TMCAL_CLOD6
ID TMCAL_CLOD6 Reviewed; 426 AA.
AC Q18B37;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=tRNA(Met) cytidine acetate ligase {ECO:0000255|HAMAP-Rule:MF_01539};
DE EC=6.3.4.- {ECO:0000255|HAMAP-Rule:MF_01539};
GN Name=tmcAL {ECO:0000255|HAMAP-Rule:MF_01539};
GN OrderedLocusNames=CD630_11740;
OS Clostridioides difficile (strain 630) (Peptoclostridium difficile).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Clostridioides.
OX NCBI_TaxID=272563;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=630;
RX PubMed=16804543; DOI=10.1038/ng1830;
RA Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N.,
RA Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H.,
RA Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N.,
RA Brooks K., Chillingworth T., Cronin A., Davis P., Dowd L., Fraser A.,
RA Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K.,
RA Price C., Rabbinowitsch E., Sharp S., Simmonds M., Stevens K., Unwin L.,
RA Whithead S., Dupuy B., Dougan G., Barrell B., Parkhill J.;
RT "The multidrug-resistant human pathogen Clostridium difficile has a highly
RT mobile, mosaic genome.";
RL Nat. Genet. 38:779-786(2006).
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:0000255|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:0000255|HAMAP-Rule:MF_01539};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01539}.
CC -!- SIMILARITY: Belongs to the TmcAL family. {ECO:0000255|HAMAP-
CC Rule:MF_01539}.
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DR EMBL; AM180355; CAJ68027.1; -; Genomic_DNA.
DR RefSeq; WP_011861133.1; NZ_CP010905.2.
DR RefSeq; YP_001087666.1; NC_009089.1.
DR AlphaFoldDB; Q18B37; -.
DR SMR; Q18B37; -.
DR STRING; 272563.CD630_11740; -.
DR EnsemblBacteria; CAJ68027; CAJ68027; CD630_11740.
DR KEGG; cdf:CD630_11740; -.
DR KEGG; pdc:CDIF630_01322; -.
DR PATRIC; fig|272563.120.peg.1224; -.
DR eggNOG; COG1323; Bacteria.
DR OMA; WARTKMA; -.
DR PhylomeDB; Q18B37; -.
DR BioCyc; PDIF272563:G12WB-1304-MON; -.
DR Proteomes; UP000001978; Chromosome.
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; -; 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; PTHR37825; 1.
DR Pfam; PF05636; HIGH_NTase1; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Ligase; Nucleotide-binding; Reference proteome;
KW RNA-binding; tRNA processing; tRNA-binding.
FT CHAIN 1..426
FT /note="tRNA(Met) cytidine acetate ligase"
FT /id="PRO_0000292799"
FT BINDING 7..20
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01539"
FT BINDING 102
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01539"
FT BINDING 176
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01539"
FT BINDING 201
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01539"
SQ SEQUENCE 426 AA; 49149 MW; CF21DFBA79EAE6B2 CRC64;
MNILGLIVEY NPFHNGHIYH LSKSIEKTNA THTVAIMSGN FLQRGEPALF DKYTRAKIAV
ENGVDLVIEL PTLFACQSAE IFSHGAITIL NSLNCINSIC FGSEEGNTEI LYNIAEILAN
EPNKFKLLLK KYLDDGLLFP TARANALFDY IHQDKKNNFI QNYSKEQLSK TLNSSNNILG
IEYIKNLIHL NSSIKPFTIS RVQSEYNSEE IESDICSATA IRTSLKENTD LFHLKNVIPE
KTYNILNEKI DNGFLPMFDD FFFDILKTII LRDMDTLKEY FEVNEGIENR IYKDIFTSEF
LHELQLAIKS KRYTLTKIKR TLNNILLGIK KSDMQLIKNI DTIPYIRILA FNDKGREILK
EIKNKSEIKI INKFSNISFS LDDTIFKTLI SYDIKATNIY NSIYYKNNKD LVKGPMDFYT
HPIYVK