ID F7P0D5_9GAMM Unreviewed; 862 AA.
AC F7P0D5;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Leucine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00049};
DE EC=6.1.1.4 {ECO:0000256|HAMAP-Rule:MF_00049};
DE AltName: Full=Leucyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00049};
DE Short=LeuRS {ECO:0000256|HAMAP-Rule:MF_00049};
GN Name=leuS {ECO:0000256|HAMAP-Rule:MF_00049};
GN ORFNames=Rhein_3535 {ECO:0000313|EMBL:EGM76473.1};
OS Rheinheimera sp. A13L.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Rheinheimera.
OX NCBI_TaxID=506534 {ECO:0000313|EMBL:EGM76473.1, ECO:0000313|Proteomes:UP000004282};
RN [1] {ECO:0000313|EMBL:EGM76473.1, ECO:0000313|Proteomes:UP000004282}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A13L {ECO:0000313|EMBL:EGM76473.1,
RC ECO:0000313|Proteomes:UP000004282};
RX PubMed=21742876; DOI=10.1128/JB.05636-11;
RA Gupta H.K., Gupta R.D., Singh A., Chauhan N.S., Sharma R.;
RT "Genome Sequence of Rheinheimera sp. Strain A13L, Isolated from Pangong
RT Lake, India.";
RL J. Bacteriol. 193:5873-5874(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:0000256|ARBA:ARBA00001372, ECO:0000256|HAMAP-
CC Rule:MF_00049};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00049}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|HAMAP-Rule:MF_00049,
CC ECO:0000256|RuleBase:RU363035}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGM76473.1}.
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DR EMBL; AFHI01000056; EGM76473.1; -; Genomic_DNA.
DR RefSeq; WP_008900360.1; NZ_AFHI01000056.1.
DR AlphaFoldDB; F7P0D5; -.
DR STRING; 506534.Rhein_3535; -.
DR eggNOG; COG0495; Bacteria.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000004282; Unassembled WGS sequence.
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; 2.20.28.290; -; 1.
DR Gene3D; 3.10.20.590; -; 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 {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_00049};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00049};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00049};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00049};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00049};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00049}.
FT DOMAIN 39..171
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 221..405
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 419..574
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 621..660
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 701..825
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 42..52
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT MOTIF 622..626
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 625
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 862 AA; 97098 MW; 74ED51435A874524 CRC64;
MHEQYNPQLI EQQLQQEWEQ TNAFKVVEDA SKEKFYCLSM FPYPSGRLHM GHVRNYTIGD
VISRFQRMQG KNVMQPMGWD AFGLPAENAA IANKTAPAKW TYANIDYMKG QLKRLGFGYD
WDREVATCKP EYYKWEQWFF TKLFEKGLVF KKMATVNWDP VDQCVLANEQ VIDGRGWRSG
ALVEQRELAQ WFIKITDYAE ELLQDLDQLD DWPEQVKTMQ KNWIGRSEGV EIEFKVADSD
QTMSVYTTRP DTLYGVTYVA VAAQHPLAQQ AAVNNPELQA FIDDCKGGKM AEADMATMEK
KGAPTGLFAI HPLTGEQVPV WVANFVLMHY GSGAVMAVPG HDQRDYEFAT KYGLAIKQVV
QPEAGSTAVC DLTTAAFTEK GVLVNSAEFN GLDFTAAFKA IADKLSAMGI GQVKVNYRLR
DWGVSRQRYW GSPIPMLTLE DGTQVPVPEE MLPVRLPEDV VMNGVTSPIK ADPEWAKTTY
KGQAAFHETD TFDTFMESSW YYARYCSPDH DKAMLDPAKA NYWLPVDQYI GGIEHAILHL
LYARFFHKLL RDVGLVQCDE PFKRLLCQGM VLAETFYRET ENGGKEWFSP ADVATERDEK
GRITASVLKA DGKPVLSAGM SKMSKSKNNG IDPQLVIDQY GADTVRLFMM FTAPPEQTLE
WQDSAVEGAN RFLRRIWTLA SEHKDLFGDA STALELNADQ KALRRDIHKT IAKVSDDIGR
RYTFNTAIAA IMELANKVQK APVDTDADKQ VKREGIQTLI QLLNPFTPHL SQHLWQELGF
SVALEQSPWP VADAAAMVED EKLVVVQING KVRAKVTVSA DATEQQVLEL AHAEENVQRF
LEGVTIRKVI YVPGKLLSLA VG
//
