ID A7IFA1_XANP2 Unreviewed; 894 AA.
AC A7IFA1;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 24-JAN-2024, entry version 111.
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 OrderedLocusNames=Xaut_1446 {ECO:0000313|EMBL:ABS66694.1};
OS Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Xanthobacteraceae; Xanthobacter.
OX NCBI_TaxID=78245 {ECO:0000313|EMBL:ABS66694.1, ECO:0000313|Proteomes:UP000002417};
RN [1] {ECO:0000313|EMBL:ABS66694.1, ECO:0000313|Proteomes:UP000002417}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1158 / Py2 {ECO:0000313|Proteomes:UP000002417};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Hammon N.,
RA Israni S., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D.,
RA Detter J.C., Han C., Tapia R., Brainard J., Schmutz J., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Kim E., Ensigns S.A., Richardson P.;
RT "Complete sequence of chromosome of Xanthobacter autotrophicus Py2.";
RL Submitted (JUL-2007) 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; CP000781; ABS66694.1; -; Genomic_DNA.
DR AlphaFoldDB; A7IFA1; -.
DR STRING; 78245.Xaut_1446; -.
DR KEGG; xau:Xaut_1446; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_5; -.
DR OMA; TFMVLAP; -.
DR OrthoDB; 9810365at2; -.
DR PhylomeDB; A7IFA1; -.
DR Proteomes; UP000002417; 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-RELATED; 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:UP000002417}.
FT DOMAIN 54..188
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 238..433
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 452..608
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 646..686
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 733..858
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 59..69
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT MOTIF 647..651
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 650
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 894 AA; 99890 MW; 94ED4DE8CEB29839 CRC64;
MTQDRTTERA PERAQERSPD RYNAREAEPK WQKTWAERGI FRTRNDDPRP KFFVMEMFPY
PSGRIHIGHG RNYVMGDVLA RYKRMQGFNV LHPMGWDAFG LPAENAAIER GIHPKSWTYE
NIASMREQLQ LLGLSLDWNR EIATCDPSYY AEQQRIFLDF LDNGLAYRKE SEVNWDPVDN
TVLANEQVID GRGWRSGAIV ERRKLSQWFL RITDFAQELL DALDTLDRWP EKVRLMQRNW
IGRSEGMEVL FEFTRASVSA GTLPAAAKAV KVYTTRPDTL FGASFLALSP DHPLAQHLAL
KDAALAAFIA ECKRGGTSAE EIETQEKMGY ATGLEVVHPL DDKRTVPVYV ANFVLMDYGT
GAIFGCPAHD QRDLDFARKY GLSVTPVVLP AETDPGAFVV DDVAYDGDGT LFNSGFLDGM
SVPDAKEAVA RRLERYRVGD EPQGTRRVNF RLRDWGISRQ RYWGCPIPVI HCDACGPVGV
PREQLPVALP DDVTFDRPGN PLDRAKAWRD VPCPKCGKPA RRETDTMDTF VDSSWYFLRY
ASDNPQVPLD KDAVAHWLPV DQYIGGIEHA ILHLLYSRFF TRALKKCGRV DLDEPFAGLF
TQGMIVHETY KDTAGKWLFP EEVKLLGNGK AVKIADGSDV TVSPPEKMSK SKRNVVAPEV
VADTYGVDCA RWFMLSDTPP ERDSEWTQGG IEGAWRFVQR VWRLVNEAVE LGASAGSPRP
DAFSPTALGL RRAAHGLVAT VAEDIERLRF NVAVAHVHEF ANAFGSAIAV ARAEKAVPAD
LAFALREAAE MLASVVAPMV PHLAEECWVA LGGSTLVAQA PWPKVEADLL RQDTVTLPIQ
INGKKRDDIV VPREATAAEV EALVLKLESV QRALDGRAPK RIIVVPQRIV NVVA
//