ID F0QVB1_VULM7 Unreviewed; 799 AA.
AC F0QVB1;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 69.
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=VMUT_1812 {ECO:0000313|EMBL:ADY02013.1};
OS Vulcanisaeta moutnovskia (strain 768-28).
OC Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Vulcanisaeta.
OX NCBI_TaxID=985053 {ECO:0000313|EMBL:ADY02013.1, ECO:0000313|Proteomes:UP000007485};
RN [1] {ECO:0000313|EMBL:ADY02013.1, ECO:0000313|Proteomes:UP000007485}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=768-28 {ECO:0000313|EMBL:ADY02013.1,
RC ECO:0000313|Proteomes:UP000007485};
RX PubMed=21398550; DOI=10.1128/JB.00237-11;
RA Gumerov V.M., Mardanov A.V., Beletsky A.V., Prokofeva M.I.,
RA Bonch-Osmolovskaya E.A., Ravin N.V., Skryabin K.G.;
RT "Complete genome sequence of 'Vulcanisaeta moutnovskia' strain 768-28, a
RT novel member of the hyperthermophilic crenarchaeal genus vulcanisaeta.";
RL J. Bacteriol. 193:2355-2356(2011).
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; CP002529; ADY02013.1; -; Genomic_DNA.
DR RefSeq; WP_013605175.1; NC_015151.1.
DR AlphaFoldDB; F0QVB1; -.
DR STRING; 985053.VMUT_1812; -.
DR GeneID; 10289464; -.
DR KEGG; vmo:VMUT_1812; -.
DR eggNOG; arCOG01951; Archaea.
DR HOGENOM; CLU_004652_1_0_2; -.
DR OrthoDB; 312894at2157; -.
DR Proteomes; UP000007485; 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 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; 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};
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 455..635
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
FT BINDING 224
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01886"
FT BINDING 410
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01886"
FT BINDING 560..562
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01886"
SQ SEQUENCE 799 AA; 92171 MW; E647284A724035F5 CRC64;
MGWIELLQGL VREGLSSNHR RLIVLVGTNE EKIAKYAAES LRVFSSLVKD PHGLYMYQPE
YSDAQRRMGK LKDLIEGIPI NIDYRPYKDT DKLLGITVDF AVLDLMNDLK PNDVGRLGGI
VRGGGIYVFM VPPLNDWIKQ LTKFQQSLLV PQYGPEHVRH FLKVRFWNKL MSMDKALIID
TDNNKLIKEP VLGDSQPWRP REIVMPERMK FTRTIYELAK TQDQVETLRA MEVLMERPPR
GKKVNVVLIA DRGRGKSAVI GLALAALAHR LRKIKGRVRF AVTAMNPSNV STLMEFVIKG
LKALNYDVST SYWGNDVVSV KVGISVFIDY IRPYDMLSED DRDIVVVDEA AMIPLPVLYG
IHERFSRVIY ASTIHGYEGA GRGFSLRFLK YLREDKNTRI IEYELKEPIR YAPNDPVEQW
LFDTLLLDAE PARITDEDQE LINRHEFNYL IPDLKEFFLL NEEQLRQFFG IYVQAHYRNE
PDDLGMMMDA PHHFIRALSL SNGKIVVSVE LAEEGGIGDD MIDMVVRGLK LPGNIIPDRL
IKYWGLTDFA KLKGWRIIRI ATHPELQDKG LGTEMLKRIE EEARERGIDW VGVGFGVNAK
LLNFWIKNGY MPVHISPERN PISGEYSVLL VKPINEKTRD IIIYANKEFR LRLLNSLQGP
FHDMEPDVVR MLLTDWGQAL DPGYTPRLTE AQTRRLVAYS WGPMTYENTA DAITELVKTY
YLRRGVDSIN LPQFYEEALI CKVLQARPWR ESAKVLSIRK STLMLMLREV IKLLIQYYVK
YVEIPEFMIS VTKLQKRSK
//
