ID   TMCA_HAEDU              Reviewed;         598 AA.
AC   Q7VLN6;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=tRNA(Met) cytidine acetyltransferase TmcA {ECO:0000255|HAMAP-Rule:MF_01886};
DE            EC=2.3.1.193 {ECO:0000255|HAMAP-Rule:MF_01886};
GN   Name=tmcA {ECO:0000255|HAMAP-Rule:MF_01886}; OrderedLocusNames=HD_1386;
OS   Haemophilus ducreyi (strain 35000HP / ATCC 700724).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=233412;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=35000HP / ATCC 700724;
RA   Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., Johnson L.,
RA   Nguyen D., Wang J., Forst C., Hood L.;
RT   "The complete genome sequence of Haemophilus ducreyi.";
RL   Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at
CC       the wobble position of tRNA(Met), by using acetyl-CoA as an acetyl
CC       donor and ATP (or GTP). {ECO:0000255|HAMAP-Rule:MF_01886}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + ATP + cytidine(34) in elongator tRNA(Met) + H2O =
CC         ADP + CoA + H(+) + N(4)-acetylcytidine(34) in elongator tRNA(Met) +
CC         phosphate; Xref=Rhea:RHEA:43788, Rhea:RHEA-COMP:10693, Rhea:RHEA-
CC         COMP:10694, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:74900, ChEBI:CHEBI:82748, ChEBI:CHEBI:456216;
CC         EC=2.3.1.193; Evidence={ECO:0000255|HAMAP-Rule:MF_01886};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01886}.
CC   -!- SIMILARITY: Belongs to the RNA cytidine acetyltransferase family. TmcA
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01886}.
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DR   EMBL; AE017143; AAP96199.1; -; Genomic_DNA.
DR   RefSeq; WP_010945248.1; NC_002940.2.
DR   AlphaFoldDB; Q7VLN6; -.
DR   SMR; Q7VLN6; -.
DR   STRING; 233412.HD_1386; -.
DR   EnsemblBacteria; AAP96199; AAP96199; HD_1386.
DR   KEGG; hdu:HD_1386; -.
DR   eggNOG; COG1444; Bacteria.
DR   HOGENOM; CLU_004652_1_1_6; -.
DR   OMA; NEPDDLG; -.
DR   Proteomes; UP000001022; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0051392; F:tRNA N-acetyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0051391; P:tRNA acetylation; IEA:UniProtKB-UniRule.
DR   GO; GO:0002101; P:tRNA wobble cytosine modification; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.20.120.890; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_01886; tRNA_acetyltr_TmcA; 1.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR000182; GNAT_dom.
DR   InterPro; IPR007807; Helicase_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR032672; TmcA/NAT10/Kre33.
DR   InterPro; IPR038321; TmcA_C_sf.
DR   InterPro; IPR033442; TmcA_tRNA_bind.
DR   InterPro; IPR024914; tRNA_acetyltr_TmcA.
DR   PANTHER; PTHR10925; PTHR10925; 1.
DR   Pfam; PF13718; GNAT_acetyltr_2; 1.
DR   Pfam; PF05127; Helicase_RecD; 1.
DR   Pfam; PF17176; tRNA_bind_3; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF55729; SSF55729; 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; ATP-binding; Cytoplasm; Nucleotide-binding;
KW   Reference proteome; RNA-binding; Transferase; tRNA processing;
KW   tRNA-binding.
FT   CHAIN           1..598
FT                   /note="tRNA(Met) cytidine acetyltransferase TmcA"
FT                   /id="PRO_0000403120"
FT   DOMAIN          332..490
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
FT   BINDING         141
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
FT   BINDING         163..172
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
FT   BINDING         288
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
FT   BINDING         411..413
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
FT   BINDING         418..424
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
FT   BINDING         462
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
SQ   SEQUENCE   598 AA;  68448 MW;  CDCEE1BDB394C9A1 CRC64;
     MRQLVILSTM PPIQGGVLLN SQNFSKAKQF LGQEYPFALY DMRSENGICF NLEAFAIIVG
     TIQENGTLYL ICPNWHSVEQ QIDVDAIRWN GGVAIACPHF FQHFKRLINK FGFEVTSRPQ
     QPFIKTAPSY PAKLIQFTDE QQNILQKLPL DPAEIHIITA ARGRGKSTLA GKLAEQFAKT
     EQVILTAHRS SSIQKILQTA SINIPFFAPD KLLNLIETKQ ISADHLLFID EAACIPLPIL
     QQLGNYFKKV ILTTTTQNYE GTGRGFKLKL VKQLHRTTKE WQLFQPLRWS NHDRLEQFTN
     ELLLLNDELI PLDQNSQFYH LLANAHYKTT ATDLRRLFDA DQQLFHQCYD KNQRLMAGIW
     AVKEGELSQD LAEAIWAGKR RPAGNLVAQY LCCQGNLIEA CQLKSIRISR IAVQPDLQNQ
     GIGSQLVTDF MQKMQKNNKN RPLDFISVSF GITPHLLTFW RRNGFQLVQI TPTKEASSGY
     HSAMMLYPLS QQGKQFVTKA VKQFERDLAL QPFYPTLKNC LAIPAQVENE MNQDDWQNLH
     GFAFAQRSLA NCYTSLKRLY ITHQAQLTIL APLFTHRYPA NQKVWLQQCR IAIRPFIQ