ID A0A1U7GKE2_9BACT Unreviewed; 962 AA.
AC A0A1U7GKE2;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=BGO49_05150 {ECO:0000313|EMBL:OJW20285.1};
OS Planctomycetales bacterium 71-10.
OC Bacteria; Planctomycetota; Planctomycetia; Planctomycetales.
OX NCBI_TaxID=1895807 {ECO:0000313|EMBL:OJW20285.1, ECO:0000313|Proteomes:UP000185848};
RN [1] {ECO:0000313|EMBL:OJW20285.1, ECO:0000313|Proteomes:UP000185848}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=71-10 {ECO:0000313|EMBL:OJW20285.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-2016) 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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00049}.
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:OJW20285.1}.
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DR EMBL; MKTT01000076; OJW20285.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1U7GKE2; -.
DR STRING; 1895807.BGO49_05150; -.
DR Proteomes; UP000185848; 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 Gene3D; 3.40.50.620; HUPs; 3.
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 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; 2.
DR Pfam; PF13603; tRNA-synt_1_2; 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}.
FT DOMAIN 13..146
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 262..426
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 725..756
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 815..926
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 730..734
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 733
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 962 AA; 108039 MW; 8304266A87CDECB5 CRC64;
MPAYHPQRIE PKWQGYWEQH QTFATPDLDR GRPKLYILDM FPYPSGAGLH VGHPEGYTAT
DIVCRFKRMK GFNVLHPMGW DAFGLPAEQY AVQTNTHPRI TTQANVDNFR RQIKSLGFSY
DWSREVDTTD PGYYKWTQWI FLKIHDTWYD PDFEWADAQG RARRGKGRPI AELPIPEGVD
PVAYRDSKRL AYRAEVPVNW CPALGTVLAN EEVVDGKSER GNHPVVRMPL TQWMLRITAY
GDRLVEDLEI VDWPKSIRDM QRNWVGRSEG AEVDFPVLVG GEAPPRPSGP FPATPAEDVI
RVYTTRPDTL FGATYMVLAP EHPLVDRITT PEQKDAVAKY REQAARKSDL DRTDLAKTKT
GVFTGGHAVN PVTGEPIPVW IADYVLISYG TGAIMAVPAH DDRDFEFAKT FGIPIRAVVE
PPAEWLRANA SPTREEAPAD PAALLAAYKA DPGAFAAVFH DEGVAIQSRN DAFVLDGKPT
AEAKPAITAW LAERGVGKKA VNYKLRDWLF SRQRYWGEPF PVLLDDQDRV TPIGEDELPV
LLPDLDDFKP TGTPEPPLSK AKEWVNYSEA YRREINTMPQ WAGSCWYYLR YIDPKNTERP
WDPEKEKYWL PVDLYVGGAE HAVLHLLYSR FWHKVLFDRG LVSTPEPFQR LVNQGMILGE
TEYTAYRDAA GAWVPAPSVE HADKGPIRKG DATGALLETV KLDDDQVVKK GEGFVIKDAP
EVRIDARAHK MSKSRGNVIN PDVVVNEYGA DSLRLYEMFM GPLEAVKPWS MKGVEGVYRF
LGRAWRMVVD YEAEEVVLDP RVTDAPPTPD QAKLIARTVA AVGDDYEALR FNTAVSRLME
FVNAFTGAEV RPKAAMETFT LLLAPMAPHL AEELWQILGH ESTLAYEPWP AFDPALLKDD
EVEIPVQILG KLRGKITVPA DADQQAIEAL ARGDARIAAL LEGKTVRKVI VVPGKLINFV
AN
//
