SYL_DESAL
ID SYL_DESAL Reviewed; 863 AA.
AC B8F9F0;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 81.
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=Dalk_1193;
OS Desulfatibacillum aliphaticivorans.
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales;
OC Desulfobacteraceae; Desulfatibacillum.
OX NCBI_TaxID=218208;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK-01;
RX PubMed=21651686; DOI=10.1111/j.1462-2920.2011.02516.x;
RA Callaghan A.V., Morris B.E., Pereira I.A., McInerney M.J., Austin R.N.,
RA Groves J.T., Kukor J.J., Suflita J.M., Young L.Y., Zylstra G.J., Wawrik B.;
RT "The genome sequence of Desulfatibacillum alkenivorans AK-01: a blueprint
RT for anaerobic alkane oxidation.";
RL Environ. Microbiol. 14:101-113(2012).
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; CP001322; ACL02896.1; -; Genomic_DNA.
DR RefSeq; WP_012610332.1; NC_011768.1.
DR AlphaFoldDB; B8F9F0; -.
DR SMR; B8F9F0; -.
DR EnsemblBacteria; ACL02896; ACL02896; Dalk_1193.
DR KEGG; dal:Dalk_1193; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_7; -.
DR OMA; TFMVLAP; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000000739; 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; 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; Reference proteome.
FT CHAIN 1..863
FT /note="Leucine--tRNA ligase"
FT /id="PRO_1000199195"
FT MOTIF 42..52
FT /note="'HIGH' region"
FT MOTIF 618..622
FT /note="'KMSKS' region"
FT BINDING 621
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 863 AA; 98398 MW; CEDE2E1693FC4A01 CRC64;
MDERYDPKKI EGKWQAHWDA AGLFKVKEDP SKEKYFLMEM FPYPSGKIHM GHVRNYSIGD
VVARFKRMQG FNVLHPMGWD AFGMPAENAA IKNNTHPAKW TYENIAAMGA QLKAMGFSYD
WDREIATCKP DYYRWEQWLF VQMFKKGMVY RKEASVNWCH TCQTVLANEQ VEQNMCWRCG
DEVEQKKLKQ WFFRITDYAD DLLEHCDKLP GWPEKVVTMQ KNWIGKSHGA EILFSVKDSD
VKIKVFTTRP DTLCGATFMC LAPEHPLVED LSKGTAQEAV VQEFVARMAK QDKAKRTADD
KEKEGVPIGA QCINPLTGKT MEIYTANFAL MEYGTGAVMS VPTHDQRDFE FATKYGLEKI
VVIQPEGEAL SPETMTEAYT DPGVLVNSGQ FDGMKNTDAM EAIAQYLDEN DMGKKTVQYR
IRDWGISRQR YWGAPIPMIH CPDCGITPVP EDQLPVILPE DANLLEGGKS PLPELDSFVK
TTCPQCGNEN ARRETDTMDT FVESSWYPER YCSPKCDDGM FDVDAVKYWM PVDQYIGGVE
HAVMHLLYSR YFTRVLNDFG LVDFKEPFTR LLTQGMVCKE TLKCPEHGWL FPHEVEGSGD
ERTCTKCGKI VEAGRVEKMS KSKLNVVDPE ELLAKYGADT IRLFCLFAAP PERDLDWSEE
GVEGSYRFLQ RVWRMFAAHM DEVKDAQPFE GSPDDLDGYL KDLYKKTHQT IKKVTEDIDG
RFHFNTAISA VMELVNMVYG LDDNLQGEKR AGVLRAAVEA VILLISPMTP HFTEELWSLF
GKTQCVLETP WPAWREDALT ADEVVVVLQV NGKLRSKLNV PLDTDDEKIK EMALADEKVQ
KFMGGKPIRK VIVVKNKLVN VVV
