TMCA_CITK8
ID TMCA_CITK8 Reviewed; 671 AA.
AC A8ADB3;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 87.
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=CKO_00313;
OS Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Citrobacter.
OX NCBI_TaxID=290338;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-895 / CDC 4225-83 / SGSC4696;
RG The Citrobacter koseri Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA Latreille P., Courtney L., Wang C., Pepin K., Bhonagiri V., Nash W.,
RA Johnson M., Thiruvilangam P., Wilson R.;
RL Submitted (AUG-2007) 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; CP000822; ABV11476.1; -; Genomic_DNA.
DR RefSeq; WP_012131306.1; NC_009792.1.
DR AlphaFoldDB; A8ADB3; -.
DR SMR; A8ADB3; -.
DR STRING; 290338.CKO_00313; -.
DR EnsemblBacteria; ABV11476; ABV11476; CKO_00313.
DR GeneID; 45134588; -.
DR KEGG; cko:CKO_00313; -.
DR HOGENOM; CLU_004652_1_1_6; -.
DR OMA; NEPDDLG; -.
DR OrthoDB; 1019071at2; -.
DR Proteomes; UP000008148; 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; 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;
KW Reference proteome; RNA-binding; Transferase; tRNA processing;
KW tRNA-binding.
FT CHAIN 1..671
FT /note="tRNA(Met) cytidine acetyltransferase TmcA"
FT /id="PRO_0000403118"
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 499
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 671 AA; 74172 MW; 2E3C2987F8A47582 CRC64;
MSDNDALRAL TAQMAQEGIR RLLVLSGDVS WCRERALALR EALAGDWLWV ATDAPAAPHC
TPQALQTLLG REFRHAVFDA QLGFDASAFA ALSGTLRAGS WLVLLTPPYS AWESRPDADS
LRWSDCPQPV ATPHFIQHLK RVMARDEQTL HWQQSQPFSW PRFPARPHWQ PATGEPQPEQ
AAILRHLLRM PPGVAAVTAA RGRGKSALAG QLISRMSGTA IVTAPSKAAT DVLAQFAGEK
FRFLAPDALL AGTETADWLI VDEAAAIPAP LLHRLASRFS RILLTTTVQG YEGTGRGFLL
KFCARFPHLR RFELRQPVRW AQGCPLEQWV GEALIFDDET FAHAPQGAIR FSAFTQALWH
TGPAQPLAVY QLLSGAHYRT SPLDLRRMMD APGQHFLGAF TAERVAGAAW LVEEGRLSAA
LSQAVWAGYR RPRGNLVAQS LAAHGGDPLA ATLTGRRVSR IAVHPARQRE GIGQQLIAEA
YGGASRCDYL SVSFGYTAEL WRFWQRCGFV LVRMGNHKEA SSGCYTAMAL LPISEAGARL
AHREHQRLRR DAEILARWNG EAIPVIPLKA STLNDDDWDE LAGFAFAHRP LLTSLGSLSR
LLERCELALP ALRGRLEEKC SDANLCIRLG LPGRKALLVA QRREVAHALT ALDDERAQRL
RERVLQWQFF H
