ID   TMCAL_AGARV             Reviewed;         416 AA.
AC   C4Z916;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 65.
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=EUBREC_1493;
OS   Agathobacter rectalis (strain ATCC 33656 / DSM 3377 / JCM 17463 / KCTC 5835
OS   / VPI 0990) (Eubacterium rectale).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Lachnospiraceae incertae sedis.
OX   NCBI_TaxID=515619;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33656 / DSM 3377 / JCM 17463 / KCTC 5835 / LMG 30912 / VPI
RC   0990;
RX   PubMed=19321416; DOI=10.1073/pnas.0901529106;
RA   Mahowald M.A., Rey F.E., Seedorf H., Turnbaugh P.J., Fulton R.S.,
RA   Wollam A., Shah N., Wang C., Magrini V., Wilson R.K., Cantarel B.L.,
RA   Coutinho P.M., Henrissat B., Crock L.W., Russell A., Verberkmoes N.C.,
RA   Hettich R.L., Gordon J.I.;
RT   "Characterizing a model human gut microbiota composed of members of its two
RT   dominant bacterial phyla.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:5859-5864(2009).
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; CP001107; ACR75247.1; -; Genomic_DNA.
DR   RefSeq; WP_012742346.1; NC_012781.1.
DR   AlphaFoldDB; C4Z916; -.
DR   SMR; C4Z916; -.
DR   STRING; 515619.EUBREC_1493; -.
DR   PRIDE; C4Z916; -.
DR   EnsemblBacteria; ACR75247; ACR75247; EUBREC_1493.
DR   KEGG; ere:EUBREC_1493; -.
DR   HOGENOM; CLU_038915_0_1_9; -.
DR   OMA; WARTKMA; -.
DR   OrthoDB; 1547014at2; -.
DR   Proteomes; UP000001477; 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:0009058; P:biosynthetic process; IEA:InterPro.
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; IPR004821; Cyt_trans-like.
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.
DR   TIGRFAMs; TIGR00125; cyt_tran_rel; 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..416
FT                   /note="tRNA(Met) cytidine acetate ligase"
FT                   /id="PRO_1000215423"
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         170
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01539"
FT   BINDING         193
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01539"
SQ   SEQUENCE   416 AA;  46138 MW;  81EB271E9FAED790 CRC64;
     MKVAGVITEY NPFHNGHKYQ LEQIKRQTSA DYIVVVMSGD FVQRGEPAII DKYERTRMAL
     LSGADLVLEL PSVFATASAE FFAGGGVSVL KNTGVVDMLC YGVESVDHEL TKLVAGVLKN
     PPSEYSASLA RLIQGGMSFP AARSRALCEY FRDTYDSASE KLDAFIASPN NILAIEYEKA
     LMDCDITGFP IQRVGEGYHS TDSTSEFSSA TAVRGVISTL IDIDKHNTIT NMQLDNSWIS
     TKFSQLIPSA CADILVNCIL GGHIVFPDDI SEMLYYRLLT GKDKGFAQYA DCTKELSAKI
     VKNIYKYEGF TQFCNLLKSK NLTYTRISRV LTHILLGIEN NDFNICMNNP YLRILGFKKS
     SGELMHLLKK RASVPIITKV ADAPYELISK DIFAADLYGR LCHSQQNEFT HGVVII