ID A0A0L0MK37_9MOLU Unreviewed; 421 AA.
AC A0A0L0MK37;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-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:KND62748.1};
GN ORFNames=AlmWB_00490 {ECO:0000313|EMBL:KND62748.1};
OS Candidatus Phytoplasma phoenicium.
OC Bacteria; Mycoplasmatota; Mollicutes; Acholeplasmatales;
OC Acholeplasmataceae; Phytoplasma; 16SrIX (Pigeon pea witches'-broom group).
OX NCBI_TaxID=198422 {ECO:0000313|EMBL:KND62748.1, ECO:0000313|Proteomes:UP000037086};
RN [1] {ECO:0000313|EMBL:KND62748.1, ECO:0000313|Proteomes:UP000037086}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA213 {ECO:0000313|EMBL:KND62748.1,
RC ECO:0000313|Proteomes:UP000037086};
RX PubMed=26223451; DOI=10.1186/s12866-015-0487-4;
RA Quaglino F., Kube M., Jawhari M., Abou-Jawdah Y., Siewert C., Choueiri E.,
RA Sobh H., Casati P., Tedeschi R., Molino Lova M., Alma A., Bianco P.A.;
RT "'Candidatus Phytoplasma phoenicium' associated with almond witches'-broom
RT disease: from draft genome to genetic diversity among strain populations.";
RL BMC Microbiol. 15:148-148(2015).
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:KND62748.1}.
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DR EMBL; JPSQ01000003; KND62748.1; -; Genomic_DNA.
DR RefSeq; WP_050336996.1; NZ_JPSQ01000003.1.
DR AlphaFoldDB; A0A0L0MK37; -.
DR PATRIC; fig|198422.3.peg.135; -.
DR OrthoDB; 9807403at2; -.
DR Proteomes; UP000037086; 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 HAMAP; MF_01161; tRNA_Ile_lys_synt; 1.
DR InterPro; IPR012796; Lysidine-tRNA-synth_C.
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 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:UP000037086};
KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_01161}.
FT DOMAIN 349..416
FT /note="Lysidine-tRNA(Ile) synthetase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00977"
FT BINDING 20..25
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01161"
SQ SEQUENCE 421 AA; 50007 MW; 053EF534931AB7CD CRC64;
MKIHLAIKLE HKNIYIISVS GGVDSMVLLD FLYHRQFCLI VVYFDHCQRK DSFKDKLLIE
QYCKTKNIPL HSFQLTTLET NNFQNNARLA RQTILKQVAS QYKTHYIITA HHLDDLAETI
FMKILRGSSL LGYSGMKSSY VLQNFIWLKP FLYLSKQTIK NYAQQNNIPF LEDSTNNLDF
YTRNKIRHHI IPKLKTMGNF LKKIKHFHLQ IQESSDLITK LTNVFLKQQK SNYFELKAFL
QLHVTIQKNI LLCLLEAKQI IANFELISNI IEGLCNYKKP NNKWYLNKKW YLIKEYDKFF
FQMHSQLDAM LLKKKAKPLL YSCINIQLLS FCTIKQIIFY DEGMLLPPFY LRQRQPGDIL
HFSFGSQKLK KFLINNKITT LQRNLLWLVV DQNNTIIFIP RLYFNKTLGQ QKYLYLGLKE
I
//
