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Database: UniProt
Entry: H8L6I9_FRAAD
LinkDB: H8L6I9_FRAAD
Original site: H8L6I9_FRAAD 
ID   H8L6I9_FRAAD            Unreviewed;       881 AA.
AC   H8L6I9;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2012, sequence version 1.
DT   27-MAR-2024, entry version 67.
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   OrderedLocusNames=Fraau_1559 {ECO:0000313|EMBL:AFC85978.1};
OS   Frateuria aurantia (strain ATCC 33424 / DSM 6220 / KCTC 2777 / LMG 1558 /
OS   NBRC 3245 / NCIMB 13370) (Acetobacter aurantius).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Frateuria.
OX   NCBI_TaxID=767434 {ECO:0000313|EMBL:AFC85978.1, ECO:0000313|Proteomes:UP000005234};
RN   [1] {ECO:0000313|Proteomes:UP000005234}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33424 / DSM 6220 / KCTC 2777 / LMG 1558 / NBRC 3245 /
RC   NCIMB 13370 {ECO:0000313|Proteomes:UP000005234};
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Teshima H.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA   Woyke T., Wu D., Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Frateuria aurantia DSM 6220.";
RL   Submitted (FEB-2012) 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; CP003350; AFC85978.1; -; Genomic_DNA.
DR   RefSeq; WP_014402983.1; NC_017033.1.
DR   AlphaFoldDB; H8L6I9; -.
DR   STRING; 767434.Fraau_1559; -.
DR   KEGG; fau:Fraau_1559; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_6; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000005234; Chromosome.
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   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:UP000005234}.
FT   DOMAIN          52..184
FT                   /note="Methionyl/Leucyl tRNA synthetase"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
FT   DOMAIN          234..422
FT                   /note="Leucyl-tRNA synthetase editing"
FT                   /evidence="ECO:0000259|Pfam:PF13603"
FT   DOMAIN          436..591
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          719..844
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
FT   MOTIF           55..65
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT   MOTIF           639..643
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT   BINDING         642
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   881 AA;  97898 MW;  09915E50290832F5 CRC64;
     MHEQNDQVSA TTANESAYAP GAVEQAAQQY WEAERAYEVT ESDPRPKFYC LAMLPYPSGA
     LHMGHVRNYT IADVISRHQR MNGRNVLQPM GWDAFGLPAE NAAIKHKTAP AAWTYQNIEH
     MRGQLKSLGY AIDWTREVTT CKPDYYRWEQ LMFTRLMKKG LAYRRNSVVN WDPVDQTVLA
     NEQVIDGRGW RSGAVVEKRE IPQWFLKITD YAQELLDGLD TLDGWPESVK TMQRNWIGRS
     EGLEIEFAVE GEAEPLSVFT TRPDTLMGVS FVSIAGEHPL ALKAAETRPE LAAFLADLRQ
     GGVSEAELET QEKRGMATGL FAIHPVSGEP VPIWVANFVL MGYGTGAVMA VPGHDERDHA
     FALKYALPIR QVVAVEGESE YDAAQWQAWY GDKTRAGLRL VNSGELDGLD HRAAFDQLAT
     RLEAAGKGRR QVNWRLRDWG VSRQRYWGCP IPVIYCPSCG AVPVPEDQLP VVLPEDVAFS
     GVQSPIKADP EWRKTSCPQC GGAAERETDT FDTFMESSWY YARYTSPGAS DLVDERANHW
     LPVDQYIGGI EHAILHLLYF RFYHKLMRDE GLVKSDEPAT RLLTQGMVIA ETYYRHEANG
     GKTWFNPADV IVQRDDRGRI TGAVLAGDGL PVEVGGVEKM SKSKNNGVDP RAMVERFGAD
     TVRLFSMFAA PPEQSLEWNE AGVEGMARFL KRVWRDASAH AANGPHAVLD AAALDAGAKT
     LRRQTHETIQ KVSDDLGRRQ SFNTAIAALM ELTNALAKYD GQGAQADAVR QEAYETLVLL
     LNPITPHFSH ALWQVLGYAE RILDDQPWPV VDSAALVRDS LTLAVQVNGK LRATIEVAAQ
     AGREVIEPLA LAHPQVQLFL EGLTIRKVIV VPGKIVNIVA G
//
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