ID V6DNI4_9LACO Unreviewed; 380 AA.
AC V6DNI4;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=tRNA(Met) cytidine acetate ligase {ECO:0000256|HAMAP-Rule:MF_01539};
DE EC=6.3.4.- {ECO:0000256|HAMAP-Rule:MF_01539};
GN Name=tmcAL {ECO:0000256|HAMAP-Rule:MF_01539};
GN ORFNames=LSCP400_20711 {ECO:0000313|EMBL:CDK36240.1};
OS Ligilactobacillus salivarius cp400.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Ligilactobacillus.
OX NCBI_TaxID=1273133 {ECO:0000313|EMBL:CDK36240.1, ECO:0000313|Proteomes:UP000018601};
RN [1] {ECO:0000313|EMBL:CDK36240.1, ECO:0000313|Proteomes:UP000018601}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cp400 {ECO:0000313|Proteomes:UP000018601};
RX PubMed=24526652; DOI=10.1128/genomeA.01231-13;
RA Mackenzie D.A., McLay K., Roos S., Walter J., Swarbreck D., Drou N.,
RA Crossman L.C., Juge N.;
RT "Draft Genome Sequence of a Novel Lactobacillus salivarius Strain Isolated
RT from Piglet.";
RL Genome Announc. 2:e01231-e01213(2014).
CC -!- FUNCTION: Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at
CC the wobble position of elongator tRNA(Met), using acetate and ATP as
CC substrates. First activates an acetate ion to form acetyladenylate (Ac-
CC AMP) and then transfers the acetyl group to tRNA to form ac(4)C34.
CC {ECO:0000256|HAMAP-Rule:MF_01539}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetate + ATP + cytidine(34) in elongator tRNA(Met) = AMP +
CC diphosphate + N(4)-acetylcytidine(34) in elongator tRNA(Met);
CC Xref=Rhea:RHEA:58144, Rhea:RHEA-COMP:10693, Rhea:RHEA-COMP:10694,
CC ChEBI:CHEBI:30089, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:74900, ChEBI:CHEBI:82748, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01539};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01539}.
CC -!- SIMILARITY: Belongs to the TmcAL family. {ECO:0000256|HAMAP-
CC Rule:MF_01539}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01539}.
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:CDK36240.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CBVR010000054; CDK36240.1; -; Genomic_DNA.
DR AlphaFoldDB; V6DNI4; -.
DR Proteomes; UP000018601; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016879; F:ligase activity, forming carbon-nitrogen bonds; IEA:UniProtKB-UniRule.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006400; P:tRNA modification; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR HAMAP; MF_01539; TmcAL; 1.
DR InterPro; IPR004821; Cyt_trans-like.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR008513; tRNA(Met)_cyd_acetate_ligase.
DR NCBIfam; TIGR00125; cyt_tran_rel; 1.
DR PANTHER; PTHR37825; TRNA(MET) CYTIDINE ACETATE LIGASE; 1.
DR PANTHER; PTHR37825:SF1; TRNA(MET) CYTIDINE ACETATE LIGASE; 1.
DR Pfam; PF05636; HIGH_NTase1; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01539};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01539};
KW Ligase {ECO:0000256|HAMAP-Rule:MF_01539};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01539};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01539};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_01539}; tRNA-binding {ECO:0000256|HAMAP-Rule:MF_01539}.
FT BINDING 7..20
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01539"
FT BINDING 101
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01539"
FT BINDING 151
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01539"
FT BINDING 176
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01539"
SQ SEQUENCE 380 AA; 43328 MW; B0C1D8C82621EEB5 CRC64;
MKIIGIIAEY NPFHNGHLYQ IEKVKEIYPE SIIIVAMSGN FLQRGEPAIV DKWVRARQAL
LNGVDVVVEI PIAGCVQPAD RFAENGVQIL SNMGCEELFF GAEHAEYDFM TYAQLVQNLD
STEFSKKNIS YAEAFQEAVA AKIGHNIDSP NDVLGLAYAK ANLKFGKKLK LNPISRNVAG
YHDKSLSPDS NIASATAIRK VLFSKDHNLV DKYLPSYQDL KDEKYISWDD FWPFLRYKLI
SSDIDELANI YGMAEGIQYR MKKKALELKT EATFDEWLKA VKSKRFTYTR LTRLSVATLV
GMKVNDVGLY NKFPYVHLLG FTKNGQKALN TMKKNSEIPL LAKISQQDKD DFYHIDYRAG
KIYQSQNYKE QDLKRAPLIF
//
