ID A0A136Q3S8_9FIRM Unreviewed; 468 AA.
AC A0A136Q3S8;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-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=HMPREF3293_01833 {ECO:0000313|EMBL:KXK65244.1};
OS Christensenella minuta.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Christensenellaceae;
OC Christensenella.
OX NCBI_TaxID=626937 {ECO:0000313|EMBL:KXK65244.1, ECO:0000313|Proteomes:UP000070366};
RN [1] {ECO:0000313|EMBL:KXK65244.1, ECO:0000313|Proteomes:UP000070366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22607 {ECO:0000313|EMBL:KXK65244.1,
RC ECO:0000313|Proteomes:UP000070366};
RA Wen L., He K., Yang H.;
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KXK65244.1}.
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DR EMBL; LSZW01000062; KXK65244.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A136Q3S8; -.
DR STRING; 626937.HMPREF3293_01833; -.
DR KEGG; cmiu:B1H56_08840; -.
DR PATRIC; fig|626937.4.peg.1811; -.
DR OrthoDB; 9807403at2; -.
DR Proteomes; UP000070366; Unassembled WGS sequence.
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; 1.20.59.20; -; 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; 1.
DR Pfam; PF11734; TilS_C; 1.
DR SMART; SM00977; TilS_C; 1.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR SUPFAM; SSF82829; MesJ substrate recognition domain-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:UP000070366};
KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_01161}.
FT DOMAIN 379..451
FT /note="Lysidine-tRNA(Ile) synthetase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00977"
FT BINDING 26..31
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01161"
SQ SEQUENCE 468 AA; 52377 MW; D98B3D31D7F5E95E CRC64;
MEERVRDFIT ENGLIGLGQT VGVAVSGGPD SMALLACLRS LVPFFSCSVA CVHFEHGIRG
QESLDDADFV SRFCEEQGIP FYMSAADVPA LAREWGMSEE TAAKRAREAY FNTLVENEDV
DVIATGHHSD DNAESVLMHI LRGSGIDGLK GIAARNGNFI RPLLCVSRED VMEYVRDKGL
HYMQDKTNDN AEYTRNFVRN TLLPQIRERI NPDVSGALNR LSAIAQEDSS FILGEAERVF
PECAKQKGDR VEIEIGHFLG FSPAVEYRII RLACAKLFVT QDIEKAHVGA VIRLAQKNRT
GTRVNLSGGL CAEVEYGTLV ICFAARRVNH SFCIVFDIEA KNETPFGDYI VCERAEACDF
NNKDPYTAYV DRDKLPAHFM FRTRYTGDRI TPLGSGGSKK LKDYFIDKKL TREERERTPL
LADGNRIIWA VGHVIGDDYK VDGTTKRILR MNYIRCGNIK EETDRGEG
//
