TMCA_NITHN
ID TMCA_NITHN Reviewed; 746 AA.
AC D5C1K8;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 1.
DT 03-AUG-2022, entry version 63.
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=Nhal_1498;
OS Nitrosococcus halophilus (strain Nc4).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Nitrosococcus.
OX NCBI_TaxID=472759;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nc4;
RG US DOE Joint Genome Institute;
RA Campbell M.A., Malfatti S.A., Chain P.S.G., Heidelberg J.F., Ward B.B.,
RA Klotz M.G.;
RT "Complete genome sequence of Nitrosococcus halophilus Nc4, a salt-adapted,
RT aerobic obligate ammonia-oxidizing sulfur purple bacterium.";
RL Submitted (APR-2010) 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: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; CP001798; ADE14641.1; -; Genomic_DNA.
DR RefSeq; WP_013032530.1; NC_013960.1.
DR AlphaFoldDB; D5C1K8; -.
DR SMR; D5C1K8; -.
DR STRING; 472759.Nhal_1498; -.
DR EnsemblBacteria; ADE14641; ADE14641; Nhal_1498.
DR KEGG; nhl:Nhal_1498; -.
DR eggNOG; COG1444; Bacteria.
DR HOGENOM; CLU_004652_1_0_6; -.
DR OMA; NEPDDLG; -.
DR OrthoDB; 1019071at2; -.
DR Proteomes; UP000001844; 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; 1.20.120.890; -; 1.
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; IPR038321; TmcA_C_sf.
DR InterPro; IPR013562; TmcA_N.
DR InterPro; IPR033442; TmcA_tRNA_bind.
DR InterPro; IPR024914; tRNA_acetyltr_TmcA.
DR PANTHER; PTHR10925; PTHR10925; 2.
DR Pfam; PF08351; DUF1726; 1.
DR Pfam; PF13718; GNAT_acetyltr_2; 2.
DR Pfam; PF05127; Helicase_RecD; 1.
DR Pfam; PF17176; tRNA_bind_3; 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;
KW Reference proteome; RNA-binding; Transferase; tRNA processing;
KW tRNA-binding.
FT CHAIN 1..746
FT /note="tRNA(Met) cytidine acetyltransferase TmcA"
FT /id="PRO_0000403122"
FT DOMAIN 405..617
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
FT REGION 181..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 202
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
FT BINDING 228..237
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
FT BINDING 370
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
FT BINDING 517..519
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
FT BINDING 524..530
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
FT BINDING 557
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
FT BINDING 564
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01886"
SQ SEQUENCE 746 AA; 81439 MW; 7B7B5AC1B2E0A9D8 CRC64;
MHPILFPPTL DNIRKITASL VAAAKASGHR RALVLSGDRE WCLQAAQVSL ASTSLEPVLW
IAAQAPENAW RMEAAKAHRS LGQEVDAIVF DAYSGFDLDA FGIITGAIRG GGLLLLLTPP
LAAWPSFNDP EHARIVTAPY EVTEVTGRFL KRLVRILREA EGVIIIEQGK ILPSVPFAAP
ARAETGGNPP SPGDSACRTE DQGRAVEAIV KVVTGQRRRP VVLTSDRGRG KSAALGIAAA
RLLQRGLKHI IVTGPRLDAV EPVFRHAQRL LPQATVSRAA LHLPEAGMEF APPDDLIRTS
RPADLLLVDE AATIPTPLLE RLLQGYSRIA FATTIHGYEG TGRGFALRFH RVLDEKTRGW
KGLRLETPIR WRSGDPLEHF VFRALLLDAT AAPDSAVASA RPETVAVERL DRDALVRDEA
TLSELFGLLV LAHYQTRPYD LRHLLDGPNL SVYVMRYRGH VVATALLAAE GGFVEETARG
IWEGRTRPHG HLLPESLAAH LGLAQAPRLH CARIMRIAVH PAVQGQGLGT HLVDTIIRET
GGEGLDYLGS SFGATVELLR FWERLDFLPV RLSVKRGATS GAHSAIVLHP LSSSGQALVK
RARERFLVHL PHQLADPLRE LEPQLAAWLL RRGDPAGPLP LDSQDWSDVL AFAFGRRVYE
VCIGPIWKLT WGALAAPESA TLLGEVERNA LIVKVLQKRS WQEAAAALEL SGRAQVIEVL
RRTLRPLVLH FGNEAVRREA ERLAGG
