SYL_HAEIG
ID SYL_HAEIG Reviewed; 861 AA.
AC A5UI62;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 91.
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};
GN OrderedLocusNames=CGSHiGG_08170;
OS Haemophilus influenzae (strain PittGG).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=374931;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PittGG;
RX PubMed=17550610; DOI=10.1186/gb-2007-8-6-r103;
RA Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R., Post J.C.,
RA Ehrlich G.D.;
RT "Characterization and modeling of the Haemophilus influenzae core and
RT supragenomes based on the complete genomic sequences of Rd and 12 clinical
RT nontypeable strains.";
RL Genome Biol. 8:R103.1-R103.18(2007).
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; CP000672; ABR00468.1; -; Genomic_DNA.
DR RefSeq; WP_012055298.1; NC_009567.1.
DR AlphaFoldDB; A5UI62; -.
DR SMR; A5UI62; -.
DR PRIDE; A5UI62; -.
DR EnsemblBacteria; ABR00468; ABR00468; CGSHiGG_08170.
DR KEGG; hiq:CGSHiGG_08170; -.
DR HOGENOM; CLU_004427_0_0_6; -.
DR OMA; TFMVLAP; -.
DR Proteomes; UP000001990; 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 Gene3D; 3.90.740.10; -; 1.
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.
FT CHAIN 1..861
FT /note="Leucine--tRNA ligase"
FT /id="PRO_1000009349"
FT MOTIF 42..52
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 861 AA; 97692 MW; 4F63A50073431A45 CRC64;
MQEQYRPDMI EPKVQQYWVE NKVFKAIKDE SKEKYYCLSM FPYPSGRLHM GHVRNYTIGD
VISRYQRMLG KNVLQPFGWD AFGLPAEGAA IKNKTAPAKW TYENIAYMKK QLQLLGFGFD
WDREIATCKP EYYKWEQWFF TELYKKGLVY KKTSTVNWCP NDETVLANEQ VHEGCCWRCD
TPVEQKEIPQ WFIKITDYAE QLLGGLDTLP QWPDMVKTMQ RNWIGRSEGV EITFDVANTN
EKVAVYTTRP DTFYGVSYLG IAAAHPLASL AAQNNPELAA FIQEAKNAKV AEADLATMEK
KGMATGLFAI HPLTGEKLPI WVANFVLMHY GTGAVMAVPA HDQRDFEFAQ KYSLPIKQVI
APLADEEIDL TKQAFVEHGK LVNSAEFDGK DFDGAFNGIA DKLEKLGVGK RQVNYRLRDW
GVSRQRYWGA PIPMLTLENG DVVPAPMEDL PIILPEDVVM DGVKSPIKAD PNWAKTTLNG
TPALKETDTF DTFMESSWYY ARYTCPQYQN GMLDAEEANY WLPVDQYIGG IEHATMHLLY
FRFFHKLLRD AGFVTSEEPA DKLLCQGMVL ADAFYYTSPT NERIWVSPTQ VTLERDEKGR
IIKATDPEGR ELVHSGMTKM SKSKNNGIDP QEMVEKYGAD TVRLFMMFAS PAEMTLEWQE
SGVEGAKRFL GRVWNLVYQY QQNPAKTSLD ITALSAEQKV LRREVHKTIA KVSDDIGRRQ
TFNTAIAAVM ELMNKLTKAP LDSEQDRAVM AEALSAVVRM LYPITPHICF ELWQALGNES
AIDTAEWVKA DEAAMVEDEK LIVVQVNGKV RGKVTVAADA DEDTVKTIAF ADENVKKFID
NQHIVKVIYV VGKLLNVVVK P