SYL_ALKMQ
ID SYL_ALKMQ Reviewed; 824 AA.
AC A6TQK3;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=Amet_2314;
OS Alkaliphilus metalliredigens (strain QYMF).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Alkaliphilus.
OX NCBI_TaxID=293826;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QYMF;
RX PubMed=27811105; DOI=10.1128/genomea.01226-16;
RA Hwang C., Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina Del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F.,
RA Land M.L., Hauser L., Kyrpides N., Mikhailova N., Ye Q., Zhou J.,
RA Richardson P., Fields M.W.;
RT "Complete genome sequence of Alkaliphilus metalliredigens strain QYMF, an
RT alkaliphilic and metal-reducing bacterium isolated from borax-contaminated
RT leachate ponds.";
RL Genome Announc. 4:0-0(2016).
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; CP000724; ABR48471.1; -; Genomic_DNA.
DR RefSeq; WP_012063446.1; NC_009633.1.
DR AlphaFoldDB; A6TQK3; -.
DR SMR; A6TQK3; -.
DR STRING; 293826.Amet_2314; -.
DR EnsemblBacteria; ABR48471; ABR48471; Amet_2314.
DR KEGG; amt:Amet_2314; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_9; -.
DR OMA; TFMVLAP; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000001572; 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; 2.
DR Pfam; PF08264; Anticodon_1; 1.
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..824
FT /note="Leucine--tRNA ligase"
FT /id="PRO_1000091285"
FT MOTIF 40..50
FT /note="'HIGH' region"
FT MOTIF 580..584
FT /note="'KMSKS' region"
FT BINDING 583
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 824 AA; 95056 MW; 7CAF3459E6CB80F7 CRC64;
MAIYDFGNIE KKWQERWQEN KAFSIIERDR PKYYVLEMFP YPSGKIHMGH VRNYSIGDVV
ARFKRMKGYN VLHPMGWDSF GLPAENAAIK HGIHPDHWTK ENVKEMKEQL DALGLSYDWD
REVSTCTPEY YKWTQWLFLQ FYHKGLAYKK ESQVNWCPSC ETVLANEQVV NGGCDRCDSS
VGKKNLNQWY FKITDYAEAL LEDIKLLDGW PEKVKTMQQN WIGKSHGAEI DFPIENTSKE
LKVFTTRPDT IYGATYMVLA PEHPYVMELV KETEYEEAVV AFRNKLQHMS DIERTSTEIE
KEGIFIGKYC INPVSNEKIP IYIANYVLAD YGTGAIMAVP AHDQRDLDFA RKYDITVTPV
IRPIDESDGF DIEKEAYTDS GIMINSEKFN GLDSEKAYED IAKHIETLNA GKRTINYRLR
DWLLSRQRYW GTPIPIIYCD DCGIVPVREE ELPVKLPVDV TFSGKGSSPL ETSEGFLNTN
CPSCGKMAKR ETDTMDTFVD SSWYFLRYTD ANNEQLPFSK EAANYWVPVD QYIGGVEHAI
LHLLYSRFFT KVMKDLGLTD QPEPFKKLLT QGMVLKDGAK MSKSKGNVVS PEEIIQKYGA
DTARLFVLFA APPERDLEWS DQGVEGSYRF LNRVWRLAEE FIDNNLFMST SLGEALTKRD
KDLKYTIHYT IKKVTSDVED RFNFNTAISA VMELINELYK YKETDPSKLN GDLFREGIET
SILLLAPFAP HFTEELWEKL GKAESVHMTN WPEYDHEAII KDEVEIVMQV NGKVKDRMMV
PTNVSKEELE SLAMKNEKII QIIEGKQIIK IIAVPKKLVN IVIK