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Database: UniProt
Entry: A0A0A6WXI6_ACTUT
LinkDB: A0A0A6WXI6_ACTUT
Original site: A0A0A6WXI6_ACTUT 
ID   A0A0A6WXI6_ACTUT        Unreviewed;       324 AA.
AC   A0A0A6WXI6;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 40.
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=MB27_38715 {ECO:0000313|EMBL:KHD72407.1};
OS   Actinoplanes utahensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Actinoplanes.
OX   NCBI_TaxID=1869 {ECO:0000313|EMBL:KHD72407.1, ECO:0000313|Proteomes:UP000054537};
RN   [1] {ECO:0000313|EMBL:KHD72407.1, ECO:0000313|Proteomes:UP000054537}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 12052 {ECO:0000313|EMBL:KHD72407.1,
RC   ECO:0000313|Proteomes:UP000054537};
RA   Velasco-Bucheli B., del Cerro C., Hormigo D., Garcia J.L., Acebal C.,
RA   Arroyo M., de la Mata I.;
RT   "Draft genome sequence of Actinoplanes utahensis NRRL 12052.";
RL   Submitted (OCT-2014) 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:KHD72407.1}.
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DR   EMBL; JRTT01000137; KHD72407.1; -; Genomic_DNA.
DR   RefSeq; WP_043533075.1; NZ_JRTT01000137.1.
DR   AlphaFoldDB; A0A0A6WXI6; -.
DR   STRING; 1869.MB27_38715; -.
DR   eggNOG; COG0037; Bacteria.
DR   OrthoDB; 5244702at2; -.
DR   Proteomes; UP000054537; 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; 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:UP000054537};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_01161}.
FT   DOMAIN          28..199
FT                   /note="tRNA(Ile)-lysidine/2-thiocytidine synthase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01171"
FT   DOMAIN          248..313
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   324 AA;  33332 MW;  38FC38D436F55BE7 CRC64;
     MAKIPPPVAA VRMAVRRGLA DLPEDALVLV ACSGGADSLA LASAARFSGR RVGLVTVDHG
     LQEGSERRAR SVAAWARDAG FDPVRIETVS VAGLPGGPEA AARTARYAAL ASAATELGAS
     AVVLGHTRDD QAETVLLALA RGGGPRGLSG MPWRRGMFRR PLLDVARADT RKACAALGLA
     PWEDPHNTDP AYARSRVRAS VLPVLVDALG TGVLANLSRT ATLVAADNAA LDELSAAALE
     SVRSAAGLSV PALAGLLPAI RSRVLHRWAR ELGAPGGALA FGHVTTLEAL VSGWRGQGPA
     HLPGGILVAR RSDDLVRVDP AFIS
//
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