SYL_SULDN
ID SYL_SULDN Reviewed; 822 AA.
AC Q30Q82;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 118.
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=Suden_1572;
OS Sulfurimonas denitrificans (strain ATCC 33889 / DSM 1251) (Thiomicrospira
OS denitrificans (strain ATCC 33889 / DSM 1251)).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Thiovulaceae; Sulfurimonas.
OX NCBI_TaxID=326298;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33889 / DSM 1251;
RX PubMed=18065616; DOI=10.1128/aem.01844-07;
RA Sievert S.M., Scott K.M., Klotz M.G., Chain P.S.G., Hauser L.J., Hemp J.,
RA Huegler M., Land M., Lapidus A., Larimer F.W., Lucas S., Malfatti S.A.,
RA Meyer F., Paulsen I.T., Ren Q., Simon J., Bailey K., Diaz E.,
RA Fitzpatrick K.A., Glover B., Gwatney N., Korajkic A., Long A.,
RA Mobberley J.M., Pantry S.N., Pazder G., Peterson S., Quintanilla J.D.,
RA Sprinkle R., Stephens J., Thomas P., Vaughn R., Weber M.J., Wooten L.L.;
RT "Genome of the epsilonproteobacterial chemolithoautotroph Sulfurimonas
RT denitrificans.";
RL Appl. Environ. Microbiol. 74:1145-1156(2008).
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; CP000153; ABB44849.1; -; Genomic_DNA.
DR RefSeq; WP_011373201.1; NC_007575.1.
DR AlphaFoldDB; Q30Q82; -.
DR SMR; Q30Q82; -.
DR STRING; 326298.Suden_1572; -.
DR PRIDE; Q30Q82; -.
DR EnsemblBacteria; ABB44849; ABB44849; Suden_1572.
DR KEGG; tdn:Suden_1572; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_7; -.
DR OMA; TFMVLAP; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000002714; 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; 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; 2.
DR Pfam; PF00133; tRNA-synt_1; 1.
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..822
FT /note="Leucine--tRNA ligase"
FT /id="PRO_1000091373"
FT MOTIF 46..56
FT /note="'HIGH' region"
FT MOTIF 590..594
FT /note="'KMSKS' region"
FT BINDING 593
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 822 AA; 94408 MW; 202B10DAC105403F CRC64;
MIYNSKELEK KWQEYWAKNR SFEPSEDFTK ETGCPRGKKY ILSMFPFPSG RLHMGHVRNY
TISDAFARYY RQEGFNVLHP IGFDSFGMPA ENAAIKNGSH PKKWTYDNID YMKGEFKSLG
FSFSKDRELA TSDELYTKFE QGFIIDMYEK GLLYRKKGFL NWCPSCHTVL ANEQVIDGSC
WRCDSSVVKK DMNQYYFKIT QYGDELLADL SKLESGWPKQ VLTMQENWIG KSNGLEFKLS
FDEKSLEKLD NKFDTFSVFT TRPDTIYGVS YAALAPEHEI VSYMIENALV GSDTIEKIKE
MKNASSIERQ KEKSGIALNL HVVHPLTKKL IPIWVANFVL MDYGSGAVMA VPAHDERDFD
FAKKYNLPIK AVIKPFDGES SIESAFTEVG ELFDSEMFNG LNSKDAQLKI IEHFEEKKIG
KKTTNYKLKD WGVSRQRYWG APIPFVHCDS CGIVMEKKEN LPIALPEDIE ITGEGNPLEK
HPTWKYCKCP KCDKDAIRET DTMDTFVESS WYFLRFCASP KNWLNEAFSK EQIKYWMGVD
HYIGGIEHAI LHLLYARFFT KVFRDLGYLE FDEPFNKLLT QGMVLKDGAK MSKSKGNTVD
PDAIIEKYGA DTARLFILFA APPTQELEWN DNAVEGAFKF IKRFYERSVN AIKTNTIPKI
NHASLSKEEK FARKKVYEAL VRSREVYGEK YTFNTMIAGV MEAMNALNLQ TNSDVWSEAY
WILTSIMEPV IPHVCSEISS VKFSLKNLSS QIVVQEVFVE DSLMLGVTVN GKRRCEIEVP
TEATQDEILQ IARESASKWL EGKTIIKEIV VPKKLVNLVI KD