TMCA_VIBCH
ID TMCA_VIBCH Reviewed; 708 AA.
AC Q9KKJ5;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 100.
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=VC_A1112;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
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; AE003853; AAF97003.1; -; Genomic_DNA.
DR PIR; A82377; A82377.
DR RefSeq; NP_233491.1; NC_002506.1.
DR AlphaFoldDB; Q9KKJ5; -.
DR SMR; Q9KKJ5; -.
DR STRING; 243277.VC_A1112; -.
DR DNASU; 2612182; -.
DR EnsemblBacteria; AAF97003; AAF97003; VC_A1112.
DR KEGG; vch:VC_A1112; -.
DR PATRIC; fig|243277.26.peg.3718; -.
DR eggNOG; COG1444; Bacteria.
DR HOGENOM; CLU_004652_1_0_6; -.
DR OMA; NEPDDLG; -.
DR BioCyc; VCHO:VCA1112-MON; -.
DR Proteomes; UP000000584; Chromosome 2.
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; IPR024914; tRNA_acetyltr_TmcA.
DR PANTHER; PTHR10925; PTHR10925; 2.
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..708
FT /note="tRNA(Met) cytidine acetyltransferase TmcA"
FT /id="PRO_0000403126"
FT DOMAIN 398..574
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
FT BINDING 189
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
FT BINDING 215..224
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
FT BINDING 357
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
FT BINDING 502..504
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
FT BINDING 509..515
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
SQ SEQUENCE 708 AA; 79285 MW; BA3CE3815746E344 CRC64;
MFPPSYDAFQ GVTAIGWACA NMAHHFGISL VMTQPITYLL QLQQLAKQGQ TRFGCWLRGD
AQWQHHLLKT LVPHFAEQPI LMLGQTELEG VTCVDYRQGQ QWLGRECQLL IVDLTQGWDA
NSFNAVLGTL VGGGLLLVVG EPTTLNHCAR VWLERACHRL LVITPQTVPA LPNSDSVTRT
NTEQTYTEQR LAIDSIIKVV TGHRKRPLVL TADRGRGKTS ALGLAAAELM SSRSMHIVVT
APTLAAVEPL FVHAQRTLPQ AHRQRGEVQT AQSSLRFMAP DELLRTQPES DLLLVDEAAA
LPLPFLKRWV ERYHRAVFSS TIHGYEGCGR GFSLKFQSWL QVQRPQMRSL HLEQPIRWAA
GDALEQWQNQ VFLLQSELPE VALEQAREPL SFSLFSQPEC VEQPERLAQV FALLVNAHYQ
TSPNDLFALL QDEAMTLFVA YQGEVCVGCV LAVREGELDA PTIEAIQLGT RRPKGHLTPV
TLANQLGISQ AARQSCWRIL RIAVHPDCQR QGIGSQLLTH FIAQHHADYY ATSFGVSEDL
LPFWLANHFV PIKLGSHRDQ ASGCYSLLMV RGEHLDWLEQ AKQQFSAHWI FELSDSLQAL
EPQIIQQLLP STVALPQPLI PLELIERYAR GGANYESVAV WLYAWLLATA PSLESLSPLL
ISKILQRKSW AACAEQFQLS GKRQVEQAVR TEILALLVNL QCKYTLPI
