ID W4B0R6_9BACL Unreviewed; 410 AA. AC W4B0R6; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 22-FEB-2023, entry version 21. 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=C161_11088 {ECO:0000313|EMBL:ETT37049.1}; OS Paenibacillus sp. FSL R5-192. OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus. OX NCBI_TaxID=1226754 {ECO:0000313|EMBL:ETT37049.1, ECO:0000313|Proteomes:UP000019041}; RN [1] {ECO:0000313|EMBL:ETT37049.1, ECO:0000313|Proteomes:UP000019041} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FSL R5-192 {ECO:0000313|EMBL:ETT37049.1, RC ECO:0000313|Proteomes:UP000019041}; RX PubMed=24422886; DOI=10.1186/1471-2164-15-26; RA Moreno Switt A.I., Andrus A.D., Ranieri M.L., Orsi R.H., Ivy R., RA den Bakker H.C., Martin N.H., Wiedmann M., Boor K.J.; RT "Genomic comparison of sporeforming bacilli isolated from milk."; RL BMC Genomics 15:26-26(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:ETT37049.1}. 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; ASPR01000014; ETT37049.1; -; Genomic_DNA. DR RefSeq; WP_036670334.1; NZ_ASPR01000014.1. DR AlphaFoldDB; W4B0R6; -. DR EnsemblBacteria; ETT37049; ETT37049; C161_11088. DR PATRIC; fig|1226754.4.peg.2268; -. DR Proteomes; UP000019041; 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; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR008513; tRNA(Met)_cyd_acetate_ligase. 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|HAMAP-Rule:MF_01539}; KW 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 102 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01539" FT BINDING 168 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01539" FT BINDING 193 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01539" SQ SEQUENCE 410 AA; 44358 MW; 29BEA0575A6FD8BA CRC64; MKAVGVIVEY NPLHNGHVYH LQEARRLSGA DAVVAVMSGP FLQRGEPAIV GKRARTEMAL HAGADLVLEL PVAYAVQPAE WFAFGAVSLL HRTGVVDSLC FGSESGDLDS LQRIARVLAV EPAGMREDIA RRLREGASYP AAYAGAAAAL APGGVDAHDA AALLEQPNNS LGLHYLIALQ RLGSAIQPYT AARTGAAYHE ATPGPGAIAS ATAVRRLLMA DGPDAAAPYV PAATLAILHR EWQEGRAPIH WERFAQPLLH LAATRRASEL ERIAEVTEGL EHRLSRALAQ LPEPSVEALL NALKTKRYTR TKLQRMLAHL LLNHTKAECS PEQLATGPGY LRVLGFNAQG QSLLKQMKKT ASLPVVLKPS TFTHNQLELD IQAQVAYGLA CEHRDTRKMF SDYYESPVRL //