ID A0A099F5W4_9RHOB Unreviewed; 873 AA.
AC A0A099F5W4;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 44.
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=IT41_05515 {ECO:0000313|EMBL:KGJ05663.1}, SAMN04487972_105133
GN {ECO:0000313|EMBL:SFA47781.1};
OS Paracoccus halophilus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=376733 {ECO:0000313|EMBL:KGJ05663.1, ECO:0000313|Proteomes:UP000029846};
RN [1] {ECO:0000313|EMBL:KGJ05663.1, ECO:0000313|Proteomes:UP000029846}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 14014 {ECO:0000313|EMBL:KGJ05663.1,
RC ECO:0000313|Proteomes:UP000029846};
RA McGinnis J.M., Wolfgang W.J.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KGJ05663.1, ECO:0000313|Proteomes:UP000029846}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 14014 {ECO:0000313|EMBL:KGJ05663.1,
RC ECO:0000313|Proteomes:UP000029846};
RA Mingle L.A., Cole J.A., Lapierre P., Musser K.A.;
RT "Paracoccus sanguinis sp. nov., isolated from clinical specimens of New
RT York State patients.";
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:SFA47781.1, ECO:0000313|Proteomes:UP000182312}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.6117 {ECO:0000313|EMBL:SFA47781.1,
RC ECO:0000313|Proteomes:UP000182312};
RA de Groot N.N.;
RL Submitted (OCT-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}.
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DR EMBL; JRKN01000005; KGJ05663.1; -; Genomic_DNA.
DR EMBL; FOJO01000005; SFA47781.1; -; Genomic_DNA.
DR RefSeq; WP_036739245.1; NZ_JRKN01000005.1.
DR AlphaFoldDB; A0A099F5W4; -.
DR STRING; 376733.SAMN04487972_105133; -.
DR eggNOG; COG0495; Bacteria.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000029846; Unassembled WGS sequence.
DR Proteomes; UP000182312; 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 CDD; cd00812; LeuRS_core; 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; 2.
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:UP000029846}.
FT DOMAIN 34..168
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 219..369
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 427..584
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 650..689
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 718..838
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 39..49
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT MOTIF 650..654
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 653
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 873 AA; 97347 MW; ED4D22761D78084C CRC64;
MPYDPAISEP HWQKAWDDAG SFLARRDERP KYYVLEMFPY PSGRIHMGHV RNYTMGDVVA
RFKRAQGFSV LHPMGWDAFG MPAENAAMEQ GGHPRDWTYG NIATMREQLK PLGLSIDWSR
EFATCDDDYV AQQQALFLDM LEAGLITRKS AQVNWDPVDM TVLANEQVID GKGWRSGAPV
ERKELTQWFF RISDYSEELL AALDGLTGWP DKVRLMQANW IGKSRGLQFH FQTSGAPAGF
DRIEVYTTRP DTLMGASFAA LSPDHPLIRA LAADRPEIAA FVEECRRLGT TEEAIETAPK
MGLDTGLTVR HPLDPNWQLP VWIANFVLMD YGTGAIFGSP AHDERDHEFA TKYGLPIRAT
FGERGMTQEQ ADAMVAKAPY VPLKSETVTY VRGFAGPAEQ TGEDAVIAAI AHAETKGYGE
GVTKYRLRDW GISRQRYWGC PIPVVHCDGC GTVPEAKQNL PVLLPRDVTF DTPGNPLDRH
PTWRRTTCPK CGGAARRETD TMDTFVDSSW YYARFTSPGA ATPTERADAD YWMNVDQYIG
GIEHAILHLL YSRFFARAMV RTGHLPESAK EPFDALFTQG MVTHEIYRIT EKYPVENLAS
DSRAVIKSEF PTAKAIHWPI YYFPEQVEHR PDGVFLKNTN TPVEVIASAK MSKSKKNVVD
PVDIVANFGA DTARWFMLSD SPPERDVEWT AAGAEAAHKF LARVWRLADE VPEGAEDPEL
LRAAHRAIAD VTRSIEGFAF NKAVAKLYEL ANIIGKSPAG GEQRRAALRI MAQLMAPMVP
HLAEEIWSKA GGQGMVVDAA WPQADPALLV SDSVVLPIQI NGKRRAEIQV PKDMPKEEIE
TLVLADETVQ RFMEGAAPKK LIVVPGRIVN VVV
//
