ID A0A172TRY4_9BACT Unreviewed; 468 AA.
AC A0A172TRY4;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=tRNA(Ile)-lysidine synthase {ECO:0000256|HAMAP-Rule:MF_01161};
DE EC=6.3.4.19 {ECO:0000256|HAMAP-Rule:MF_01161};
DE AltName: Full=tRNA(Ile)-2-lysyl-cytidine synthase {ECO:0000256|HAMAP-Rule:MF_01161};
DE AltName: Full=tRNA(Ile)-lysidine synthetase {ECO:0000256|HAMAP-Rule:MF_01161};
GN Name=tilS {ECO:0000256|HAMAP-Rule:MF_01161};
GN ORFNames=SY85_03850 {ECO:0000313|EMBL:ANE49752.1};
OS Flavisolibacter tropicus.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Flavisolibacter.
OX NCBI_TaxID=1492898 {ECO:0000313|EMBL:ANE49752.1, ECO:0000313|Proteomes:UP000077177};
RN [1] {ECO:0000313|Proteomes:UP000077177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LCS9 {ECO:0000313|Proteomes:UP000077177};
RA Kim M.K., Srinivasan S., Lee J.-J.;
RT "Flavisolibacter sp./LCS9/ whole genome sequencing.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ANE49752.1, ECO:0000313|Proteomes:UP000077177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LCS9 {ECO:0000313|EMBL:ANE49752.1,
RC ECO:0000313|Proteomes:UP000077177};
RX PubMed=27259556; DOI=10.1099/ijsem.0.001207;
RA Lee J.J., Kang M.S., Kim G.S., Lee C.S., Lim S., Lee J., Roh S.H., Kang H.,
RA Ha J.M., Bae S., Jung H.Y., Kim M.K.;
RT "Flavisolibacter tropicus sp. nov., isolated from tropical soil.";
RL Int. J. Syst. Evol. Microbiol. 66:3413-3419(2016).
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:0000256|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;
CC Evidence={ECO:0000256|ARBA:ARBA00000047, ECO:0000256|HAMAP-
CC Rule:MF_01161};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|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 {ECO:0000256|HAMAP-Rule:MF_01161}.
CC -!- SIMILARITY: Belongs to the tRNA(Ile)-lysidine synthase family.
CC {ECO:0000256|HAMAP-Rule:MF_01161}.
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DR EMBL; CP011390; ANE49752.1; -; Genomic_DNA.
DR RefSeq; WP_066401888.1; NZ_CP011390.1.
DR AlphaFoldDB; A0A172TRY4; -.
DR STRING; 1492898.SY85_03850; -.
DR KEGG; fla:SY85_03850; -.
DR PATRIC; fig|1492898.3.peg.842; -.
DR OrthoDB; 9807403at2; -.
DR Proteomes; UP000077177; 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; HUPs; 1.
DR HAMAP; MF_01161; tRNA_Ile_lys_synt; 1.
DR InterPro; IPR012796; Lysidine-tRNA-synth_C.
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 NCBIfam; TIGR02433; lysidine_TilS_C; 1.
DR NCBIfam; TIGR02432; lysidine_TilS_N; 1.
DR PANTHER; PTHR43033; TRNA(ILE)-LYSIDINE SYNTHASE-RELATED; 1.
DR PANTHER; PTHR43033:SF1; TRNA(ILE)-LYSIDINE SYNTHASE-RELATED; 1.
DR Pfam; PF01171; ATP_bind_3; 2.
DR Pfam; PF11734; TilS_C; 1.
DR SMART; SM00977; TilS_C; 1.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR SUPFAM; SSF56037; PheT/TilS domain; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01161};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01161};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_01161};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01161};
KW Reference proteome {ECO:0000313|Proteomes:UP000077177};
KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_01161}.
FT DOMAIN 391..463
FT /note="Lysidine-tRNA(Ile) synthetase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00977"
FT BINDING 29..34
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01161"
SQ SEQUENCE 468 AA; 53649 MW; 9A3EE3526AF5B4F1 CRC64;
MNNLLLQRFI NNLKLIAVTE QHTLLLAVSG GLDSVVLCHL CKLAGYSFAI AHCNFGLRGE
ESNKDEAFVK ALAAQLEVPF YVNNFNTKAF AAEHKLSIQV AARELRYQWF HEIVNGQLSV
INEKASSYST HLPSITTHYS PLTFIATAHH LDDNIETLLM NLFKGTGISG LHGIQPKSGK
IVRPLLFAKR EEIKDFATEH NLLWVEDSSN AEIKYTRNYI RHKIIPSIES IFPTVKENIA
DSIERLREAE ILYEQAMQVH KKKLLEFKGQ EVYIPVLKLE RTSPLATIIY EIIKDYGFSS
QQVPEVIKLL RSESGRYVTS ASHRILHNRD WLIITPLPQV QDTVLIIEEA TTQLAFTEGT
LLFKTLPAES ITIEADAAVA LLDKEEMQFP LILRKWKEGD YFYPLGMRKK KKLARFFIDQ
KLSQLQKEKV WVLESNKRIV WVVGRRIDDR FKIKPSTKEV VRIELKPV
//
