SYL_AFIC5
ID SYL_AFIC5 Reviewed; 879 AA.
AC B6JAI4; F8BS31;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=OCAR_4363, OCA5_c01660;
OS Afipia carboxidovorans (strain ATCC 49405 / DSM 1227 / KCTC 32145 / OM5)
OS (Oligotropha carboxidovorans).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Afipia.
OX NCBI_TaxID=504832;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49405 / DSM 1227 / KCTC 32145 / OM5;
RX PubMed=18539730; DOI=10.1128/jb.00614-08;
RA Paul D., Bridges S., Burgess S.C., Dandass Y., Lawrence M.L.;
RT "Genome sequence of the chemolithoautotrophic bacterium Oligotropha
RT carboxidovorans OM5T.";
RL J. Bacteriol. 190:5531-5532(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49405 / DSM 1227 / KCTC 32145 / OM5;
RX PubMed=21742883; DOI=10.1128/jb.05619-11;
RA Volland S., Rachinger M., Strittmatter A., Daniel R., Gottschalk G.,
RA Meyer O.;
RT "Complete genome sequences of the chemolithoautotrophic Oligotropha
RT carboxidovorans strains OM4 and OM5.";
RL J. Bacteriol. 193:5043-5043(2011).
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; CP001196; ACI91509.1; -; Genomic_DNA.
DR EMBL; CP002826; AEI04898.1; -; Genomic_DNA.
DR RefSeq; WP_012561540.1; NC_015684.1.
DR AlphaFoldDB; B6JAI4; -.
DR SMR; B6JAI4; -.
DR STRING; 504832.OCAR_4363; -.
DR PRIDE; B6JAI4; -.
DR EnsemblBacteria; AEI04898; AEI04898; OCA5_c01660.
DR KEGG; oca:OCAR_4363; -.
DR KEGG; ocg:OCA5_c01660; -.
DR PATRIC; fig|504832.7.peg.175; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_5; -.
DR OMA; TFMVLAP; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000007730; 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..879
FT /note="Leucine--tRNA ligase"
FT /id="PRO_1000091340"
FT MOTIF 43..53
FT /note="'HIGH' region"
FT MOTIF 636..640
FT /note="'KMSKS' region"
FT BINDING 639
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 879 AA; 98025 MW; 9C29A2C1EF90A0A5 CRC64;
MSTERYNARE VEPRWQQIWD EKGVFASRND DSRPKYYVLE MFPYPSGRIH MGHVRNYTMG
DVVARYRRAK GHNVLHPMGW DAFGMPAENA AMQNKTHPAK WTYANIAAMK KQLKSMGLSL
DWAREIATCD PSYYKHQQRM FLDFLKAGLV ERKQSKVNWD PVDQTVLANE QVIDGRGWRS
GALVEQRELT QWFFKISDYS EELLTALDTL DRWPEKVRLM QKNWIGRSEG LLVRFALDAA
TAPAGESEVE VFTTRPDTLF GAKFVALSPD HPLAAEVAKA NPKLEAFIAE CHRHGTAQAE
IDTAEKLGFD TGLRARHPFD PDWLLPVYVA NFVLMDYGTG AIFGCPAHDQ RDLDFVNKYG
LGNTPVVCPE GQDPKSFVIT DTAYDGDGRM INSRFLDGMT IADAKEDVAK RLETATLPRA
NGGGNAPVAK RQVNYRLRDW GISRQRYWGC PIPIIHCESC GIVPVPVKDL PVKLPDDIEF
DRPGNPLDRH PTWKHVACPQ CGGKARRETD TMDTFVDSSW YFARFTDPWN ENAPTTRKVV
DAMMPVDQYI GGIEHAILHL LYSRFFTRAM KATGHVGFDE PFAGLFTQGM VVHETYKNAD
GSWAAPSEIK IEGTGDARHA TLIDTGAPVE IGSIEKMSKS KRNTIDPDDI IGTYGADTAR
WFMLSDSPPD RDVIWSEEGV QGANRFVQRV WRLVNLAAPH LPKDSAAAGT SADTKPLRST
AHRTLADVSQ AIERLRFNTA IAKLYAFVGP LNEAIDDPRL KADPAWAASV REALDMLVRM
IAPMMPHLAE QCWEALGGQG LVSEAAWPEV DPVLLVEDTI TLPVQINGKK RADVTVGRNA
PNPEIEAAVL ALDAVKTALA GATPRKIIVV PQRIVNVVV
