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Database: UniProt
Entry: W9GFJ6_9MICO
LinkDB: W9GFJ6_9MICO
Original site: W9GFJ6_9MICO 
ID   W9GFJ6_9MICO            Unreviewed;       331 AA.
AC   W9GFJ6;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   24-JAN-2024, entry version 43.
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=N865_09055 {ECO:0000313|EMBL:EWT03588.1};
OS   Intrasporangium oryzae NRRL B-24470.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC   Intrasporangium.
OX   NCBI_TaxID=1386089 {ECO:0000313|EMBL:EWT03588.1, ECO:0000313|Proteomes:UP000019489};
RN   [1] {ECO:0000313|EMBL:EWT03588.1, ECO:0000313|Proteomes:UP000019489}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL B-24470 {ECO:0000313|EMBL:EWT03588.1,
RC   ECO:0000313|Proteomes:UP000019489};
RA   Liu H., Wang G.;
RT   "Intrasporangium oryzae NRRL B-24470.";
RL   Submitted (AUG-2013) 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:EWT03588.1}.
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DR   EMBL; AWSA01000001; EWT03588.1; -; Genomic_DNA.
DR   RefSeq; WP_034800473.1; NZ_AWSA01000001.1.
DR   AlphaFoldDB; W9GFJ6; -.
DR   STRING; 1386089.N865_09055; -.
DR   PATRIC; fig|1386089.3.peg.72; -.
DR   eggNOG; COG0037; Bacteria.
DR   OrthoDB; 5244702at2; -.
DR   Proteomes; UP000019489; 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:UP000019489};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_01161}.
FT   DOMAIN          28..203
FT                   /note="tRNA(Ile)-lysidine/2-thiocytidine synthase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01171"
FT   DOMAIN          255..319
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   331 AA;  34515 MW;  CF3F9E17670D8FDD CRC64;
     MPGPDPAVAA TRLAVREHVA DLADGSLVLV ACSGGADSLA LAAALAFEAP RAGLRAGAVV
     VDHGLQEGSD LVAEMAAETC RELGLDPVEV TRADVHTTGA GLEADARTAR YAAIEAVAAR
     LHAEVVLVGH TRDDQAEQVL LGLSRGSGAR SLSGMPARRG RIVRPLLALP RATTRAACEA
     YGIEPWDDPH NSDESFRRVR ARRVLAVLEG ELGPGFGAAL ARSADLLRED ADYLERLAHE
     ARAELPDAEG LPGVDLDALA ALPRAIRTRV WRILAAEAGA PLADVSAAHV ESLDALLTSW
     HGQGPLHVPG GIAVARDRGA IRFRPLASGV E
//
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