ID F9Z402_ODOSD Unreviewed; 923 AA.
AC F9Z402;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 78.
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=Odosp_2649 {ECO:0000313|EMBL:ADY33628.1};
OS Odoribacter splanchnicus (strain ATCC 29572 / DSM 20712 / CIP 104287 / JCM
OS 15291 / NCTC 10825 / 1651/6) (Bacteroides splanchnicus).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Odoribacteraceae;
OC Odoribacter.
OX NCBI_TaxID=709991 {ECO:0000313|EMBL:ADY33628.1, ECO:0000313|Proteomes:UP000006657};
RN [1] {ECO:0000313|EMBL:ADY33628.1, ECO:0000313|Proteomes:UP000006657}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29572 / DSM 20712 / JCM 15291 / NCTC 10825 / 1651/6
RC {ECO:0000313|Proteomes:UP000006657};
RX PubMed=21677857; DOI=10.4056/sigs.1714269;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Goker M., Gronow S., Zeytun A., Nolan M., Lucas S., Lapidus A., Hammon N.,
RA Deshpande S., Cheng J.F., Pitluck S., Liolios K., Pagani I., Ivanova N.,
RA Mavromatis K., Ovchinikova G., Pati A., Tapia R., Han C., Goodwin L.,
RA Chen A., Palaniappan K., Land M., Hauser L., Jeffries C.D., Brambilla E.M.,
RA Rohde M., Detter J.C., Woyke T., Bristow J., Markowitz V., Hugenholtz P.,
RA Eisen J.A., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Odoribacter splanchnicus type strain
RT (1651/6).";
RL Stand. Genomic Sci. 4:200-209(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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00049}.
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DR EMBL; CP002544; ADY33628.1; -; Genomic_DNA.
DR RefSeq; WP_013612821.1; NZ_CP086000.1.
DR AlphaFoldDB; F9Z402; -.
DR STRING; 709991.Odosp_2649; -.
DR PaxDb; 709991-Odosp_2649; -.
DR GeneID; 69854957; -.
DR KEGG; osp:Odosp_2649; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_10; -.
DR OrthoDB; 9810365at2; -.
DR BioCyc; OSPL709991:G1GRN-2697-MONOMER; -.
DR Proteomes; UP000006657; 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 Gene3D; 3.40.50.620; HUPs; 3.
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 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; 1.
DR Pfam; PF13603; tRNA-synt_1_2; 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:UP000006657}.
FT DOMAIN 11..144
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 276..459
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 773..884
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 697..701
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 700
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 923 AA; 105988 MW; 0C256B2B41406C70 CRC64;
MEYNFKEVEK KWQSYWKENQ TYKVDVDPSK PKFYVLDMFP YPSGAGLHVG HPLGYIASDI
YSRYKRLKGF NVLHPMGFDA YGLPAEQYAI QTGQHPAITT EKNIARYREQ LDKIGFSFDW
DREVRTCDPK YYKWTQWAFI QMFNHWFNKD TQKAEPIAKL VETFEKEGNA NINAANSDTP
IFTAEAWKAM DIREQQRVLL NYRIAYLADT MVNWCPQLGT VLANDEVKEG LSVRGGFPVV
QKNMRQWSLR VSAYAQRLLD GLNHLEWSDS LKDIQRNWIG RSQGADVIFD VKDSDIQLKI
FTTRPDTIYG VSFMVLAPES DYVRQLTTPD QEKAVAEYLD YVAKRTERER QSEIKTVTGV
FTGSYAMNPF TNEAIPVWIS EYVLAGYGTG AIMAVPAHDS RDYAFARKFN LPVIPVIDNG
QPIDLSKSSY DAKEGKMINS GLIDGMEVKE AIAFIAEEVE KRGIGKSKIN YRLRDAIFSR
QRYWGEPFPV YYKDSMPYMI DEAELPLELP EIDKYLPTEN GEPPLGRAKN WTTKEGYPIE
LNTMPGFAGS SAYYLRYMDP HNDKALVSHE ADAYWRNVDL YLGGAEHATG HLIYSRFWNM
FLYDLGVVCE PEPFKKLINQ GMIQGRSNFV YRIVGTNTYV SAGLKSQYET TEIHVDVNIV
KNDILDTEAF RKWMPDYADA EFILEDGKYI CGWAVEKMSK SMFNVVNPDD IIEQFGADTL
RLYEMFLGPL EAHKPWDTQG IDGVYKFLRK FWRLFLNGEE FSVSDEVPTK EELKVLHKTL
KKIEFDIENF SFNTSIPAFM ICTNELAALK CNKRAILEPL VVAIAPYAPH IAEELWHLLG
HAESVTGATF PQWEEKYLVE DSFEYPVSFN GKVRFKLNMP LTATQAEIEA AVKASPEAGK
WLEGKEIRKM IIVPKKIVNV VIA
//
