TMCA_SALTY
ID TMCA_SALTY Reviewed; 672 AA.
AC Q8ZN74;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 107.
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=STM2485;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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; AE006468; AAL21379.1; -; Genomic_DNA.
DR RefSeq; NP_461420.1; NC_003197.2.
DR RefSeq; WP_001279831.1; NC_003197.2.
DR AlphaFoldDB; Q8ZN74; -.
DR SMR; Q8ZN74; -.
DR STRING; 99287.STM2485; -.
DR PaxDb; Q8ZN74; -.
DR EnsemblBacteria; AAL21379; AAL21379; STM2485.
DR GeneID; 1254007; -.
DR KEGG; stm:STM2485; -.
DR PATRIC; fig|99287.12.peg.2623; -.
DR HOGENOM; CLU_004652_1_1_6; -.
DR OMA; NEPDDLG; -.
DR PhylomeDB; Q8ZN74; -.
DR BioCyc; SENT99287:STM2485-MON; -.
DR Proteomes; UP000001014; 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; IBA:GO_Central.
DR GO; GO:0051392; F:tRNA N-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0051391; P:tRNA acetylation; IBA:GO_Central.
DR GO; GO:0002101; P:tRNA wobble cytosine modification; IBA:GO_Central.
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; IPR013562; TmcA_N.
DR InterPro; IPR033442; TmcA_tRNA_bind.
DR InterPro; IPR024914; tRNA_acetyltr_TmcA.
DR PANTHER; PTHR10925; PTHR10925; 2.
DR Pfam; PF08351; DUF1726; 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..672
FT /note="tRNA(Met) cytidine acetyltransferase TmcA"
FT /id="PRO_0000403124"
FT DOMAIN 349..531
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
FT BINDING 180
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
FT BINDING 202..211
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
FT BINDING 319
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
FT BINDING 461..463
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
FT BINDING 468..474
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
FT BINDING 506
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
SQ SEQUENCE 672 AA; 74016 MW; 1575C39686D427FC CRC64;
MSDIDALQAL TSQMTQEGIR RLLVISGDAA WCRKRAEAIR AALPGDWLWV APDAPAQPCC
TPQALQTLLG REFRHAIFDA WQGFDAAAFA ALSGTLQAGS WLLLLMPPYE TWESRPDTDS
LRWSDCAQPI PTPQFAQHLK RTLSRDPQTL LWRQRQPFCW PSYPSRECWR PATGEPQPEQ
AAILSRLREM PPGVATVIAP RGRGKSALAG QFISRMAGTA IVTAPAKTAT DILAAFAGER
FCFMAPDALL ASGARADWLV VDEAAAIPTP LLLQLVSRFP RILLTTTVQG YEGTGRGFLL
KFCARFPQLH RFTLRQPVRW APECPLENIV SEALIFDDEA FAQAPHGAIE ISAFYQQAWV
NTPALPRAVY QLLSGAHYRT SPLDLRRMMD APGQHFLQAT ANNRVAGALW LVEEGGLSAE
LSQAVWCGFR RPRGNLVAQS LAAHGSDPLA ATLVGRRVSR IAVHPARQRE GIGQQLIACA
CMQAAQCDYL SVSFGYTPKL WRFWQRCGFV LVRMGNHREA SSGCYTAMAL LPLSDAGKRL
AQQEHRRLRR DADILTQWNG EAIPLAALRE QALNDEDWRE LVGFAFAHRP LLTSLGCLHR
LLQYSALPLP ALRGRLEEKA SDAELCARLR ISGRKALLAL QRAQAAQALI ALDAGRTQSL
RDVMPGGGDH AG
