SYL_SHEAM
ID SYL_SHEAM Reviewed; 859 AA.
AC A1S8S8;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 03-AUG-2022, entry version 94.
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=Sama_2582;
OS Shewanella amazonensis (strain ATCC BAA-1098 / SB2B).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=326297;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1098 / SB2B;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Fredrickson J.,
RA Richardson P.;
RT "Complete sequence of Shewanella amazonensis SB2B.";
RL Submitted (DEC-2006) 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: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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABM00785.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000507; ABM00785.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041409865.1; NC_008700.1.
DR AlphaFoldDB; A1S8S8; -.
DR SMR; A1S8S8; -.
DR STRING; 326297.Sama_2582; -.
DR PRIDE; A1S8S8; -.
DR EnsemblBacteria; ABM00785; ABM00785; Sama_2582.
DR KEGG; saz:Sama_2582; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_6; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000009175; 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 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; Reference proteome.
FT CHAIN 1..859
FT /note="Leucine--tRNA ligase"
FT /id="PRO_0000334812"
FT MOTIF 42..52
FT /note="'HIGH' region"
FT MOTIF 618..622
FT /note="'KMSKS' region"
FT BINDING 621
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 859 AA; 96507 MW; E62046CFEC2DE27D CRC64;
MQEQYIHSEI EAEVQKYWAD NKTFEVTEDP AKEKFYCLSM FPYPSGRLHM GHVRNYTIGD
VVARFQRLQG KNVLQPIGWD AFGLPAENAA IKNATAPAPW TYENIDYMKN QLKMLGFGYD
WSREIATCTP EYYRWEQWFF TKLYEKGLVY KKTSAVNWCP NDQTVLANEQ VQDGCCWRCD
TPVEQKEIPQ WFIKITAYAE ELLNDIDNLE GWPEQVKTMQ RNWIGRSEGV EMTFKVKDSD
DSFDIYTTRP DTVMGVTYVA IAAGHPLAEK AALNNPELAA FVEECKQSGT SEAELATMEK
KGVATGLYAI HPLTGEEVPV WAANFVLMNY GTGAVMSVPA HDQRDYEFAK KYGLALKAVI
KPADGEVDIS EAAYTEKGVL FNSAEFDGLD FDGAFNAIAD KLAAEGKGKR QVNFRLRDWG
VSRQRYWGAP IPMVTLEDGT VMPTPEDQLP VILPEDVVMD GVQSPIKADK EWAKTQVNGQ
DALRETDTFD TFMESSWYYA RYCSPKANEM LDPAKANYWL PVDQYIGGIE HACMHLLYFR
FFHKLLRDAG LVNSNEPAKR LLTQGMVLAD AFYYNNEKGA RVWVSPLDVT VVEKDDKGRI
LKAVDTEGHE LVYTGMSKMS KSKNNGIDPQ VMVEKYGADT VRLFMMFASP PELTLEWQES
GVEGAHRFIK RLWKLASEYS AAPATEALDV SALNADQKTL RRELHKTIAK VTDDLGRRQM
FNTAVAAVME LMNHLQKAPL ASAQDKALMN EALSAVVRLL YPIAPHVCFN LWRELGNSGA
IEDAGWPATD ESALVEDSKL IVVQVNGKVR AKLTVAADAT KEQVEALGLA EDAVRKYTDG
VTVRKVIYVP GKLLNIVAN