SYL_CORGL
ID SYL_CORGL Reviewed; 952 AA.
AC Q8NLC4;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 126.
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=Cgl3018, cg3346;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAF18958.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BA000036; BAC00412.1; -; Genomic_DNA.
DR EMBL; BX927157; CAF18958.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_602213.1; NC_003450.3.
DR RefSeq; WP_011015573.1; NC_006958.1.
DR AlphaFoldDB; Q8NLC4; -.
DR SMR; Q8NLC4; -.
DR STRING; 196627.cg3346; -.
DR KEGG; cgb:cg3346; -.
DR KEGG; cgl:Cgl3018; -.
DR PATRIC; fig|196627.13.peg.2953; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_11; -.
DR OMA; TFMVLAP; -.
DR Proteomes; UP000000582; 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; -; 3.
DR HAMAP; MF_00049_B; Leu_tRNA_synth_B; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
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; 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..952
FT /note="Leucine--tRNA ligase"
FT /id="PRO_0000152007"
FT MOTIF 66..77
FT /note="'HIGH' region"
FT MOTIF 722..726
FT /note="'KMSKS' region"
FT BINDING 725
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 952 AA; 106779 MW; 3A1D2E2CD12D13E5 CRC64;
MTNPSEGTTP LAFRYTPELA NKIEGEWQNY WTDNGTFNAP NPVGDLAPAD GKALPEDKLF
VQDMFPYPSG AGLHVGHPLG YIATDVFARY NRMLGKNVLH TLGYDAFGLP AEQYAIQTGT
HPRTTTMANI ENMKRQLGAL GLGHDSRRAV ATTDPEFYKW TQWIFLQIFN SWFDAEQQKA
RPISELIPLL ESGELKTKDG ADYNALGDVE KQKAVDDYRL VYRSNSTVNW CPGLGTVLAN
EEVTADGRSE RGNFPVFRKN LSQWMMRITA YSDRLIDDLE LLDWTEKVKS MQRNWIGRSR
GAEVDFSAEG ETVTVFTTRP DTLFGATYMV LAPEHELVDV LLEKAGSYEG VDARWTNGQA
SPAEAVAAYR ASIAAKSDLE RQENKEKTGV FLGVYATNPV NGDQITVFIA DYVLTGYGTG
AIMAVPAHDE RDYEFATVLG LPIKEVVAGG NIEEAAFTES GEAVNSANDN GLDINGLAKD
EAIAKTIEWL EEKELGRGTI QYKLRDWLFA RQRYWGEPFP IVYDENGQAH ALPDSMLPVE
LPEVEDYKPV SFDPEDADSE PSPPLAKARE WVEVELDLGD GKKKYTRDTN VMPQWAGSSW
YQLRYVDPSN DEQFCNIENE RYWTGPRPET HGPNDPGGVD LYVGGVEHAV LHLLYARFWH
KVLFDLGHVS SKEPYRRLYN QGYIQAFAYT DSRGVYVPAD DVEEKDGKFF YQGEEVNQEY
GKMGKSLKNA VAPDDICNNF GADTLRVYEM AMGPLDTSRP WATKDVVGAQ RFLQRLWRLV
VDENTGEVLT RDEVLTDDDN KQLHRTIAGV RDDYTNLRVN TVVAKLIEYV NYLTKTYPDT
IPAGAVLPLI VMVSPIAPHI AEELWKKLGH DDTVTYEPFP TFEEKWLTDD EIELPVQVNG
KVRGRITVAA DASQEQVIEA ALADEKVQEQ ISGKNLIKQI VVPGRMVNLV VK
