SYL_GLOC7
ID SYL_GLOC7 Reviewed; 854 AA.
AC B7KCI7;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-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};
GN OrderedLocusNames=PCC7424_1860;
OS Gloeothece citriformis (strain PCC 7424) (Cyanothece sp. (strain PCC
OS 7424)).
OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC Aphanothecaceae; Gloeothece; Gloeothece citriformis.
OX NCBI_TaxID=65393;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7424;
RX PubMed=21972240; DOI=10.1128/mbio.00214-11;
RA Bandyopadhyay A., Elvitigala T., Welsh E., Stockel J., Liberton M., Min H.,
RA Sherman L.A., Pakrasi H.B.;
RT "Novel metabolic attributes of the genus Cyanothece, comprising a group of
RT unicellular nitrogen-fixing Cyanobacteria.";
RL MBio 2:E214-E214(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; CP001291; ACK70292.1; -; Genomic_DNA.
DR RefSeq; WP_012599235.1; NC_011729.1.
DR AlphaFoldDB; B7KCI7; -.
DR SMR; B7KCI7; -.
DR STRING; 65393.PCC7424_1860; -.
DR PRIDE; B7KCI7; -.
DR EnsemblBacteria; ACK70292; ACK70292; PCC7424_1860.
DR KEGG; cyc:PCC7424_1860; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_3; -.
DR OMA; TFMVLAP; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000002384; 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..854
FT /note="Leucine--tRNA ligase"
FT /id="PRO_1000199189"
FT REGION 586..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 42..52
FT /note="'HIGH' region"
FT MOTIF 615..619
FT /note="'KMSKS' region"
FT BINDING 618
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 854 AA; 96892 MW; E7E26E0AA0BBCC43 CRC64;
MESVYNAEAI EKKWQQTWVE MGLDQTPEDN TKPKYYALSM FPYPSGNLHM GHVRNYVITD
VIARLKRMQG HRVLHPMGWD AFGLPAENAA IERGIHPAKW TYQNIAQMRQ QLQQLGLSID
WSREVTTCSP DYYQWTQWLF LQFFQAGLAY QKEAAVNWDP VDQTVLANEQ VDSEGKSWRS
GAKVERKMLR QWFLKITDYA EQLLNDLDKL PGWPEKVKLM QANWIGKSIG AYLEFPIVGM
DEKIAVFTTR PDTVYGVTYV VLAPEHPLTP KVTTAKNKKA VEKFIKEVTS ESEQERTAED
KPKKGILTGG KAINPFNGQE VPILIANYVL YEYGTGAVMG VPAHDIRDFK FAQENKLPIR
VVIVPEDQQD QDVTLTQAYT EPGIMVNSGS FDGMDSITGK TAIIDYAEKQ GFGKARVQYR
LRDWLISRQR YWGCPIPVIH CPSCGTVPVP DEDLPVKLPE DVEFSGRGAS PLAKLDSWIN
VPCPSCGEPA KRETDTMDTF IDSSWYFLRY TDANDQQTAF SLDKVNDWMS VDQYVGGVEH
AILHLLYSRF FTKVVRDRGL VDVDEPFQRL LTQGMVQGMT YKNPKTGKYI PSSQVNPEDP
KDPETGEPLS VFYEKMSKSK YNGVDPKQVL AKYGADTARM FILFKAPPEK DLEWDDADVE
GQFRFLNKVW RIVGEYQSNH KSSSKKKGSL TKVEKDLRRA IHIAIKEITE DLDGEYQFNT
AVSELMKLSN ALVDAKCYES PVYTEGVQTL LILLAPFAPH IAEELWHTLG HSESVHLQGW
PQLDPSALEV DEITLVIQIM GKTRGTIQVP SSATKEELEK FAFESEVAQR HLKDQEVKKV
IVVPGKLVNF VVGK
