TMCAL_CLOBJ
ID TMCAL_CLOBJ Reviewed; 409 AA.
AC C1FSR0;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 51.
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=CLM_2790;
OS Clostridium botulinum (strain Kyoto / Type A2).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=536232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Kyoto / Type A2;
RA Shrivastava S., Brinkac L.M., Brown J.L., Bruce D., Detter C.C.,
RA Johnson E.A., Munk C.A., Smith L.A., Smith T.J., Sutton G., Brettin T.S.;
RT "Genome sequence of Clostridium botulinum A2 Kyoto.";
RL Submitted (OCT-2008) 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; CP001581; ACO86937.1; -; Genomic_DNA.
DR RefSeq; WP_012705595.1; NC_012563.1.
DR AlphaFoldDB; C1FSR0; -.
DR SMR; C1FSR0; -.
DR STRING; 536232.CLM_2790; -.
DR EnsemblBacteria; ACO86937; ACO86937; CLM_2790.
DR KEGG; cby:CLM_2790; -.
DR eggNOG; COG1323; Bacteria.
DR HOGENOM; CLU_038915_0_1_9; -.
DR OMA; WARTKMA; -.
DR Proteomes; UP000001374; 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..409
FT /note="tRNA(Met) cytidine acetate ligase"
FT /id="PRO_1000185217"
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 169
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01539"
FT BINDING 194
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01539"
SQ SEQUENCE 409 AA; 46808 MW; 5F60EB883AFFBAD4 CRC64;
MNVSAIVVEY NPMHNGHLYH IKKTKKLTNC DALVCIMSGN FVQRGFPSIL DKWTKANIAI
SNGVDLVIEL PTLYSLSSAE FFSFGAVSIL DSLNIINSIC FGSEIGNINA LQDIATTLLE
EPLEYKILLK NYLDKGISFA KARNLALVEL NRDNKIMSEN ISKILSLSNN ILGIEYLKSL
LLLNSSIKPF TITREGADYK DENLHEEYSS ASSIRKYLKE NKNINILKDF LPLEGFLEFK
RLITKGYNFS MEDSMINYIR YKYISGYKNL HNLIDVSEGL DNRIYKSLEK NFTYDSLVGE
IKSKRYAYSR IGRILCQYFI GFENYDLNSL LKSTPNYMRV LASNEMGLKV LKKIKKHSSI
NIYTKLPKNT NTLLSLDIKA TNAYSLLNNN IRFNEDYFRS PTIIKNTIY