ID A3WHB8_9SPHN Unreviewed; 835 AA.
AC A3WHB8;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 97.
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 ECO:0000313|EMBL:EAQ28695.1};
GN ORFNames=NAP1_13888 {ECO:0000313|EMBL:EAQ28695.1};
OS Erythrobacter sp. NAP1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX NCBI_TaxID=237727 {ECO:0000313|EMBL:EAQ28695.1, ECO:0000313|Proteomes:UP000002995};
RN [1] {ECO:0000313|EMBL:EAQ28695.1, ECO:0000313|Proteomes:UP000002995}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NAP1 {ECO:0000313|EMBL:EAQ28695.1,
RC ECO:0000313|Proteomes:UP000002995};
RX PubMed=21952547; DOI=10.1128/JB.05845-11;
RA Koblizek M., Janouskovec J., Obornik M., Johnson J.H., Ferriera S.,
RA Falkowski P.G.;
RT "Genome Sequence of the Marine Photoheterotrophic Bacterium Erythrobacter
RT sp. Strain NAP1.";
RL J. Bacteriol. 193:5881-5882(2011).
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:EAQ28695.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAMW01000002; EAQ28695.1; -; Genomic_DNA.
DR RefSeq; WP_007165901.1; NZ_CH672390.1.
DR AlphaFoldDB; A3WHB8; -.
DR STRING; 237727.NAP1_13888; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_5; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000002995; 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; 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:UP000002995}.
FT DOMAIN 41..172
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 222..403
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 417..573
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 611..650
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 680..797
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 611..615
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 614
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 835 AA; 93289 MW; 5FED0E0817A415EA CRC64;
MTDTRFDPST ADGRWQAAWE KAGTFTANSD SDKPKSYILE MFPYPSGRIH MGHVRNYTMG
DVLARYKAMR GFEVLHPMGW DAFGMPAENA AMEKKVHPGE WTYANIEAMK AQLKRIGFAL
DWTREFATCD AEYYGHEQAL FLDMYEAGLV YRRSSEVNWD PVDMTVLANE QVIDGKGWRS
GAEVEKRKLD QWFLKITDFA QGLLDGLDEL EDWPDKVKLM QENWIGKSSG LEFSFDLSNG
EKLPVYTTRP DTIFGASFVA VAADHPVAQG LAGDPEVAAF IEECKRGGTT AAALETAEKL
GYRTEITARH PFTGEAMPLF IANFVLMDYG TGAVMGVPGH DQRDFEFATK YELPIQRVVA
RDASEADAPM GNEAESGDGV IVNSDFLDGQ SVEDAKAEVI RRAEEGDWGK GTTVWRLRDW
GISRQRYWGT PIPFIHCDEC GIVPVPKDQL PVKLPEDVDF ETPGNPLERH ATWKHVDCPK
CGGKATRETD TLDTFTNSSW YFLRFASQPA DAPFDPEEIA KWMPVQHYIG GIEHAILHLL
YARFWTRALA HIGKLDVKEP FASLFTQGMV THETYRLADR GWLSPAEVRI EGEKAFSLDG
GEEVERGRVV KMSKSKKNVV DPDNIIDEYG ADAVRWFMLS DSPPERDLPW SEAGIEGCWR
FVQRLWRLFD QIDESATGED KSLARKAHQA IVAVAEDIEA LSFNKAVARI YELTGAAEKA
APSESRNFAI RTILHLIAPM MPHLAEEAYA KLGADGLLAD AAWPEHDPAM LVEDEVTIAI
QHKGKLRDTL TAPKGASKED LEALALASEK VQRSLDGAQV RKVIVVPDRL VNIVT
//
