ID T0HRE8_9SPHN Unreviewed; 837 AA.
AC T0HRE8;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 55.
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 ECO:0000313|EMBL:EQB00134.1};
GN ORFNames=L485_14525 {ECO:0000313|EMBL:EQB00134.1};
OS Sphingobium baderi LL03.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1114964 {ECO:0000313|EMBL:EQB00134.1, ECO:0000313|Proteomes:UP000015524};
RN [1] {ECO:0000313|EMBL:EQB00134.1, ECO:0000313|Proteomes:UP000015524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LL03 {ECO:0000313|EMBL:EQB00134.1,
RC ECO:0000313|Proteomes:UP000015524};
RX PubMed=24051322;
RA Kaur J., Verma H., Tripathi C., Khurana J.P., Lal R.;
RT "Draft Genome Sequence of a Hexachlorocyclohexane-Degrading Bacterium,
RT Sphingobium baderi Strain LL03T.";
RL Genome Announc. 1:e00751-13(2013).
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:EQB00134.1}.
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DR EMBL; ATIB01000071; EQB00134.1; -; Genomic_DNA.
DR RefSeq; WP_021245537.1; NZ_KQ130471.1.
DR AlphaFoldDB; T0HRE8; -.
DR PATRIC; fig|1114964.3.peg.2846; -.
DR eggNOG; COG0495; Bacteria.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000015524; 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}; Reference proteome {ECO:0000313|Proteomes:UP000015524}.
FT DOMAIN 40..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..575
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 612..651
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 683..801
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 613..617
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 616
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 837 AA; 93167 MW; 8ED3BCFECA1C1AC9 CRC64;
MQRRFNPLEA DARWQAVWDE KQTFRASDSS GKPRSYVLEM FPYPSGRIHI GHVRNYSMGD
VLARFRRMTG HEVLHPMGWD AFGMPAENAA MEKKVHPGEW TRSNIANMRA QLKKLGFAID
WSRELATCEP DYYGHEQALF LDMLEAGLVY RKESAVNWDP VDMTVLANEQ VIDGRGWRSG
ALVEKRKLSQ WFLKITQFAD DLLEGLKTLD QWPDKVRTMQ ENWIGKSVGL QFRFQPVAPF
DTEIEVYSTR PDTIFGASFV AIAADHPVAQ AVAAGNAEAA AFIETCKAGG TTAAELETAE
KLGFDTGLSV VHPFDPEWKL PVFIANFVLM DYGTGAVMGV PAHDQRDLDF ARKYMLAVER
VVAAEGDEAK PIQNEAYVGP GRLVNSRFLD GMGVEEAKAE VIRRAEEGGW GAGQTVFRLR
DWGVSRQRYW GTPIPVIHCD DCGVVGVPKD QLPVTLPEDV SFDIPGNPLD RHPTWKHVDC
PQCGKPARRE TDTLDTFADS SWYFIRFASQ PKDRPFDRET VEKWLPVGQY IGGVEHAILH
LLYARFWTRA LQHMGQLGFA EPFTGLFTQG MVTHETYKAG DGSWLSPGEV KKSGDDYVHI
ESGAPVTVGR VEKMSKSKKN VVDPDDIIAQ YGADAVRWFM LSDSPPERDL PWTESGIEGS
WRFVNRLWRL FGEADKGAEG QDKPLDRKLH QTIDGIARDI EALSFNKAVA KIYELANAVE
KAKPSASRSA AIRTLALLVA PMTPHLAEDA WAAMGEEGLI ADAPWPAVDP ALLVDDEVTI
ACQVMGKLRD TITVPKGTPK EELEKLALAA PNVARTLDGA TPKKVIVVPD RLVNLVI
//
