ID A9CUN8_HOEPD Unreviewed; 876 AA.
AC A9CUN8;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 91.
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=HPDFL43_18647 {ECO:0000313|EMBL:EDQ35242.1};
OS Hoeflea phototrophica (strain DSM 17068 / NCIMB 14078 / DFL-43).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Hoeflea.
OX NCBI_TaxID=411684 {ECO:0000313|EMBL:EDQ35242.1, ECO:0000313|Proteomes:UP000004291};
RN [1] {ECO:0000313|EMBL:EDQ35242.1, ECO:0000313|Proteomes:UP000004291}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DFL-43 {ECO:0000313|EMBL:EDQ35242.1,
RC ECO:0000313|Proteomes:UP000004291};
RA Wagner-Dobler I., Ferriera S., Johnson J., Kravitz S., Beeson K.,
RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDQ35242.1, ECO:0000313|Proteomes:UP000004291}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DFL-43 {ECO:0000313|EMBL:EDQ35242.1,
RC ECO:0000313|Proteomes:UP000004291};
RA Fiebig A.;
RL Submitted (JUN-2012) 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: 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:EDQ35242.1}.
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DR EMBL; ABIA03000005; EDQ35242.1; -; Genomic_DNA.
DR RefSeq; WP_007199473.1; NZ_CM002917.1.
DR AlphaFoldDB; A9CUN8; -.
DR STRING; 411684.HPDFL43_18647; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_5; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000004291; 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 CDD; cd07958; Anticodon_Ia_Leu_BEm; 1.
DR CDD; cd00812; LeuRS_core; 1.
DR Gene3D; 2.20.28.290; -; 1.
DR Gene3D; 3.10.20.590; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 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; 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:UP000004291}.
FT DOMAIN 38..172
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 222..412
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 431..607
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 631..671
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 717..838
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 43..53
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT MOTIF 632..636
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 635
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 876 AA; 97663 MW; 943222CE0AEAA2DB CRC64;
MAIERYNPKQ AEIRWQRQWD EAKIYETDND SPDPKYYVLE MFPYPSGRIH MGHVRNYALG
DVVARYKRAR GFNVLHPMGW DAFGMPAENA AMQNKVHPRE WTYANIDAMR KQLKSMGLSL
DWSREFATCD VDYYKQQQAL FLDFLAAGLI YRRNSKVNWD PVDMTVLANE QVIDGRGWRS
GALVEQRELT QWFFRISDFA EDLLQSLDGL DQWPEKVRLM QKNWIGKSEG LSLRWQIADP
ETAGGASEIE VYTTRPDTLY GASFMAIAAD HPIAKDLATK DPAIAEFCDQ CRRAGTSLAA
LETAEKIGYR TPVNVVHPLD PDWTVPVYIA NFVLMDYGTG AIFGCPSGDQ RDLDFARKYN
LPVTPVVMPA DADAASFVIT DEAYVGDGVM INSRDLDGLS PAEAFDRVAS MLEARTLDDA
PQAARKTNFR LRDWGLSRQR YWGAPIPVIH CDICGVVPVP AKDLPVQLPD DVTLDTPGNP
LDHHPTWRHI ACPTCGQDAR RETDTMDTFV DSSWYFARFT APRCDTPTEP AAANAWLPVD
QYIGGIEHAI LHLLYSRFFT RAMQKTGHVD LKEPFRGLFT QGMVVHETYR AERDGKKEWI
APADVIIEEQ NGKRQARHSQ TGESLSIGSI EKMSKSKKNV VDPDDIIDGY GADTARFFML
SDSPPDRDVI WSEAGVEGAH RFVQKIWRLI GEASENLKSA EAAAGAESRA LEVSRASHKT
VKAVGEDIEK LAFNKAVARL YELVNTLAGP LSDVAAGKAD EVLTSACKQA ASHLVQLFAP
MMPHLAEECW ILLGNDGMVA TSTWPAYDPA LVIDDQITLP VQINGKKRGD LTIDADADQA
AVEQAVLALD FVQASTGGNP PRKLIIVPRR IVNVVI
//
