ID SYL_PROMA Reviewed; 870 AA.
AC Q7VBZ5;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 27-MAR-2024, 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=Pro_0947;
OS Prochlorococcus marinus (strain SARG / CCMP1375 / SS120).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC Prochlorococcaceae; Prochlorococcus.
OX NCBI_TaxID=167539;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SARG / CCMP1375 / SS120;
RX PubMed=12917486; DOI=10.1073/pnas.1733211100;
RA Dufresne A., Salanoubat M., Partensky F., Artiguenave F., Axmann I.M.,
RA Barbe V., Duprat S., Galperin M.Y., Koonin E.V., Le Gall F., Makarova K.S.,
RA Ostrowski M., Oztas S., Robert C., Rogozin I.B., Scanlan D.J.,
RA Tandeau de Marsac N., Weissenbach J., Wincker P., Wolf Y.I., Hess W.R.;
RT "Genome sequence of the cyanobacterium Prochlorococcus marinus SS120, a
RT nearly minimal oxyphototrophic genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10020-10025(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}.
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DR EMBL; AE017126; AAP99991.1; -; Genomic_DNA.
DR RefSeq; NP_875339.1; NC_005042.1.
DR RefSeq; WP_011125099.1; NC_005042.1.
DR AlphaFoldDB; Q7VBZ5; -.
DR SMR; Q7VBZ5; -.
DR STRING; 167539.Pro_0947; -.
DR EnsemblBacteria; AAP99991; AAP99991; Pro_0947.
DR KEGG; pma:Pro_0947; -.
DR PATRIC; fig|167539.5.peg.996; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_3; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000001420; 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 CDD; cd07958; Anticodon_Ia_Leu_BEm; 1.
DR CDD; cd00812; LeuRS_core; 1.
DR Gene3D; 3.40.50.620; HUPs; 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 NCBIfam; TIGR00396; leuS_bact; 1.
DR PANTHER; PTHR43740:SF2; LEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 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; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 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..870
FT /note="Leucine--tRNA ligase"
FT /id="PRO_0000152063"
FT MOTIF 55..65
FT /note="'HIGH' region"
FT MOTIF 626..630
FT /note="'KMSKS' region"
FT BINDING 629
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 870 AA; 99805 MW; 673DF65DC039FA7C CRC64;
MASKISQTPE KQPSTAYDPL SIETRWQQSW KEQGLYKTKE PTKSQKTFYA LSMFPYPSGT
LHMGHVRNYV ITDVIARLHR MKGDSVLHPM GWDAFGLPAE NAAIERGIPA DIWTYKNIED
MRNQLNRLGL SIDWDKEVTT CKEEYYKWTQ YIFLELYEAG LAYQKSATVN WDPIDKTVLA
NEQVDANGRS WRSGALVEKK KLKQWFLKIT DFADELLEDI ELLSGWPQNV KTMQQNWIGR
SNGTEIDFYI KGKNNIFITV FTTRPDTLHG TEYLVLAPDH ELINSIIDKN KITELEQFRT
EISILTDQER TSDGNNKRGM FLGCHAINPI NKKIIPIWVG EYVLSSYATG AVMGVPAHDK
RDYKFAKKYS LPIQYVIKSP SQEASDLEAS SAYVKEGIMI NSGEFNGINS KEAGFMITKL
GVKQGWAKNK VTYKLRDWLI SRQRMWGCPI PIIYCPDCGS VPVKREELPV KLTNPSVIGK
SQENKNNIPI MKCSKCNKDS ILETDTMDTF MCSSWYFLRY IDVENNKLPF TKTEVDKWLP
VDQYVGGIEH AILHLLYSRF LIKALRNRGL LNIKEPFSNL LTQGMVQGVT FKNPKTSKYI
SPDHINDINT PLDPETGEPL DVLYEKMSKS KYNGVDPASV IDKYGTDTAR MFILFKAPPE
KDLEWDESDV EGQYRFLNRL WRIVIYSIET KDINISNCTQ EILLNDLSDK ERKLIKVLNN
TIKEVTNDLV NDFQFNTAIS ELMILCNSIY ENIDDCGDYI VTETFKKLTL LLAPFAPHIA
EEFWIKLKGK GSVHENSWPT YDPKALLEDS YKLIIQINGK VRGNISVNHE DSELELKNKA
LACETTQKWL NGIEPKRIII VKGKIINIVF
//
