ID A0A1D8RTJ2_9GAMM Unreviewed; 742 AA.
AC A0A1D8RTJ2;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=tRNA(Met) cytidine acetyltransferase TmcA {ECO:0000256|HAMAP-Rule:MF_01886};
DE EC=2.3.1.193 {ECO:0000256|HAMAP-Rule:MF_01886};
GN Name=tmcA {ECO:0000256|HAMAP-Rule:MF_01886};
GN ORFNames=A3Q34_05970 {ECO:0000313|EMBL:AOW76446.1};
OS Colwellia sp. PAMC 20917.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Colwelliaceae; Colwellia.
OX NCBI_TaxID=1816218 {ECO:0000313|EMBL:AOW76446.1, ECO:0000313|Proteomes:UP000177820};
RN [1] {ECO:0000313|EMBL:AOW76446.1, ECO:0000313|Proteomes:UP000177820}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAMC 20917 {ECO:0000313|EMBL:AOW76446.1,
RC ECO:0000313|Proteomes:UP000177820};
RA Kim H.-W.;
RT "Complete genome sequence of Colwellia sp. PAMC 20917.";
RL Submitted (MAR-2016) 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:0000256|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:0000256|HAMAP-Rule:MF_01886};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01886}.
CC Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}.
CC -!- SIMILARITY: Belongs to the TmcA family. {ECO:0000256|HAMAP-
CC Rule:MF_01886}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01886}.
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DR EMBL; CP014944; AOW76446.1; -; Genomic_DNA.
DR RefSeq; WP_070374531.1; NZ_CP014944.1.
DR AlphaFoldDB; A0A1D8RTJ2; -.
DR STRING; 1816218.A3Q34_05970; -.
DR KEGG; coz:A3Q34_05970; -.
DR OrthoDB; 5578851at2; -.
DR Proteomes; UP000177820; 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 CDD; cd04301; NAT_SF; 1.
DR Gene3D; 3.40.50.11040; -; 1.
DR Gene3D; 3.40.630.30; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.20.120.890; tRNA(Met) cytidine acetyltransferase, tail domain; 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; N-ACETYLTRANSFERASE 10; 1.
DR PANTHER; PTHR10925:SF5; RNA CYTIDINE ACETYLTRANSFERASE; 1.
DR Pfam; PF13718; GNAT_acetyltr_2; 1.
DR Pfam; PF05127; Helicase_RecD; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315, ECO:0000256|HAMAP-
KW Rule:MF_01886};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01886};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01886};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01886}; Reference proteome {ECO:0000313|Proteomes:UP000177820};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_01886};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01886};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_01886};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|HAMAP-
KW Rule:MF_01886}.
FT DOMAIN 429..609
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
FT BINDING 184
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01886"
FT BINDING 367
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01886"
SQ SEQUENCE 742 AA; 83203 MW; 9127D8AABEE38B07 CRC64;
MSNRNFVEWL EEMQCQALSK FQRQLVLLVG DACWVKQLLQ LNEQNQSKDA WLVFSHHPEI
SATINNKHFA QQLGSEHSRI LFSGVENSDC SALNSINLDA FAALSGTLVA GGVMCLWLEK
PLIQAIEQTK KASLKYFYRQ LLDNKALITI SQSDEQTFPL LDDIAPAIST VSSDFLYQCK
TKEQQIAVEH IIKVSRGHRN RPLVLTADRG RGKSSALAIA CVELIANNTA MGHEKINIVI
TAPHVRSLSV FYRQLACSLA ALGEKFDYAN TSKTALVHPL GSITFVAVDQ LIRRDDSLNI
SLLLVDEAAA IPVPLLTSLT ALFSRVVFSS TVHGYEGAGR GFTVKFQQAL TKQVPQWRSF
HMHQPIRWRQ DDPLEVFVFE SCLLNAKLTE LPLLTQPVSE ISFNKTTLSQ SSTVQLAKES
LSFSQVSSTS LIEDTALLKQ VFAVLVTAHY QTSPNDITLL LDNKALQLFV AKLGDDIVGV
ALLLEEGCNK TADIQAIATN QRRLKNQFIP QSLLTHCGFS ESFSYQYLRV LRIAIHPQYQ
GYGFGRCFIK ALENFAKKQQ VDFIGASFGA NAQLLKFWQD ADYQIARIGF TKDQASGEHS
ALVVSAMSDR GQFFQRKIAS EFYSSFDYLL TDEYKGLSPK LVWQILHHCP DKSLPQLSAH
QLSSISDFVQ QKRQFSHCVK ALHYWCLLHC KENYQASILV LIERILQKKP VDEVCKNHQL
TGKKMLNQAL IDYIAQAQAQ AH
//
