ID SYL_AZOSB Reviewed; 873 AA.
AC A1KAH5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 105.
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=azo3215;
OS Azoarcus sp. (strain BH72).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC Azoarcus.
OX NCBI_TaxID=418699;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BH72;
RX PubMed=17057704; DOI=10.1038/nbt1243;
RA Krause A., Ramakumar A., Bartels D., Battistoni F., Bekel T., Boch J.,
RA Boehm M., Friedrich F., Hurek T., Krause L., Linke B., McHardy A.C.,
RA Sarkar A., Schneiker S., Syed A.A., Thauer R., Vorhoelter F.-J.,
RA Weidner S., Puehler A., Reinhold-Hurek B., Kaiser O., Goesmann A.;
RT "Complete genome of the mutualistic, N2-fixing grass endophyte Azoarcus sp.
RT strain BH72.";
RL Nat. Biotechnol. 24:1385-1391(2006).
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; AM406670; CAL95831.1; -; Genomic_DNA.
DR RefSeq; WP_011766939.1; NZ_CP016210.1.
DR AlphaFoldDB; A1KAH5; -.
DR SMR; A1KAH5; -.
DR STRING; 62928.azo3215; -.
DR KEGG; aoa:dqs_3352; -.
DR KEGG; azo:azo3215; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_4; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000002588; 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 CDD; cd07958; Anticodon_Ia_Leu_BEm; 1.
DR CDD; cd00812; LeuRS_core; 1.
DR Gene3D; 2.20.28.290; -; 1.
DR Gene3D; 3.10.20.590; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 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; 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 NCBIfam; TIGR00396; leuS_bact; 1.
DR PANTHER; PTHR43740:SF2; LEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 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; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 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..873
FT /note="Leucine--tRNA ligase"
FT /id="PRO_1000009290"
FT MOTIF 42..52
FT /note="'HIGH' region"
FT MOTIF 628..632
FT /note="'KMSKS' region"
FT BINDING 631
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 873 AA; 96943 MW; 9516D7967993F4CB CRC64;
MQDKYQPAAV ETAAQQHWES TAAFRVTEDA TRPKYYCLSM FPYPSGKLHM GHVRNYTIGD
VLARFHRMRG YNVLQPMGWD AFGMPAENAA IQNNVPPAKW TYANIDYMKG QLKRLGFAID
WSREVATCTP EYYRWEQWLF TRLFEKGLIY KKLGTVNWDP VDETVLANEQ VIDGRGWRSG
ALVEKREIPM YYMKITAYAD ELLEALDGLP GWPEQVKLMQ KNWIGRSEGV EVHFPYDLST
IGSSGVLKVF TTRGDTLMGA TYVAVAAEHP LATQAAAGNP ELAAFIDECK QGGVAEADLA
TMEKKGMPTG LRVVHPITGE YLPVWVANYV LMGYGEGAVM AVPAHDERDF AFATKYKLPI
KMVVRSTHDA YENVAAPWID AYAEHGKLVN SGKYDNLHFQ DAVDAIAADL AAKGLGNKRV
QYRLRDWGIS RQRYWGCPIP MVRCDDCGDV PVPDEQLPVV LPENVEITGR GSPLAKMPEF
YQCSCPKCGK PARRETDTMD TFVESSWYFL RYASPDSTTA MVDERVNYWA PVDQYIGGIE
HAILHLLYSR FFTRAMRDCG LVNVSEPFTN LLTQGMVVAE TYYRELDGGK KQWLNPADVQ
VERDERGRIT AAKLASDGLP VVIGGTEKMS KSKNNGVDPQ ALVDQYGADT ARLFIIFAAP
PDQQLEWSDS GVEGASRFLR RVWNFGHAFA SEFRAALPAA RALAAGTLPA ALADVRREIH
THLKQANYDF GKHQFNTVVS AAMKILNALE KAPRDDAAAH AEVAEEGFSI LVRLLSPITP
HIAHALWQDC GFGGDIVQAA WPEPLEAALK QDEIELMLQV NGKLRGSVKV AADAGKSDIE
ALALASEAAQ KFMEGKPPKK VVVVPGRLVN IVV
//
