TMCA_THEPD
ID TMCA_THEPD Reviewed; 801 AA.
AC A1RY08;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 88.
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=Tpen_0686;
OS Thermofilum pendens (strain DSM 2475 / Hrk 5).
OC Archaea; Crenarchaeota; Thermoprotei; Thermofilales; Thermofilaceae;
OC Thermofilum.
OX NCBI_TaxID=368408;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2475 / Hrk 5;
RX PubMed=18263724; DOI=10.1128/jb.01949-07;
RA Anderson I., Rodriguez J., Susanti D., Porat I., Reich C., Ulrich L.E.,
RA Elkins J.G., Mavromatis K., Lykidis A., Kim E., Thompson L.S., Nolan M.,
RA Land M., Copeland A., Lapidus A., Lucas S., Detter C., Zhulin I.B.,
RA Olsen G.J., Whitman W., Mukhopadhyay B., Bristow J., Kyrpides N.;
RT "Genome sequence of Thermofilum pendens reveals an exceptional loss of
RT biosynthetic pathways without genome reduction.";
RL J. Bacteriol. 190:2957-2965(2008).
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; CP000505; ABL78088.1; -; Genomic_DNA.
DR RefSeq; WP_011752353.1; NC_008698.1.
DR AlphaFoldDB; A1RY08; -.
DR SMR; A1RY08; -.
DR STRING; 368408.Tpen_0686; -.
DR EnsemblBacteria; ABL78088; ABL78088; Tpen_0686.
DR GeneID; 4601886; -.
DR KEGG; tpe:Tpen_0686; -.
DR eggNOG; arCOG01951; Archaea.
DR HOGENOM; CLU_004652_1_0_2; -.
DR OMA; NEPDDLG; -.
DR OrthoDB; 2707at2157; -.
DR Proteomes; UP000000641; 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; 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; IPR013562; TmcA_N.
DR InterPro; IPR024914; tRNA_acetyltr_TmcA.
DR PANTHER; PTHR10925; PTHR10925; 2.
DR Pfam; PF08351; DUF1726; 1.
DR Pfam; PF13718; GNAT_acetyltr_2; 2.
DR Pfam; PF05127; Helicase_RecD; 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..801
FT /note="tRNA(Met) cytidine acetyltransferase TmcA"
FT /id="PRO_0000403134"
FT DOMAIN 457..637
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
FT BINDING 228
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
FT BINDING 256..265
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
FT BINDING 412
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
FT BINDING 562..564
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
FT BINDING 569..575
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
FT BINDING 602
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
SQ SEQUENCE 801 AA; 91017 MW; 51B4087CCD7C384E CRC64;
MPLVPLEHLD EVREELVKAR KSRHRRLLVI TGDDDSRLVT TALDFIYNVK DLLSGEKVLY
TYHAFYSDGA MRKELFEKGV PRELSVDYVS YHKLDEVLGR TYAAAVADLV NNLEPNDLGR
VMGVVEGGGL YIFLLPSFTR LLETVTRFQS NLIVPGYTDK DLKRYFEKRF IKKVMEHQGV
AVYDADNRYW VKKFGKTPST PYARPKPVLP QKSKIPVKVF NLALTQDQVE VLKIFEHFYA
KAEKEKLVFV LTADRGRGKS SAVGLGVGWL AHRLRRAKGK CKVVVTAPAV TNVQEVFRFS
AAVLDLFKHK VEVLEDESGM ITKLLSKGIE IEYVTPLDVL KAKGDLLVVD EAASIPVPLL
FKMLKRFNKV VYSSTIHGYE GAGRGFSLRF LKRLKNEEGV KLYEYEMSEP IRYAPEDPIE
KWTFDLLLLD AEPCEITEDD LSLVSAGEVY YDAPNEEELF LKNEEELRQF FGIYIMAHYR
NNPNDLGIMM DAPHHFLRMV RLKNGKIVVS LELASEGNLG EDLSKESAKG AWLMGNIIPD
RLIKHYKILD FGNLRGIRVV RIATHPSVMG KGLGSFALSR LEEEARRNGY DWVGAGFGVT
YELLKFWLKN GYIPVHMSPE KNPVSGEYTV IVVKPLSEKA KRIVDVIAKE FKQKLLGSLA
SPYFDLEPEV ALLLLKSTPS FEVKVNLTKL QLARFLTYAW SDMTLENCID VVGIMTRLYF
LSKKKPSLSE LQELLLVSKI LQAKSWHLTC QELNLSLAEA TSNMKQIAQI FSKEFLGVNS
EEEALRYFFL RMDDLNEGVS A
