ID A0A1I4S988_ECTMO Unreviewed; 689 AA.
AC A0A1I4S988;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=SAMN05421721_11437 {ECO:0000313|EMBL:SFM61042.1};
OS Ectothiorhodospira mobilis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Ectothiorhodospira.
OX NCBI_TaxID=195064 {ECO:0000313|EMBL:SFM61042.1, ECO:0000313|Proteomes:UP000199556};
RN [1] {ECO:0000313|EMBL:SFM61042.1, ECO:0000313|Proteomes:UP000199556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4180 {ECO:0000313|EMBL:SFM61042.1,
RC ECO:0000313|Proteomes:UP000199556};
RA de Groot N.N.;
RL Submitted (OCT-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; FOUO01000014; SFM61042.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I4S988; -.
DR STRING; 195064.SAMN05421721_11437; -.
DR OrthoDB; 5578851at2; -.
DR Proteomes; UP000199556; Unassembled WGS sequence.
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; 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; IPR013562; TmcA_N.
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 Pfam; PF08351; TmcA_N; 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:UP000199556};
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 412..552
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
FT BINDING 160
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01886"
FT BINDING 334
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01886"
FT BINDING 477..479
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01886"
SQ SEQUENCE 689 AA; 72739 MW; 9ADA5B0C15464D95 CRC64;
MPSDEIRLLP AGDPAHRRLV WLRGPAETAR ARAAAWCRQL AHTQRAAWVG MAPPAHLPVS
VCPPPQADTL LGRSLDALVF DAAEGIAPDA LGAAAGALCG GGVLLLILPV AGLSSPFGRR
MRRILEAALE AAPGDTPLPL PGTPPGAIQP DRDGCLTPDQ RRAVAALERL SRGRGGRPLV
LTADRGRGKS AALGIAAGRL LARARPGGRP PLRMVLTAPR LTAVAPVLER ARAALPPGQG
RRETAPLTGP GGHMEYLPPE AASRVPAELV LVDEAGGIPV QWLQRLLDAH GRIAFTTTLH
GYEGTGQGFA ARFCPLLYRR FPGTRFLHLE RPVRWAAGDP LEALLERLLL LGARPREVPP
VAEGRVERLS PQRLAGDEAL LEAVYGLLAL AHYRTRPSDL QRLLEDAAME TTVLWSGGAV
AAVALVAREG GLEPDLCRQV WAGRRRPRGH LLPVGLILHG GLAPDAGRLR YHRVVRIAVH
PGLQGRGLGG RLLAAVVQRA GDAGADAVGA SFGASAKLLA FWRGQGFAPV RVGVKPEVSS
GGWGVTVLRP LTPAGEGLAT AARQRFARAL APLLADPLAG MEPALAAGLW RGAAVAPPDP
DQARALAGFA HDQRVFEACL PELAVAVPWG LSDPARAAAL DACERDALVM RVLQHRDWDA
VARHARVHGR RGVIRLLRGA LARWLPPPG
//
