UniProt: A0A239STR5

Database: UniProt
Entry: A0A239STR5_9BURK

LinkDB:  A0A239STR5_9BURK 
Original site:  A0A239STR5_9BURK

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Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (14)   
   InterPro (9)   
   Pfam (4)   
   PROSITE (1)   
All databases (23)   

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ID   A0A239STR5_9BURK        Unreviewed;       863 AA.
AC   A0A239STR5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
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:SNU88881.1};
GN   ORFNames=SAMEA4530655_04431 {ECO:0000313|EMBL:SNU88881.1};
OS   Pandoraea sputorum.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Pandoraea.
OX   NCBI_TaxID=93222 {ECO:0000313|EMBL:SNU88881.1, ECO:0000313|Proteomes:UP000215126};
RN   [1] {ECO:0000313|EMBL:SNU88881.1, ECO:0000313|Proteomes:UP000215126}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC13161 {ECO:0000313|EMBL:SNU88881.1,
RC   ECO:0000313|Proteomes:UP000215126};
RG   Pathogen Informatics;
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; LT906435; SNU88881.1; -; Genomic_DNA.
DR   RefSeq; WP_039393192.1; NZ_LT906435.1.
DR   AlphaFoldDB; A0A239STR5; -.
DR   STRING; 93222.NA29_00990; -.
DR   KEGG; pspu:NA29_00990; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000215126; Chromosome 1.
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   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          38..171
FT                   /note="Methionyl/Leucyl tRNA synthetase"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
FT   DOMAIN          220..406
FT                   /note="Leucyl-tRNA synthetase editing"
FT                   /evidence="ECO:0000259|Pfam:PF13603"
FT   DOMAIN          420..575
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          622..662
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          706..827
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           623..627
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT   BINDING         626
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   863 AA;  96202 MW;  345D0887A0DE735C CRC64;
     MQEKYVPADV EASAQSHWQA IDAYKTTERA DKQKFYCVSM LPYPSGKLHM GHVRNYTIND
     VMYRQMRMRG YNVLMPMGWD AFGMPAENAA MANGVPPAKW TYDNIDYMKK QMQAMGLAID
     WSREVATCKP EYYRWNQWLF LKMLEKGVVY LKTGTVNWDP IDQTVLANEQ VIDGRGWRSG
     ALVEKREIPM YYMRITEYAD ELLGDLDDLG WPERVKVMQQ NWIGKSFGVN FGFPYELDGE
     QKLLRVFTTR ADTIMGVTFA AIAAEHPLAT RLAADRPDLQ AFIAECKQGG VAEADIATME
     KKGMPTGFFV THPLTGDKVE VWIGNYVLMG YGEGAVMGVP AHDERDFAFA RKYNLPIRQV
     VAVEGETYST DAWQAWYGEK EGTLINSGKY DGLAFAAAID AIAADLKAKG AGDKQVTFRL
     RDWGISRQRY WGTPIPIIHC DTCGAVPVPE KDLPVVLPED LVPDGTGNPL AKSEAFLKCD
     CPKCGKPARR ETDTMDTFVD SSWYFSRYAC PDAETMVDER TNYWMPMDQY IGGIEHAILH
     LLYSRFWTKV MRDLGLVSFK EPAQNLLTQG MVLNETFYRE DTSGKKTWFN PLDVQVQFDD
     KGRPAGATSK ADGADVTLGG IEKMSKSKNN GVDPQSLIDQ YGADTARLFV MFAAPPEQQL
     EWSGAGVEGA SRFLRRLWGF GQSQAALLRQ TDAAIDTANP AAQALRLEIH SVLKQANYDY
     QRVQYNTVVS AAMKMLNAIE SDKGAAGAGA VRECYGILLR VLYPVVPHVT HGLWVELGYA
     AQSGDLLDAS WPEVDEAALV QDEIELVLQV AGKVRGAVRV AKDASREAIE QAALEHEMTA
     KFGEGKPVKK VIVVPGRLVN VVV
//

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