ID A0A140L091_9CLOT Unreviewed; 468 AA.
AC A0A140L091;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
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 ECO:0000313|EMBL:KXG73966.1};
GN ORFNames=AN619_27230 {ECO:0000313|EMBL:KXG73966.1};
OS Thermotalea metallivorans.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Thermotalea.
OX NCBI_TaxID=520762 {ECO:0000313|EMBL:KXG73966.1, ECO:0000313|Proteomes:UP000070456};
RN [1] {ECO:0000313|EMBL:KXG73966.1, ECO:0000313|Proteomes:UP000070456}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B2-1 {ECO:0000313|EMBL:KXG73966.1,
RC ECO:0000313|Proteomes:UP000070456};
RA Patel B.K.;
RT "Draft genome sequence of the thermoanaerobe Thermotalea metallivorans, an
RT isolate from the runoff channel of the Great Artesian Basin, Australia.";
RL Submitted (DEC-2015) 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:KXG73966.1}.
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DR EMBL; LOEE01000070; KXG73966.1; -; Genomic_DNA.
DR RefSeq; WP_068557817.1; NZ_LOEE01000070.1.
DR AlphaFoldDB; A0A140L091; -.
DR STRING; 520762.AN619_27230; -.
DR PATRIC; fig|520762.4.peg.3004; -.
DR OrthoDB; 9807403at2; -.
DR Proteomes; UP000070456; 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 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 InterPro; IPR015262; tRNA_Ile_lys_synt_subst-bd.
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; PF09179; TilS; 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:UP000070456};
KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_01161}.
FT DOMAIN 384..456
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; 54869 MW; 41535828403DC691 CRC64;
MLNKFLKTVE RHRMLEKGEG VVVGVSGGPD SICLLHLLWR IKDMYDLKLY AVHLNHRFRG
EEADADAAYV KEFCDKLDIP SFIFSEDIAR YSREKGISFE EAGRERRYQL FYQVMAQQRA
GKIAVAQNMD DQAETVLMRF MRGSGMEGLG AISYVRNHTI IRPLLDISRR EIEDYCEAFQ
LKPRIDKTNL ETIYTRNRIR LELIPYIQKY FNPRIKETLW RTANLFREDR EWIELLVQKS
FEEAARKEND AVRLDCQAIR KMHPAMGKRV LRRAVQEVCG NLADTEYVHI EHILELMQKG
NVGASIDLPK GMIAELGYGV LKIMKGRVIG PVEFIYPLGI GESLYLPELN ATVTSKIISL
DQWNPQDKHP YKRYFDLEKI EQGMIIRNRR AGDRFVPYGM QGRKKLKDYF IDEKVPREMR
DRIPLVCDGH EIMWVVGYRT SERYKIGPQT KKVLVLEWKF QYQPEEMP
//
