TMCA_YERPD
ID TMCA_YERPD Reviewed; 699 AA.
AC D0JFM7; D0JFM6;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 2.
DT 03-AUG-2022, entry version 58.
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};
GN OrderedLocusNames=YPD4_2678/YPD4_2679;
OS Yersinia pestis (strain D106004).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=637382;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D106004;
RX PubMed=19815893; DOI=10.4269/ajtmh.2009.09-0174;
RA Zhang Z., Hai R., Song Z., Xia L., Liang Y., Cai H., Liang Y., Shen X.,
RA Zhang E., Xu J., Yu D., Yu X.J.;
RT "Spatial variation of Yersinia pestis from Yunnan Province of China.";
RL Am. J. Trop. Med. Hyg. 81:714-717(2009).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ACY59585.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=ACY59586.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; CP001585; ACY59585.1; ALT_FRAME; Genomic_DNA.
DR EMBL; CP001585; ACY59586.1; ALT_FRAME; Genomic_DNA.
DR AlphaFoldDB; D0JFM7; -.
DR SMR; D0JFM7; -.
DR KEGG; ypd:YPD4_2678; -.
DR KEGG; ypd:YPD4_2679; -.
DR PATRIC; fig|637382.3.peg.3562; -.
DR HOGENOM; CLU_085975_0_0_6; -.
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; 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; 2.
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; RNA-binding;
KW Transferase; tRNA processing; tRNA-binding.
FT CHAIN 1..699
FT /note="tRNA(Met) cytidine acetyltransferase TmcA"
FT /id="PRO_0000403128"
FT DOMAIN 359..543
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
FT BINDING 179
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
FT BINDING 201..210
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
FT BINDING 323
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
FT BINDING 471..473
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
FT BINDING 511
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
FT BINDING 518
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
SQ SEQUENCE 699 AA; 78263 MW; AEA990F0A4D51252 CRC64;
MTNPIVASQP QMAQQGIRRL LILSGQADWS RQQAIMLRQH LAGDWLWLSE QPPEGVNSIS
PTAARTLLGQ ENLHGVFDAT DGLNIEALAI VAGTLRAGSW LLLLVPEWDD WPQRPDKDSL
RWSEQPAPIV TANFIRHLQR QFLADPDVVL WQQDRPLILP AVGSRPCWQQ PDGSPTAQQQ
HILQRLMQAD SGIWVLTAAR GRGKSTLAGM LVTHWQGACW VTGPGKAATQ VLNQQAGERA
RFWAPDALLD YCQRHDVSDI DWLLIDEAAA IPTPLLSALL AYFPRALLTT TVQGYEGTGR
GFLLKFCATL GDWHHLTLTD PIRWATDDPL ERVMDNAMLF HDELLGNHPL PKRPPVAQIE
IPLYEQRDWR DNPELLRRFY GLLSTAHYRT TPLDLRRLMD APGMHFSAAR VADAVIGALW
LVDEGGLSEA LALDVWAGRR RPRGNLVAQS LAAHSGQWQA PTLLSRRISR VAVTAAWRQQ
GIARRMIAAE QAHARQQQCD FLSVSFGYTA ELAHFWHRCG FRLVRIGSHK EASSGCYTAM
ALLPLSPAGE ALCQAAQQQL KRDWYWLQQW IGIPTPVFLR LPEPPEVTLT DDDWRELAGF
AFAFRPLEAS LPALQRLLLH TELPLSALRH YLQLRTPQSE IINTLGLIGR KALVALWRQE
AAEGMAMIDV DKMIMSAKPS ARCSTVRLPG RKNLTICQC
