SYL_XANAC
ID SYL_XANAC Reviewed; 880 AA.
AC Q8PIW4;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Leucine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00049};
DE EC=6.1.1.4 {ECO:0000255|HAMAP-Rule:MF_00049};
DE AltName: Full=Leucyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00049};
DE Short=LeuRS {ECO:0000255|HAMAP-Rule:MF_00049};
GN Name=leuS {ECO:0000255|HAMAP-Rule:MF_00049}; OrderedLocusNames=XAC2781;
OS Xanthomonas axonopodis pv. citri (strain 306).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=190486;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=306;
RX PubMed=12024217; DOI=10.1038/417459a;
RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT specificities.";
RL Nature 417:459-463(2002).
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:0000255|HAMAP-Rule:MF_00049};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00049}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00049}.
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DR EMBL; AE008923; AAM37626.1; -; Genomic_DNA.
DR RefSeq; WP_011051821.1; NC_003919.1.
DR AlphaFoldDB; Q8PIW4; -.
DR SMR; Q8PIW4; -.
DR STRING; 190486.XAC2781; -.
DR EnsemblBacteria; AAM37626; AAM37626; XAC2781.
DR GeneID; 66911870; -.
DR KEGG; xac:XAC2781; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_6; -.
DR OMA; TFMVLAP; -.
DR Proteomes; UP000000576; 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 Gene3D; 3.40.50.620; -; 2.
DR Gene3D; 3.90.740.10; -; 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; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR PANTHER; PTHR43740; PTHR43740; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 3.
DR Pfam; PF13603; tRNA-synt_1_2; 1.
DR PRINTS; PR00985; TRNASYNTHLEU.
DR SUPFAM; SSF47323; SSF47323; 1.
DR SUPFAM; SSF50677; SSF50677; 1.
DR TIGRFAMs; TIGR00396; leuS_bact; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1..880
FT /note="Leucine--tRNA ligase"
FT /id="PRO_0000152120"
FT MOTIF 46..56
FT /note="'HIGH' region"
FT MOTIF 638..642
FT /note="'KMSKS' region"
FT BINDING 641
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 880 AA; 98506 MW; 69F65F9BE39D95FD CRC64;
MSTVEPNVYD PQQVETSAQQ FWDATRAFQV DENSEKPKFY CLSMLPYPSG ALHMGHVRNY
TISDVVSRYK RMTGHNVLQP MGWDAFGLPA ENAAIKNKTA PAKWTYANIE HMRAQLKSLG
YAIDWSREFA TCTPDYYVHE QRMFTRLMRK GLAYRRNAVV NWDPIDQTVL ANEQVIDGRG
WRSGAVVEKR EIPQWFLRIT DYAQELLDGL DQLDGWPDSV KTMQRNWIGR SEGLEIQFDV
RDPDGATLDP LRVFTTRPDT LMGVTFVSIA AEHPLALHAA KSNPELAALL ETLKHGGVSE
AELETQEKRG MATGLTAVHP ISGEQVPVWV ANFVLMGYGT GAVMAVPGHD QRDFEFANKY
GLPIVQVVKL REPRNEEEQT WDATHWRDWY TDKSRELELI NSAEFDGLDF GGAFEALAER
FERKGQGQRR VNYRLRDWGV SRQRYWGCPI PVIYCAKCGA VPVPEDQLPV VLPENVEFSG
TGSPIKTDPT WRQTTCPDCG GPAERETDTF DTFMESSWYV ARYTSPKARD MVDRRANYWM
PADLYVGGIE HAILHLMYFR FYHKLMRDAR LVDSDEPVTN LLTQGMVIAD TFYRDADNGG
KDWINPADVE IQRDERGRVT GAVLIADGQP VQIGGTEKMS KSKNNGVDPQ SMVAKYGADT
VRLFSMFAAP PEQSLEWNEA GVDGMARFMR RLWAQVHKHV GEGTAVALDV AALSAEQKAI
RRKTHETIGK VGDDYGRRHS FNTAIAAVME LSNALAKFDD ASEQGRAVRQ EALEAMVLLL
NPITPHASHA LWQVLGRGET LLENVAFPQA DASALVRDAL TLAVQINGKL RGTIDVAADA
TREQIEALAQ AEPNAAKFLE GLSVRKIIIV PGKIVNIVAG
