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Database: UniProt
Entry: A0A315AT86_9BURK
LinkDB: A0A315AT86_9BURK
Original site: A0A315AT86_9BURK 
ID   A0A315AT86_9BURK        Unreviewed;       896 AA.
AC   A0A315AT86;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
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=B9Z51_04275 {ECO:0000313|EMBL:PUE11511.1};
OS   Limnohabitans sp. T6-5.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Limnohabitans.
OX   NCBI_TaxID=1100724 {ECO:0000313|EMBL:PUE11511.1, ECO:0000313|Proteomes:UP000251804};
RN   [1] {ECO:0000313|EMBL:PUE11511.1, ECO:0000313|Proteomes:UP000251804}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T6-5 {ECO:0000313|EMBL:PUE11511.1,
RC   ECO:0000313|Proteomes:UP000251804};
RA   Kasalicky V., Mehrshad M., Andrei S.-A., Salcher M., Kratochvilova H.,
RA   Simek K., Ghai R.;
RT   "Unexpected and diverse lifestyles within the genus Limnohabitans.";
RL   Submitted (APR-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}.
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:PUE11511.1}.
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DR   EMBL; NERV01000001; PUE11511.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A315AT86; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000251804; 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; 1.
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:UP000251804}.
FT   DOMAIN          38..171
FT                   /note="Methionyl/Leucyl tRNA synthetase"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
FT   DOMAIN          227..419
FT                   /note="Leucyl-tRNA synthetase editing"
FT                   /evidence="ECO:0000259|Pfam:PF13603"
FT   DOMAIN          649..680
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          738..858
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           649..653
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT   BINDING         652
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   896 AA;  99606 MW;  C49AAFA6154CF070 CRC64;
     MQDKYTHLDV EAAAQARWTA RDAYRVTEDQ SKKKFYACSM LPYPSGKLHM GHVRNYTIND
     MLTRQLRMRG YNVLMPMGWD AFGLPAENAA LKNKVPPAKW TYDNIAYMKK QMQAMGLAID
     WSREVATCDP TYYKWNQWLF LKMLEKGIAY RKTQVVNWDP VDQTVLANEQ VIDGKGWRTG
     APVEKREIPG YYLNITAYAQ ELLDHVQIGN DKATLNGWPD KVRLMQENWI GKSEGVRFAF
     PHSIAGADGA LIGEGKMYVF TTRADTIMGV TFCAVAAEHP LALHAASTNP ALAAFLEECK
     TGGTTEAELA TQEKKGMPTG LFVTHPLTGA QVEVWVGNYV LMSYGDGAVM GVPAHDERDF
     AFALKYALPI QQVVSVKDQA FDDKTWQEWY ADKQNCVCVN SGELDGLTQK AAVIKVAELL
     AAKDLGEKKT TWRLRDWGVS RQRYWGTPIP IIHCEEHGAV PVPEKDLPVV LPQDCIPDGS
     GNPLHKHEGF HAGVTCPVCG KPARRETDTM DTFVDSSWYF MRYCDPNNTE KMVAGGADYW
     MPMDQYIGGI EHAILHLLYA RFWTKVMRDL GLVKVDEPFS KLLTQGMVLN HIYSRRTAKG
     GKDYFWPHDV EHVLDETGKV VGAKLKNEAD SGDGRLPVGT AIDYEGVGTM SKSKNNGVDP
     QDLIEKYGAD TARLYTMFTA PPEVTLEWND AAVEGSYRFL RRVWNFGVKQ EAALKAGIAV
     DRSQAVDFSK AAKALRLDIH TVLKQANYDY ERMQYNTVVS AVMKMLNTLE DVALSESPED
     AAALAEGFSI LLRVLYPACP HIAEQLWTEL GYAACCGELL DVAWPGVDES ALQRDELELM
     LQINGKLRGS ILVPATADKA QIEAAALASE AFVKQAAGAA PKKVIVVPGR LVNIVV
//
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