ID A0A1G5PMV0_9GAMM Unreviewed; 855 AA.
AC A0A1G5PMV0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 18-JUN-2025, entry version 34.
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=SAMN03097708_00504 {ECO:0000313|EMBL:SCZ50812.1};
OS Thiohalomonas denitrificans.
OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC Thiohalomonadales; Thiohalomonadaceae; Thiohalomonas.
OX NCBI_TaxID=415747 {ECO:0000313|EMBL:SCZ50812.1, ECO:0000313|Proteomes:UP000199648};
RN [1] {ECO:0000313|EMBL:SCZ50812.1, ECO:0000313|Proteomes:UP000199648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HLD2 {ECO:0000313|EMBL:SCZ50812.1,
RC ECO:0000313|Proteomes:UP000199648};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=tRNA(Leu) + L-leucine + ATP = L-leucyl-tRNA(Leu) + AMP +
CC diphosphate; 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:ARBA00047469, 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; FMWD01000001; SCZ50812.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G5PMV0; -.
DR STRING; 415747.SAMN03097708_00504; -.
DR Proteomes; UP000199648; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0002161; F:aminoacyl-tRNA deacylase 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 FunFam; 3.10.20.590:FF:000001; Leucine--tRNA ligase; 1.
DR FunFam; 3.40.50.620:FF:000003; Leucine--tRNA ligase; 1.
DR FunFam; 3.90.740.10:FF:000012; Leucine--tRNA ligase; 1.
DR FunFam; 1.10.730.10:FF:000011; Leucine--tRNA ligase chloroplastic/mitochondrial; 1.
DR Gene3D; 3.10.20.590; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR Gene3D; 1.10.730.10; Isoleucyl-tRNA Synthetase, Domain 1; 1.
DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
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:UP000199648}.
FT DOMAIN 42..184
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 223..423
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 436..651
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 698..817
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 365..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 44..54
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 COMPBIAS 373..382
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 616
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 855 AA; 95558 MW; B4575FE4EA03EEC2 CRC64;
MALDEQYQPA VIEAEAQQYW QENRCFEVTE DPDKEKFYCL AMFPYPSGRL HMGHVRNYTI
GDVISRYQRM IGKNVLQPMG WDAFGLPAEN AAIKNNVPPA KWTYENIDYM RGQLQRLGFG
YDWKRELATC HPQYYKWEQW LFTRLFKKGL VYKKTSPVNW CPNDLTVLAN EQVIEGRCWR
CDTSVERKEI PQYFMKITAY ADELLAGLDK LDGWPEQVRT MQRNWIGRSE GVEIAFGVEG
RDEPLKVYTT RPDTLMGVSY VAVAPEHPLA IEAATQNSEL AGFIEEAGNL QISEAAMETM
EKKGVDTGLK ALHPISGEPV PIYAANFVLM AYGEGAVMAV PGHDQRDWEF ARKYGLPIKQ
VIKPADDSEA DDAQGSASAA GGRMPGADLT QAAFTDKGIL VDSGEFSNLT SGQAFDAIAE
YLEQRGRGKK RVNYRLRDWG VSRQRYWGCP IPIINCPSCG EVPVPEDQLP VVLPEDVAFD
GIGSPIKKMP EFYETTCPTC GGKAERETDT FDTFMESSWY YARYTCRDND DAMLDERGDY
WLPVDQYVGG IEHAILHLLY ARFYHRLMRD FVGDAQGSAS AAGGRKPGAA LVDSDEPFAN
LLTQGMVLKD GAKMSKSKGN TVDPQDMIAQ YGADTVRLFT MFAAPPEQSL EWNDSGVEGA
YRFLKRLWAF AHEHAEAIGA AAAEQPDREN MADTVKTARR EIHEALAQAR TDFGRYQFNT
VVSACMKVMN ILAKLDDTKG ADVLRREGLG ILLPLLSPTA PHVTHHLWRE LGYGDDILTA
PWPEVDESAL KRDTIDLVVQ VNGKMRGKVQ VSAAADKTSV EATALADENV QRFIEGKEVK
KVIVVPGRLV NVVAT
//
