ID I3YH06_THIV6 Unreviewed; 793 AA.
AC I3YH06;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 59.
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 OrderedLocusNames=Thivi_4477 {ECO:0000313|EMBL:AFL76274.1};
OS Thiocystis violascens (strain ATCC 17096 / DSM 198 / 6111) (Chromatium
OS violascens).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Thiocystis.
OX NCBI_TaxID=765911 {ECO:0000313|EMBL:AFL76274.1, ECO:0000313|Proteomes:UP000006062};
RN [1] {ECO:0000313|EMBL:AFL76274.1, ECO:0000313|Proteomes:UP000006062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17096 / DSM 198 / 6111
RC {ECO:0000313|Proteomes:UP000006062};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Teshima H., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Vogl K., Liu Z.,
RA Frigaard N.-U., Bryant D., Woyke T.;
RT "Complete sequence of Thiocystis violascens DSM 198.";
RL Submitted (JUN-2012) 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; CP003154; AFL76274.1; -; Genomic_DNA.
DR RefSeq; WP_014780648.1; NC_018012.1.
DR AlphaFoldDB; I3YH06; -.
DR STRING; 765911.Thivi_4477; -.
DR KEGG; tvi:Thivi_4477; -.
DR eggNOG; COG1444; Bacteria.
DR HOGENOM; CLU_004652_1_0_6; -.
DR Proteomes; UP000006062; 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; 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; 2.
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:UP000006062};
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 496..639
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
FT REGION 182..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 250
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01886"
FT BINDING 416
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01886"
FT BINDING 564..566
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01886"
FT BINDING 604
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01886"
FT BINDING 611
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01886"
SQ SEQUENCE 793 AA; 85876 MW; 83ECBDB6516A270A CRC64;
MIVAHALSVD LVRNLWEQAR ASHHRRVLLL AGAADWTASG ARLAVAALPE LSPVWLTQRP
LADSIRPIRD AIQLLGQDLE LLIYDAHGGF DPDGFGAATG AIRGGGLLIL LTPPLADWPN
RSDPEAERIA VWPHSADSLT GRFLARLVRV LMADPTIVAI QQQDLLLSLP DWTASQPAGC
ATPGLNEAEG RSVTSVTVPS PKDERRRVED GHGPWPLPIL RSVEPARAET PERIRPGVLR
PRAEPVTLDQ QQAVDAILKT SHGRARRPLV LTAHRGRGKS AALGLAAGHL LHAGECRILV
TAPRRASVDP VFRHAEAVLR ETEHPEVAAA IGKLSFQSPA ELIAAGPDAD LLLVDEAAGI
PAPLLETLLA RYPRVVFATT VHGYEGTGRG FEIRFRATLD RLTPNWRALR LDTPIRWAPA
DPLETLTFRA LLLDAAPAPD DQLTAASPAT CRCERLDPEA LAQDEPTLRE LFGLLVLAHY
QTRPMDLRML LDGANVRIYV LRHGERIAAT LLAAEEGGFA DPALRESIYL GQRRPRGHLL
PQTLSAHAGL LEAPAFRYLR VIRIAVHPAL IGRGLGRRLL RALFRDGRAD GIDLAGASFG
ATPELLRFWD RCGYRPVQIG TSRNAASGEQ AVVVLRRLNV HGWRFAALAR QRLASRLPVL
LAGPLRALSP DVAVALLASL PAGTESPTQA RESRHELAGF VSGHRTLDAT LPLLAHMTRH
QLRTSLDAGS ITPREAALLV ATACQLRPMA ELISIFLFPG HSGLLSDLRR IAGQLRNPDK
AETANDDNGH ALG
//
