FT BINDING 584
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 824 AA; 94728 MW; BDD2B77DF3ADA95E CRC64;
MDRKYDFKSI EAKWQAYWEN KQLFKVEEDP EKPKYYNLEM FPYPSGHLHM GHVRNYAIGD
VVARFKSMNG FNVLHPMGWD AFGLPAENAA IKNAIHPATW TYSNIENMKR QLKTMGISYD
WDRELATCKP DYYKFTQWMF LKLYENKLAY KKKSAVNWCP SCQTVLANEQ VVDGACERCE
AVIEKKQLEQ WFFKITDYAQ RLLDDLALLP GWPEKVKTMQ KNWIGRSEGC EFSLHIEDSD
EVLTVFTTRP DTVFGVTYMV LAPEHPLVEK ICHPEQEKEV KAFVNKMKYL NEMARTSTEA
EKEGVFTGAY AINPMDGSRI PIWIANYVLM DYGTGAIMAV PAHDQRDFEF ARKYDIPVKV
VIKGEDTPLD GNLLQESYPG DGHMVNSGNF DGLTVEEGQK AVIKFMEEKG IGQGTVNYRL
RDWLISRQRY WGAPIPIVYC PECGPVAVPE EELPLYLPED IDFKPYAESP LKHLERFYKT
TCPSCGKEAL RETDTMDTFV CSSWYFDRFC SPHESKQPFS REAVDYWMPV DQYIGGVEHA
ILHLMYARFF TKFLFDINVL SCQEPFTRLL TQGMVLKDNA KMSKSKGNVV SPEEIIDTYG
ADTARLFILF ASPPERDLEW SEQGVEGAFR FLNRVWRLVS ELAEGIKDLP AAEHFPELDS
EAKNLRFKTH ATIKKVTEDI GERFNFNTAI SAIMELSNTL GAYKGIKKPN WPVVKEAVDN
LLILLSPFSP HICEELWQLT GHAESIYLQK WPKYDPEALL QEEIEIVLQI SGKVRDRIMV
PVDAGREELE KIALDNPKIR ELTRGKEIVK LIVVPGKLVN VVAK
