SYL_SYNFM
ID SYL_SYNFM Reviewed; 829 AA.
AC A0LK15;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 101.
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=Sfum_2084;
OS Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales;
OC Syntrophobacteraceae; Syntrophobacter.
OX NCBI_TaxID=335543;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10017 / MPOB;
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., Pitluck S., Goltsman E.G.,
RA Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R.,
RA McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J., Sieber J.,
RA Stams A.J.M., Worm P., Henstra A.M., Richardson P.;
RT "Complete sequence of Syntrophobacter fumaroxidans MPOB.";
RL Submitted (OCT-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}.
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DR EMBL; CP000478; ABK17767.1; -; Genomic_DNA.
DR RefSeq; WP_011698936.1; NC_008554.1.
DR AlphaFoldDB; A0LK15; -.
DR SMR; A0LK15; -.
DR STRING; 335543.Sfum_2084; -.
DR PRIDE; A0LK15; -.
DR EnsemblBacteria; ABK17767; ABK17767; Sfum_2084.
DR KEGG; sfu:Sfum_2084; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_7; -.
DR OMA; TFMVLAP; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000001784; 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; 2.
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; 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..829
FT /note="Leucine--tRNA ligase"
FT /id="PRO_1000009454"
FT MOTIF 42..52
FT /note="'HIGH' region"
FT MOTIF 584..588
FT /note="'KMSKS' region"
FT BINDING 587
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 829 AA; 93354 MW; 5AA680E8AE916D5A CRC64;
MDYKYAPKRI EKKWQEHWER EKLFEVSEIP GREKFYLLEM FPYPSGRIHM GHVRNYSIGD
VVARFLRMRG YNVLHPMGWD AFGMPAENAA IKAKTHPARW TYENIAYMRS QLKQLGFSYD
WSREFATCDV SYYRWEQLFF LKMYEKGLAY KRSAYVNWCG TCLTVLANEQ VEGGACWRCD
QPVVQKEMEQ WFFKITDYVE ELLDYTHRLP GWPERVLTMQ QNWIGKSLGS KLLFPLASGD
GSITVFTTRA DTLFGATFMS LAPEHPLVEG LCRGNPQESE VLRFVQAAKQ AKRNDREAEL
LEKEGVFTGS CCINPVTGAK MPIYVANFVV MEYGTGAVMA VPAHDQRDFE FARKYGLPVK
VVIKPADAAA APAAQELSAA FEDDGVLVDS GAYSGMASAE ARTAITADLA GKGLGEQTVQ
YRLRDWGISR QRYWGAPIPI VYCDKCGTVP VPEKDLPVVL PTDVALLPNG ASPLPAHAPF
LNTDCPRCGG PARRETDTMD TFVESSWYFA RFACARYDQG PLDLPKVKYW MPVDQYIGGI
EHAVLHLLYS RFFVKVLRDM GALEVDEPFR NLLTQGMVIK DGAKMSKSKG NVVDPDDMIK
AYGADTVRLF CLFASPPEKD LEWSDQGVEG SFRFLSRIWR LVSDNLDALR SAPRHNGGGA
LPEPLEALHR KTHQTIKKVT EDIRDRFHFN TAIAAIMELV NQIYQVVEGG SRAGNIWPVV
KEAVEALILL VSPMAPHIAE EIWHELGHTR SVLLEPWPEW SGKALQAEEV MLVVQVNGRL
RSRITVPSDA TPEQMEAAAL ADSRVQEFIA GKPVRKVVVV PKKIINVVV