ID I3QH48_9FLAO Unreviewed; 929 AA.
AC I3QH48;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 58.
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:AFJ90933.1};
GN ORFNames=BGIGA_504 {ECO:0000313|EMBL:AFJ90933.1};
OS Blattabacterium sp. (Blaberus giganteus).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Blattabacteriaceae; Blattabacterium.
OX NCBI_TaxID=1186051 {ECO:0000313|EMBL:AFJ90933.1, ECO:0000313|Proteomes:UP000006466};
RN [1] {ECO:0000313|EMBL:AFJ90933.1, ECO:0000313|Proteomes:UP000006466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGIGA {ECO:0000313|EMBL:AFJ90933.1,
RC ECO:0000313|Proteomes:UP000006466};
RX PubMed=22843586; DOI=10.1128/JB.00789-12;
RA Huang C.Y., Sabree Z.L., Moran N.A.;
RT "Genome Sequence of Blattabacterium sp. Strain BGIGA, Endosymbiont of the
RT Blaberus giganteus Cockroach.";
RL J. Bacteriol. 194:4450-4451(2012).
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:RU363039}.
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; CP003535; AFJ90933.1; -; Genomic_DNA.
DR RefSeq; WP_014726802.1; NC_017924.1.
DR AlphaFoldDB; I3QH48; -.
DR STRING; 1186051.BGIGA_504; -.
DR KEGG; bbg:BGIGA_504; -.
DR PATRIC; fig|1186051.3.peg.485; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_10; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000006466; 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 Gene3D; 3.40.50.620; HUPs; 3.
DR HAMAP; MF_00049_B; Leu_tRNA_synth_B; 1.
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; 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.
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}; Cytoplasm {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}.
FT DOMAIN 34..144
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 277..445
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 782..890
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 703..707
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 706
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 929 AA; 110155 MW; F683C1A89F2E31DA CRC64;
MEYNFREIEK RWQIYWKKHN IFHTKEDKRI KKYYILNMFP YPSGTGLHVG HCLGYIASDV
YARYKRAEGY NVLNPIGFDS FGLPAEQYAI QTGKHPYDTI CENSRRYKKQ MNRIGLSFDW
NRKIYTSNPN YYRWTQWIFI QIFNSWYDKN SEQAKPIDFL IKEFNKNGNN FINASTTFNY
KFDSKTWNQL NLYEKESILL DYRLAFLCNN IVNWCPDLGT VLANDEIKNG KSERGGYPVY
KKKMLQWHIR ISSYAERLIK GLNFIDCSQS LKKLQYNWIG KSIGISILLK IIHPIGKINQ
IELFTSSPEM MFGMTFIILS TDHPLAERIS IFSLQHHKNV LTYLTKEFYI DKKTKNISGI
FTGNYVFHPF IKNKKIPIYI SNFFTVNNQT KSIIGIPGHE EKSKKFAKKF GIEIIKILDS
NEICINSNFL NGFNRKQAKE KIIKILVNNK IGETKTSYKI RDAIFSRQRY WGEPIPIYFK
NKIPKTIPVE KLPILLPKID KFHPEKGKSP LVLAKNWAWD EKNMKIVPNT LIDHKHVFPI
ETSTMPSWAG SSWYFLRYMD AHNNQFFLDK RKENYWKNVD LYIGGSEHST GHLIYARFFH
KFLLDRGWIT TEEPFKKILN QGMILSYSAI ILKVIGENIF VSYGLKNKKH AYSSLQEVYV
DLSLIKDNNE LDINRFKKFR PEFYSSIFIF EKGSFLCKRK LEKMSKSKYN VINPDDIYEK
YGSDIFRVYE MFLGPIHQSK PWNEEKINGI KNFINKFWCL FHKNNIFQVN EKNPTFQEFQ
ILHRTIKKIQ NKIQSFSWNT SISLLMMMTN QLTVLKCNKR KILEPLVQLL APFAPHISEE
LWYKLGKRKS IIFYNIPAFN TKYIVENEIT YPIMFNGKLK FLEKFDSNTS IDEIKNKILS
HPKTKFFLKK KIFKKLILIP KKVINILFK
//
