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Database: UniProt
Entry: W0HR63_9GAMM
LinkDB: W0HR63_9GAMM
Original site: W0HR63_9GAMM 
ID   W0HR63_9GAMM            Unreviewed;       736 AA.
AC   W0HR63;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 44.
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   ECO:0000313|EMBL:AHF76284.1};
GN   ORFNames=Sant_1215 {ECO:0000313|EMBL:AHF76284.1};
OS   Sodalis praecaptivus.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Bruguierivoracaceae; Sodalis.
OX   NCBI_TaxID=1239307 {ECO:0000313|EMBL:AHF76284.1, ECO:0000313|Proteomes:UP000019028};
RN   [1] {ECO:0000313|EMBL:AHF76284.1, ECO:0000313|Proteomes:UP000019028}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HS1 {ECO:0000313|EMBL:AHF76284.1,
RC   ECO:0000313|Proteomes:UP000019028};
RX   PubMed=24407854; DOI=10.1093/gbe/evt210;
RA   Oakeson K.F., Gil R., Clayton A.L., Dunn D.M., von Niederhausern A.C.,
RA   Hamil C., Aoyagi A., Duval B., Baca A., Silva F.J., Vallier A.,
RA   Jackson D.G., Latorre A., Weiss R.B., Heddi A., Moya A., Dale C.;
RT   "Genome degeneration and adaptation in a nascent stage of symbiosis.";
RL   Genome Biol. Evol. 6:76-93(2014).
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; CP006569; AHF76284.1; -; Genomic_DNA.
DR   AlphaFoldDB; W0HR63; -.
DR   KEGG; sod:Sant_1215; -.
DR   PATRIC; fig|1239307.3.peg.1301; -.
DR   HOGENOM; CLU_004652_1_1_6; -.
DR   Proteomes; UP000019028; 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; IPR033442; TmcA_tRNA_bind.
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   Pfam; PF17176; tRNA_bind_3; 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:UP000019028};
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          432..609
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51186"
FT   BINDING         186
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01886"
FT   BINDING         328
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01886"
FT   BINDING         537..539
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01886"
FT   BINDING         584
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01886"
SQ   SEQUENCE   736 AA;  81033 MW;  C4C185D7085B98BB CRC64;
     MTASRPSWLA SVHHETAAMR RAGVRRLLVI SGEPGWCSWQ AATLCDALAG DWLWVGEQSE
     RGVGCRPAAL KTLLGREFLH AVFDARQALS VDALAALAGT LVAGSWLVLL VPPWSRWPRV
     PDGDSLRWSE QPQPIATPCF TRYFRASLLA DPAVALLRQN RAPQLTPLPS RPPWQAPVPG
     RPTADQRRLL RRLTQAEPGI YIMIAPRGRG KSALAGMFAH KLADACCITA PAKAAVDVLR
     RYAGPDAPFF APDALLARCR EGARARWLLV DEAAALPLPL LRQLMGYFSH VLLTTTVAGY
     EGTGRGFLLK FCDGLPRWHP LVLDAPLRWS INDPLERWLT QTLLLEDADA QIIAAEPAPP
     DADRVAARVA PQDSAMGSTP PAVAVASAPS SAPGFTSAVR TGSRAVSGEN PSARGIMDDR
     CAARWRIDRV GALTWRRQPA ARQAFYRLLT RAHYRTSPID LRRLMDAPGM SFFTAHQHGD
     MMGGLWLVEE GGLTPRLAHA VWAGYRRPPG SLVAQSLAAH GNLWRAPRLR SRRISRIAVA
     PAARRHGMGL AMIDQAARQA ARDERDFLSV SFGYTAALWH FWRRAGFQLV RMGTHREASS
     GLYSAMALLP LSDAGRELTR RAAEGFERDG RLAAGEQQPL ALEDWRCLAG FAFAQRPPEA
     CRSALIRLIR HSTLPLPALR LWLTQPLPDE ALAAHLALSG KKALWRRWRQ ETAAAMTAVD
     ARLTRRWRCF SQQPTR
//
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