ID A0A1I6YWW9_9FIRM Unreviewed; 468 AA.
AC A0A1I6YWW9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=SAMN02910301_1688 {ECO:0000313|EMBL:SFT54711.1};
OS Lachnospiraceae bacterium XBD2001.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1520820 {ECO:0000313|EMBL:SFT54711.1, ECO:0000313|Proteomes:UP000199425};
RN [1] {ECO:0000313|EMBL:SFT54711.1, ECO:0000313|Proteomes:UP000199425}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=XBD2001 {ECO:0000313|EMBL:SFT54711.1,
RC ECO:0000313|Proteomes:UP000199425};
RA de Groot N.N.;
RL Submitted (OCT-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}.
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DR EMBL; FPAN01000006; SFT54711.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6YWW9; -.
DR STRING; 1520820.SAMN02910301_1688; -.
DR OrthoDB; 9807403at2; -.
DR Proteomes; UP000199425; 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; 3.40.50.620; HUPs; 1.
DR Gene3D; 3.50.40.10; Phenylalanyl-trna Synthetase, Chain B, domain 3; 1.
DR HAMAP; MF_01161; tRNA_Ile_lys_synt; 1.
DR InterPro; IPR012796; Lysidine-tRNA-synth_C.
DR InterPro; IPR020825; Phe-tRNA_synthase-like_B3/B4.
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:UP000199425};
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; 53212 MW; 567FE2BF463AE6FD CRC64;
MLSFLDKVRN FIQTNELLEH GEQVTVGVSG GADSVCLLFV LLDLQEEYDL KVQAVYVEHG
IRGEESVEDG RFVEKLCISK GVPFRQADVD APELASLEHM SLEEAARRLR YEALIQTAKH
GDKGGKIAVA HNADDNVETI LYQMARGTGI RGLCGMEPLS PRKDGTKIIR PLLCVERGEI
EMYLADKEQD YVTDSTNADD NYARNRIRHD ILPVLREINS EAVAHINESA KQLTRLYKSH
MDDADRILDA VRGKQGIVRE RLLKYPDAMQ AEVVRRFLLQ ECGGIRDITR AHFVSAVDLL
SAEVGKRIDL PGGIKLKADY DELIVEKIVD EEVPQDPWSI DIPKLEVGES YEISLDEYDI
HMEVVQWTAE EEIPDKTYAK IFDYDKIKDK LNIRSRNMGD RMQVLADGGT KRLKDYFIDE
KIPKEERDSI PLLAEGQDIL WVIGYRRSEA ALVTDETSRV LKVEVWRN
//
