TMCA_PYRAB
ID TMCA_PYRAB Reviewed; 817 AA.
AC Q9UZ78; G8ZH77;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=tRNA(Met) cytidine acetyltransferase TmcA {ECO:0000255|HAMAP-Rule:MF_01886};
DE EC=2.3.1.193 {ECO:0000255|HAMAP-Rule:MF_01886};
GN Name=tmcA {ECO:0000255|HAMAP-Rule:MF_01886}; OrderedLocusNames=PYRAB12760;
GN ORFNames=PAB2428;
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(2012).
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:0000255|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:0000255|HAMAP-Rule:MF_01886};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01886}.
CC -!- SIMILARITY: Belongs to the RNA cytidine acetyltransferase family. TmcA
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01886}.
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DR EMBL; AJ248287; CAB50181.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE70714.1; -; Genomic_DNA.
DR PIR; H75035; H75035.
DR RefSeq; WP_010868389.1; NC_000868.1.
DR AlphaFoldDB; Q9UZ78; -.
DR SMR; Q9UZ78; -.
DR STRING; 272844.PAB2428; -.
DR EnsemblBacteria; CAB50181; CAB50181; PAB2428.
DR GeneID; 1496660; -.
DR KEGG; pab:PAB2428; -.
DR PATRIC; fig|272844.11.peg.1357; -.
DR eggNOG; arCOG01951; Archaea.
DR HOGENOM; CLU_004652_1_0_2; -.
DR OMA; NEPDDLG; -.
DR OrthoDB; 2707at2157; -.
DR PhylomeDB; Q9UZ78; -.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; 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; 3.40.50.300; -; 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; PTHR10925; 2.
DR Pfam; PF08351; DUF1726; 1.
DR Pfam; PF13718; GNAT_acetyltr_2; 1.
DR Pfam; PF05127; Helicase_RecD; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 3: Inferred from homology;
KW Acyltransferase; ATP-binding; Cytoplasm; Nucleotide-binding; RNA-binding;
KW Transferase; tRNA processing; tRNA-binding.
FT CHAIN 1..817
FT /note="tRNA(Met) cytidine acetyltransferase TmcA"
FT /id="PRO_0000403132"
FT DOMAIN 469..664
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
FT BINDING 265
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
FT BINDING 289..298
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
FT BINDING 439
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
FT BINDING 589..591
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
FT BINDING 596..602
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
FT BINDING 629
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
FT BINDING 636
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
SQ SEQUENCE 817 AA; 94668 MW; F058E4DE3F9BB9F7 CRC64;
MTIKIRFPKD VREYARKEKV KESIIKLTET SLAEAITNFH RRMIILQGDT LEKAKLAGIL
AGGVARILSE YIPEFLDRKL RDEDKIEVLY ATDALGEDTY GRKRFEEFRK HFSVLAPNAE
LTSVTFKYSR DILGRTFDIL VLDLSYDYSP NDLGRIIETV RGGGLIFILT NPFEKWKDMW
TGFHKSLVTP PYTIDDVKKR FNRRLIRKFT EHKGIYIVDA DKKKIERRPR KNKSQAKLPE
REKVEIPRDI KFPRELYELC LTRGQVEVLK ALEDLIENPG MVVLTADRGR GKSVSVGIAS
IGLAITSKKK NFRIVVTAPE LENVQSLLKF AERSLKVLGY KTKTVKESGL IKEVYAKGIG
IRYYPPTKGY RQKADLYIVD EAAGIHVPIL HRYLEKERVV FSSTIHGYEG AGRGFSVKFL
KKAKEKREYK EIHLSVPIRY AEGDPIERWL FDVLLLDAEP VELTEEDYEL IRKMEVYLEE
PDLDDWFEND REDLRHFVGI YVLAHYRNRP SDVALLADAP HHEARVLRLK NGKIVTAIQI
AKEGGIPKAV IDKMAKGYKP PGNIIPDMMV KHHYAKEFAK LRGYRIVRIA THPDAMDLGL
GSKALELLVK EAQEKGLDWV GSGFGASEEL IRFWVRNGFA VVHLSPTRNP VSGEYTAIVI
KPISERAKEI VKKANDEFRL RLTEWLGDTH RDLEPEIARW LFETPFGEAV NYPIHLTKVQ
RKRLEMFIKR VLTYDTVVDA VKPLVKLYFL DGWMRPYLDD RQIALLIHRV LQAHDWKETA
KLLNRTELYT MIELRDIVRG LWYYYKHMLK DEEKDIS
