ID N9VF82_9GAMM Unreviewed; 674 AA.
AC N9VF82;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 49.
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=G114_00745 {ECO:0000313|EMBL:ENY73927.1};
OS Aeromonas diversa CDC 2478-85.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=1268237 {ECO:0000313|EMBL:ENY73927.1, ECO:0000313|Proteomes:UP000023775};
RN [1] {ECO:0000313|EMBL:ENY73927.1, ECO:0000313|Proteomes:UP000023775}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2478-85 {ECO:0000313|EMBL:ENY73927.1,
RC ECO:0000313|Proteomes:UP000023775};
RX PubMed=23792745; DOI=10.1128/genomeA.00330-13;
RA Farfan M., Spataro N., Sanglas A., Albarral V., Loren J.G., Bosch E.,
RA Fuste M.C.;
RT "Draft Genome Sequence of the Aeromonas diversa Type Strain.";
RL Genome Announc. 1:S69-S82(2013).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ENY73927.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; APVG01000001; ENY73927.1; -; Genomic_DNA.
DR RefSeq; WP_005345874.1; NZ_CDCE01000020.1.
DR AlphaFoldDB; N9VF82; -.
DR PATRIC; fig|1268237.3.peg.147; -.
DR eggNOG; COG1444; Bacteria.
DR OrthoDB; 5578851at2; -.
DR Proteomes; UP000023775; 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 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; IPR013562; TmcA_N.
DR InterPro; IPR033442; TmcA_tRNA_bind.
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 Pfam; PF17176; tRNA_bind_3; 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};
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 383..536
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
FT BINDING 165
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01886"
FT BINDING 319
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01886"
FT BINDING 501
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01886"
SQ SEQUENCE 674 AA; 74955 MW; AB1D10EDB0092598 CRC64;
MTLREGLRQA GERRLIWLEG EEQECIAKTR EWLDGHIVWL GEGPAEHSPL PAAKALRYLG
RECDTLVCNA FSGFHPDAFG ALSGTLRAGG LLLLLTPPRA RWPIYADPDR LRLIADPVDL
PRCGQGFIER MVRLLSQDPA LALELPEGVP SWQPLGLERP RTADQEAAIQ AIGQVLRGHR
KRPLVLSADR GRGKSSALGM AAAALLTEEP GLRIGITAPA QATLSTLLLH AGEDKRLLFF
SPDRLLEERP ALDLLLVDEA AAIPTPLLEG LLAHYHRMVF ATTEHGYEGT GRGFHLRFKR
TLDRRTPGWR ELHMQAPIRW SDNDPLEPLV NRLLALSAEP PTPLLTAPPR WEPVSAASLT
HDEDRLSALF GLLVLAHYQT SPSDLRALLE CPDLDIHQLC SGGSLLGVAL VMREGPIPSA
LAEEIWAGRR RPRGQLLPQS LLAHSGVRPA ADRRFARVMR IAIHPSLHRK GLGAQLLTAL
EDHYRAQQFD YLGSAFSAGV ELLPFWLNRR LRVVRIGLQR DAASGCHSLL MLKALTPALE
PELDEWQRRF LLGLPSLLAG ELRTVSAELL AQCLPGSPLT PLPGLESWEW EELACFAHHH
KPFELCQGTL QRWLLTRHAE LAQWSQQEQR LMVGAIWQYK SWESLARELG LSGRGAVITQ
LREQIGSRID HNQL
//
