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Database: UniProt
Entry: A0A0R0MHX7_9BURK
LinkDB: A0A0R0MHX7_9BURK
Original site: A0A0R0MHX7_9BURK 
ID   A0A0R0MHX7_9BURK        Unreviewed;       897 AA.
AC   A0A0R0MHX7;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 43.
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:KRH98735.1};
GN   ORFNames=AO057_04390 {ECO:0000313|EMBL:KRH98735.1};
OS   Curvibacter sp. PAE-UM.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Curvibacter.
OX   NCBI_TaxID=1714344 {ECO:0000313|EMBL:KRH98735.1, ECO:0000313|Proteomes:UP000051912};
RN   [1] {ECO:0000313|EMBL:KRH98735.1, ECO:0000313|Proteomes:UP000051912}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PAE-UM {ECO:0000313|EMBL:KRH98735.1,
RC   ECO:0000313|Proteomes:UP000051912};
RA   Ma D.;
RT   "The whole genome sequence of a typical ultramicrobacteria PAE-UM from
RT   river sediment.";
RL   Submitted (SEP-2015) 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:KRH98735.1}.
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DR   EMBL; LKCX01000031; KRH98735.1; -; Genomic_DNA.
DR   RefSeq; WP_057674489.1; NZ_KQ483358.1.
DR   AlphaFoldDB; A0A0R0MHX7; -.
DR   STRING; 1714344.AO057_04390; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000051912; 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-RELATED; 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:UP000051912}.
FT   DOMAIN          38..171
FT                   /note="Methionyl/Leucyl tRNA synthetase"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
FT   DOMAIN          227..420
FT                   /note="Leucyl-tRNA synthetase editing"
FT                   /evidence="ECO:0000259|Pfam:PF13603"
FT   DOMAIN          645..678
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          736..862
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           645..649
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT   BINDING         648
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   897 AA;  100344 MW;  5BED1A7FCA0B410B CRC64;
     MQDKYQHLEV EKAAHSHWVA RDAYRVTEDA GKKKFYACSM LPYPSGKLHM GHVRNYTIND
     MLTRYLRMNG YNVLMPMGWD AFGLPAENAA LKNGVPPAKW TYENIAYMKG QMQAMGLAID
     WSREVATCDP TYYKWNQWLF LKMLEKGIAY RKTQVVNWDP VDQTVLANEQ VIDGRGWRTG
     ALVEKREIPG YYLKITDYAQ ELLDHVQIGN DKATLKGWPE RVRLMQENWI GRSEGVRFAF
     THNIQGEDGQ PIGDGRMYVF TTRADTIMGV TFCAVAPEHP LAQHAAKSNP KLAAFIEDCK
     KGGTTEAELA LRDKEGMPTG LFVKHPLIDE QVEVWVGNYV LMSYGDGAVM GVPAHDERDF
     AFALKYQLPI RQVVHVDGEH YDYHHWHEWY ADKAKGVTIN SDTFSGLAYA EAVNAVAHAL
     QVRGLGEKKT TWRLRDWGVS RQRYWGTPIP IIHCEEHGAV PVPEKDLPVV LPQDCIPDGS
     GNPLHKHEDF HAGVVCPVCG KPARRETDTM DTFVDSSWYY MRYCDPANPD KMVADGAQYW
     MPMDQYIGGI EHAILHLLYA RFWTKVMRDL GLVKVDEPFT KLLTQGMVLN HIYSRRTDKG
     GKEYYWPHDV EHVLDAGGKI TGARLNKAVG GLPSGTAIDY EGVGTMSKSK NNGVDPQDLI
     EKYGADTARL YTMFTAPPEA TLEWNDAAVE GSYRFLRRVW NFGVKLSGLD HTTALASVAG
     VKKLKDVSFG KEAKALRLEI HSVLKQVDYD YQRMQYNTVV SGAMKLLNAL EDFKAAGTPG
     AEVALIEGFG ILLRCIYPAT PHITHALWSE LGYAGVLGEL LDAPWPQVDE SALQQDEIEL
     MLQINGKLRG AILVPAGASK EAIEAIAVAS EPVQTQAEGG AIKRVIVVPG RLVNVVV
//
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