TMCAL_ACET2
ID TMCAL_ACET2 Reviewed; 415 AA.
AC A3DF04;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 67.
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=Cthe_1301;
OS Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC
OS 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Clostridium thermocellum).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Oscillospiraceae;
OC Acetivibrio.
OX NCBI_TaxID=203119;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL
RC B-4536 / VPI 7372;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Wu J.H.D.,
RA Newcomb M., Richardson P.;
RT "Complete sequence of Clostridium thermocellum ATCC 27405.";
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000568; ABN52533.1; -; Genomic_DNA.
DR RefSeq; WP_004463686.1; NC_009012.1.
DR AlphaFoldDB; A3DF04; -.
DR SMR; A3DF04; -.
DR STRING; 203119.Cthe_1301; -.
DR EnsemblBacteria; ABN52533; ABN52533; Cthe_1301.
DR KEGG; cth:Cthe_1301; -.
DR eggNOG; COG1323; Bacteria.
DR HOGENOM; CLU_038915_0_1_9; -.
DR OMA; WARTKMA; -.
DR OrthoDB; 1547014at2; -.
DR Proteomes; UP000002145; 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..415
FT /note="tRNA(Met) cytidine acetate ligase"
FT /id="PRO_0000300170"
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 165
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01539"
FT BINDING 190..191
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01539"
SQ SEQUENCE 415 AA; 46456 MW; BF424EB421BC27E5 CRC64;
MKVLGLIVEY NPFHNGHLYH LEESKKISGA DFVVCVMSGN FIQRGEPAIV NKWARTKMAL
SAGADLVIEL PLSCAMASAE YFASGAVRIL NDIGIVDYIC FGSEHGDVKT LDYIAQILVE
EPESYKSFLK EELDNGLSYP AARESALKKY TAHSINIPQI ISSSNNILGI EYLKALRRIK
SSIIPLTIKR INNDYNTENI TGSISSASSI RKYISTSNST SFDDVLAMTM PKTSVDILFE
EFSAGRGPVF KEDFYPVVTS LIRKMTPEQI RNFAYVSEGL ENRIKSAADT AGTYEELVES
ICTRRYTKTR VQRILMGILM GVTSKDLDML SRFDSPQYAR ILGFNSKGKQ LLSQIKKKSS
IPLVLKLSDF IKSCDPVLKR KLELEILATD LYVMCYKNPA FRKAGQEFTQ NIIIM
