TILS_BRADU
ID TILS_BRADU Reviewed; 361 AA.
AC Q9XBG6; Q79U41;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=tRNA(Ile)-lysidine synthase {ECO:0000255|HAMAP-Rule:MF_01161};
DE EC=6.3.4.19 {ECO:0000255|HAMAP-Rule:MF_01161};
DE AltName: Full=tRNA(Ile)-2-lysyl-cytidine synthase {ECO:0000255|HAMAP-Rule:MF_01161};
DE AltName: Full=tRNA(Ile)-lysidine synthetase {ECO:0000255|HAMAP-Rule:MF_01161};
GN Name=tilS {ECO:0000255|HAMAP-Rule:MF_01161}; OrderedLocusNames=bll7147;
OS Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS NBRC 14792 / USDA 110).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Bradyrhizobium.
OX NCBI_TaxID=224911;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=USDA 110spc4;
RX PubMed=10572147; DOI=10.1128/jb.181.23.7394-7397.1999;
RA Narberhaus F., Urech C., Hennecke H.;
RT "Characterization of the Bradyrhizobium japonicum ftsH gene and its
RT product.";
RL J. Bacteriol. 181:7394-7397(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT Bradyrhizobium japonicum USDA110.";
RL DNA Res. 9:189-197(2002).
CC -!- FUNCTION: Ligates lysine onto the cytidine present at position 34 of
CC the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an
CC ATP-dependent manner. Cytidine is converted to lysidine, thus changing
CC the amino acid specificity of the tRNA from methionine to isoleucine.
CC {ECO:0000255|HAMAP-Rule:MF_01161}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + cytidine(34) in tRNA(Ile2) + L-lysine = AMP +
CC diphosphate + H(+) + lysidine(34) in tRNA(Ile2);
CC Xref=Rhea:RHEA:43744, Rhea:RHEA-COMP:10625, Rhea:RHEA-COMP:10670,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:32551,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:82748, ChEBI:CHEBI:83665,
CC ChEBI:CHEBI:456215; EC=6.3.4.19; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01161};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01161}.
CC -!- DOMAIN: The N-terminal region contains the highly conserved SGGXDS
CC motif, predicted to be a P-loop motif involved in ATP binding.
CC -!- SIMILARITY: Belongs to the tRNA(Ile)-lysidine synthase family.
CC {ECO:0000255|HAMAP-Rule:MF_01161}.
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DR EMBL; AJ243808; CAB51028.1; -; Genomic_DNA.
DR EMBL; BA000040; BAC52412.1; -; Genomic_DNA.
DR RefSeq; NP_773787.1; NC_004463.1.
DR RefSeq; WP_011089882.1; NZ_CP011360.1.
DR AlphaFoldDB; Q9XBG6; -.
DR SMR; Q9XBG6; -.
DR STRING; 224911.27355429; -.
DR EnsemblBacteria; BAC52412; BAC52412; BAC52412.
DR GeneID; 64026904; -.
DR KEGG; bja:bll7147; -.
DR PATRIC; fig|224911.44.peg.7207; -.
DR eggNOG; COG0037; Bacteria.
DR HOGENOM; CLU_018869_3_2_5; -.
DR InParanoid; Q9XBG6; -.
DR OMA; PWQDPHN; -.
DR PhylomeDB; Q9XBG6; -.
DR Proteomes; UP000002526; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016879; F:ligase activity, forming carbon-nitrogen bonds; IEA:UniProtKB-UniRule.
DR GO; GO:0006400; P:tRNA modification; IEA:UniProtKB-UniRule.
DR CDD; cd01992; PP-ATPase; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_01161; tRNA_Ile_lys_synt; 1.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR011063; TilS/TtcA_N.
DR InterPro; IPR012094; tRNA_Ile_lys_synt.
DR InterPro; IPR012795; tRNA_Ile_lys_synt_N.
DR PANTHER; PTHR43033; PTHR43033; 1.
DR Pfam; PF01171; ATP_bind_3; 1.
DR TIGRFAMs; TIGR02432; lysidine_TilS_N; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Ligase; Nucleotide-binding; Reference proteome;
KW tRNA processing.
FT CHAIN 1..361
FT /note="tRNA(Ile)-lysidine synthase"
FT /id="PRO_0000181661"
FT BINDING 32..37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01161"
SQ SEQUENCE 361 AA; 38526 MW; 11C9949DB5232DC3 CRC64;
MSDDDNSPIS AREAKQLFAE LKSAPALVLA VSGGPDSIAL MWLAARWQRS LARGPRLTVV
TVDHGLRAEA AREAREVKRL ATELGLPHRT LRWRGAKPKT GLPAAAREAR YRLLMQAARS
AGASHVLTAH TRDDQAETLL MRLVRGSGLA GLSAMARLTE RDGIVLARPL LDVPKAQLIA
TLKRAKIGFA DDPTNRDTAF TRPRLRALLP QLAAEGGDAR SLARLAARLA RANAAVEVLT
DGAERFLRLR DRDDAPHGPD MRSFEAGAFA TLPEEVRLRM LLRAINALGH EGPAELGKVE
TLLAALDQAI AAGMAAAPRA AVNGRPVLKQ TLAGALISLA GGRIQIAPAP ARRRKGDRGG
S
