ID W5VZN9_9PSEU Unreviewed; 321 AA.
AC W5VZN9;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 47.
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=KALB_359 {ECO:0000313|EMBL:AHH93736.1};
OS Kutzneria albida DSM 43870.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Kutzneria.
OX NCBI_TaxID=1449976 {ECO:0000313|EMBL:AHH93736.1, ECO:0000313|Proteomes:UP000019225};
RN [1] {ECO:0000313|EMBL:AHH93736.1, ECO:0000313|Proteomes:UP000019225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43870 {ECO:0000313|EMBL:AHH93736.1};
RX PubMed=25301375; DOI=10.1186/1471-2164-15-885;
RA Rebets Y., Tokovenko B., Lushchyk I., Ruckert C., Zaburannyi N.,
RA Bechthold A., Kalinowski J., Luzhetskyy A.;
RT "Complete genome sequence of producer of the glycopeptide antibiotic
RT Aculeximycin Kutzneria albida DSM 43870T, a representative of minor genus
RT of Pseudonocardiaceae.";
RL BMC Genomics 15:885-885(2014).
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; CP007155; AHH93736.1; -; Genomic_DNA.
DR RefSeq; WP_025354017.1; NZ_CP007155.1.
DR AlphaFoldDB; W5VZN9; -.
DR STRING; 1449976.KALB_359; -.
DR KEGG; kal:KALB_359; -.
DR PATRIC; fig|1449976.3.peg.363; -.
DR eggNOG; COG0037; Bacteria.
DR HOGENOM; CLU_018869_1_1_11; -.
DR OrthoDB; 5244702at2; -.
DR Proteomes; UP000019225; 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; 1.20.59.20; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 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 InterPro; IPR015262; tRNA_Ile_lys_synt_subst-bd.
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 SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR SUPFAM; SSF82829; MesJ substrate recognition domain-like; 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:UP000019225};
KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_01161}.
FT DOMAIN 28..201
FT /note="tRNA(Ile)-lysidine/2-thiocytidine synthase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF01171"
FT DOMAIN 249..314
FT /note="tRNA(Ile)-lysidine synthase substrate-binding"
FT /evidence="ECO:0000259|Pfam:PF09179"
FT BINDING 33..38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01161"
SQ SEQUENCE 321 AA; 33567 MW; 6FB123884E19326D CRC64;
MGQPDEAVSQ VRTAVRRLLT GAGATGEVAV AVSGGADSLA LAAAARHVSR RLDLRVLGLV
VDHGLQPGSD QVAGRAADQL RGLGLDEVRV LTTEVTGPGG VEAAARRARY AALRGARTPG
TWVLLGHTRD DQAETVLLGL GRGSGPRSIA GMRPLDPPWA RPLLAVSRAT TVRACAALGL
TPWQDPHNTD PAFTRVRLRH EALPLLEDVL RGGVADALAR TAAQLREDND ALDALAADLL
GRALNGATLD AAVLAAEPAA LRRRAVRSWL TDQGVTDLTD AQLREVDELV GNWRGQGGVR
LRGGLVAGRA HGRLGLDRAE S
//
