SYL_SYNAS
ID SYL_SYNAS Reviewed; 862 AA.
AC Q2LQK5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 100.
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=SYNAS_01790;
GN ORFNames=SYN_02374;
OS Syntrophus aciditrophicus (strain SB).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophales; Syntrophaceae;
OC Syntrophus.
OX NCBI_TaxID=56780;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB;
RX PubMed=17442750; DOI=10.1073/pnas.0610456104;
RA McInerney M.J., Rohlin L., Mouttaki H., Kim U., Krupp R.S.,
RA Rios-Hernandez L., Sieber J., Struchtemeyer C.G., Bhattacharyya A.,
RA Campbell J.W., Gunsalus R.P.;
RT "The genome of Syntrophus aciditrophicus: life at the thermodynamic limit
RT of microbial growth.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:7600-7605(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; CP000252; ABC76058.1; -; Genomic_DNA.
DR RefSeq; WP_011416093.1; NC_007759.1.
DR AlphaFoldDB; Q2LQK5; -.
DR SMR; Q2LQK5; -.
DR STRING; 56780.SYN_02374; -.
DR PRIDE; Q2LQK5; -.
DR EnsemblBacteria; ABC76058; ABC76058; SYN_02374.
DR KEGG; sat:SYN_02374; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_7; -.
DR OMA; TFMVLAP; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000001933; 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; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 2.
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..862
FT /note="Leucine--tRNA ligase"
FT /id="PRO_1000009453"
FT MOTIF 42..52
FT /note="'HIGH' region"
FT MOTIF 614..618
FT /note="'KMSKS' region"
FT BINDING 617
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 862 AA; 98777 MW; E81B3D4E8454F1A9 CRC64;
MNRKYVPQEI EEKWQRYWEE KNTFKVTEDP SKKKYYLLEM FPYPSGKIHI GHVRNYTIGD
VVARYKRMEG YNVLHPMGWD SFGMPAENAA IERGIHPSLW TNENITHMRK QLKRMGFSYD
WDREVSTCEP VYYRWEQLFF LWMYEKGLAY KKTSSVNWCP RCQTVLANEQ VEAGLCWRCG
SEVVEKILDQ WFFRITAYID ELLAGCDRLT GWPERVLTMQ RNWIGKSYGC EVSFPMADGN
GDIKVFTTRQ DTLFGATFML IAAEHPLVME LIKGKPVEKD ARTFAEEVKK QDKLMRTSDY
YEKQGLFLDC YCLNPLTGWE MPIFATNFVL ADYGTGCVMA VPTHDQRDFE FAEKFGLRKV
VVISPPDKTL DPETMTEAYV EEGILVNSGP FNGMENLKAL DAIADHLIAL GRGKRTIQYR
LRDWGISRQR YWGAPIPMIM CPKCGTVPVP EAELPVVLPR DVDFSGEGGS PLAKHPEFLN
TTCPSCGGPA KRESDTMDTF VESSWYFERY CCPHFAEKPG LNRQQVDYWM PVDQYIGGIE
HAILHLLYAR FYTRMLRDFG LVGVDEPFTN LLTQGMVCKE TTRCPDHGYL YPEEVREGRC
IHCLAEVIVG KTEKMSKSLK NVVDPDYLVR QYGADTARMF CLFAAPPEKD LEWSDQGVEG
SFRFIGRTWR IVVDYLDDLQ GIAPFAGDGE LEGELKSLRR KTHQTIRKVR DDMGERFHFN
TAISAIMELV NTLYGLPRPP REDRTALAVI RETIEAIILL LAPIVPHLTE ELWQMLGHQG
TCLADTPLPV YDPTVAAEDE MTIVIQVNGK VRSRVIVAAD EAEDKIKALA MGDEKVSRFL
EGKSVIKQVY VPKKLVNIVV KG