ID A0A2N1A8G3_9GAMM Unreviewed; 634 AA.
AC A0A2N1A8G3;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=CXF74_00905 {ECO:0000313|EMBL:PKG40934.1};
OS Psychromonas sp. Urea-02u-13.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Psychromonadaceae; Psychromonas.
OX NCBI_TaxID=2058326 {ECO:0000313|EMBL:PKG40934.1, ECO:0000313|Proteomes:UP000233836};
RN [1] {ECO:0000313|EMBL:PKG40934.1, ECO:0000313|Proteomes:UP000233836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Urea-02u-13 {ECO:0000313|EMBL:PKG40934.1,
RC ECO:0000313|Proteomes:UP000233836};
RA Collins E., Ducluzeau A.-L.;
RT "Pharmacopeia of the Arctic Ocean.";
RL Submitted (DEC-2017) 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}.
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:PKG40934.1}.
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DR EMBL; PJBZ01000035; PKG40934.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N1A8G3; -.
DR OrthoDB; 5578851at2; -.
DR Proteomes; UP000233836; 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; 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.
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 37..96
FT /note="tRNA(Met) cytidine acetyltransferase TmcA N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08351"
FT DOMAIN 149..299
FT /note="Helicase"
FT /evidence="ECO:0000259|Pfam:PF05127"
FT DOMAIN 335..450
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|Pfam:PF13718"
FT BINDING 129
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01886"
FT BINDING 282
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01886"
FT BINDING 427..429
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01886"
FT BINDING 467
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01886"
SQ SEQUENCE 634 AA; 70986 MW; F76EE53DD53FE070 CRC64;
MGPLAWCYEQ CMEMISASAL PYFWLGDAPA TITSHLYKQI LGQEISLLVI NAHNAFDANL
FAASEGTLRG GGTLVLLCPT DIDNNDNFYT YISKQLECFP FITIMQGDKL PELNNKAINQ
QPQLHLEQQN NAIKAIIKTV TGHRRRPLVL TANRGRGKSS ALGIAAKQLI ELGYQQILIC
APSKDATNTL FKHAGDSTKI SFIAPDLLLK NKPACDLLMI DEAAAIPVAT LEALSEHYSR
LVFATTLHGY EGSGRGFALR FQKRLKQIAP QMRSLHIDQP IRWGKDDPLE QFTLQHLCLT
ESQTPSPVYD KTQKVHFSVV TATQLLADPG LLTEIFSLLV TAHYQTKPSD LEKLLNDKLL
SILLLTQNKQ VLAVALVNHE GDLDEGLAQQ VYQGSRRLKG HLVAQSLTFH CAQQDAAKHK
YARIQRIATH PALQQQGLGK LFMLKMTDWA TTQQFDHLCA SFGATAELLR FWQMNHFSSL
RIGSSKDKSS GTHSFIVNRP LSIRGKQLHQ AVVQQFHLQL AVQIARQLQQ LDSQLIATLL
NELPKGSYQH PLLVSYCQGN LPYDFVEFHL IAVIINSDLS LLDKKQQTLT IQKTLQNRSW
ADICENNKYT GKKQAQLELR NNITLLTAPY KIEE
//
