TMCAL_STRPZ
ID TMCAL_STRPZ Reviewed; 368 AA.
AC B5XJU1;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 54.
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}; OrderedLocusNames=Spy49_0264;
OS Streptococcus pyogenes serotype M49 (strain NZ131).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=471876;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NZ131;
RX PubMed=18820018; DOI=10.1128/jb.00672-08;
RA McShan W.M., Ferretti J.J., Karasawa T., Suvorov A.N., Lin S., Qin B.,
RA Jia H., Kenton S., Najar F., Wu H., Scott J., Roe B.A., Savic D.J.;
RT "Genome sequence of a nephritogenic and highly transformable M49 strain of
RT Streptococcus pyogenes.";
RL J. Bacteriol. 190:7773-7785(2008).
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; CP000829; ACI60603.1; -; Genomic_DNA.
DR RefSeq; WP_009880639.1; NC_011375.1.
DR AlphaFoldDB; B5XJU1; -.
DR SMR; B5XJU1; -.
DR EnsemblBacteria; ACI60603; ACI60603; Spy49_0264.
DR KEGG; soz:Spy49_0264; -.
DR HOGENOM; CLU_038915_0_2_9; -.
DR OMA; WARTKMA; -.
DR Proteomes; UP000001039; 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; RNA-binding;
KW tRNA processing; tRNA-binding.
FT CHAIN 1..368
FT /note="tRNA(Met) cytidine acetate ligase"
FT /id="PRO_1000146635"
FT BINDING 7..20
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01539"
FT BINDING 96
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01539"
FT BINDING 152
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01539"
FT BINDING 175
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01539"
SQ SEQUENCE 368 AA; 41662 MW; FD3BC090A115274C CRC64;
MTVTGIIAEF NPFHNGHKYL LETAEGLKII AMSGNFMQRG EPALIDKWIR SEMALKNGAD
IVVELPFFVS VQSADYFAQG AIDILCQLGI QQLAFGTENV IDYQKLIKVY EKKSEQMTAY
LSTLEDTLSY PQKTQKMWEI FAGVKFSGQT PNHILGLSYA KASAGKHIQL CPIKRQGAAY
HSKDKNHLLA SASAIRQHLN DWDFISHSVP NAGLLINNPH MSWDHYFSFL KYQILNHSDL
TSIFQVNDEL ASRIKKAIKV SQNIDHLVDT VATKRYTKSR VRRILTYILV NAKEPTLPKG
IHILGFTSKG QAHLKKLKKS RPLITRIGAE TWDEMTQKAD SIYQLGHQDI PEQSFGRIPI
IIKNERLN