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Database: UniProt
Entry: E1V9Z1_HALED
LinkDB: E1V9Z1_HALED
Original site: E1V9Z1_HALED 
ID   E1V9Z1_HALED            Unreviewed;       724 AA.
AC   E1V9Z1;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   24-JAN-2024, entry version 68.
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:CBV43879.1};
GN   OrderedLocusNames=HELO_3995 {ECO:0000313|EMBL:CBV43879.1};
OS   Halomonas elongata (strain ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198
OS   / 1H9).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=768066 {ECO:0000313|EMBL:CBV43879.1, ECO:0000313|Proteomes:UP000008707};
RN   [1] {ECO:0000313|Proteomes:UP000008707}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198 / 1H9
RC   {ECO:0000313|Proteomes:UP000008707};
RX   PubMed=20849449; DOI=10.1111/j.1462-2920.2010.02336.x;
RA   Schwibbert K., Marin-Sanguino A., Bagyan I., Heidrich G., Lentzen G.,
RA   Seitz H., Rampp M., Schuster S.C., Klenk H.P., Pfeiffer F., Oesterhelt D.,
RA   Kunte H.J.;
RT   "A blueprint of ectoine metabolism from the genome of the industrial
RT   producer Halomonas elongata DSM 2581(T).";
RL   Environ. Microbiol. 13:1973-1994(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; FN869568; CBV43879.1; -; Genomic_DNA.
DR   AlphaFoldDB; E1V9Z1; -.
DR   STRING; 768066.HELO_3995; -.
DR   KEGG; hel:HELO_3995; -.
DR   eggNOG; COG1444; Bacteria.
DR   HOGENOM; CLU_004652_1_0_6; -.
DR   OMA; IMRIAVH; -.
DR   OrthoDB; 5578851at2; -.
DR   Proteomes; UP000008707; 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; 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.
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          442..584
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51186"
FT   BINDING         197
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01886"
FT   BINDING         368
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01886"
FT   BINDING         509..511
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01886"
SQ   SEQUENCE   724 AA;  78422 MW;  FE3A19097D9AE89D CRC64;
     MPPVNTASAP PELETFHREL ISRRWRGLLW LSGDAERCRD RAREVWASEA WRAALWVGPA
     APEGIESTAW LPANKARTRL GGEQDLVVFD AVSPEAGFDP EAFGALSGTL RAGGLMVLMT
     PADWGARPDA DYARLAEHPW SPENLSSRYL ARLSSLLSNA PEVAPWPAGA APVIPVLASA
     PRQAAAPSDP ACLTPDQADA VARLVRLRRR RPLVITADRG RGKTAALGIA CARLLARGID
     EILVTAPRPS AVAGLFERLA VLCPEGVRRG NRFEVEGGCV SFLAPDELQS RIERGEAGGA
     GRWLLVDEAA AIPAGLLGGW LEAFPRIAFA TTVHGYEGAG RGFALRFRER LTRFAPDWRE
     IHLATPVRWT EGDPLEALTS RLLMLDAEPD SGQPGTVSRQ REDRRALAVD EPRLRAIFGL
     LVQAHYRTTP GDLRRLLDAP ATRIASLSGD AGVAAVAVTS DEGGFDAELA ERVARGERRP
     RGHLLAQSLA AHAGEREALT ARLRRILRIA VVPQCRRQGL GARLLAAEQT DAEAEGIDLL
     GASFGAEPGL LAFWQAQGFR VVRLGLTRET STGEHALMMV RPLSGTGEAL VARLIRRFHR
     QLPSLLAFEL SELEPLVALV LLGERPAESL SPEDRRDLDD VAHGHRDPAM ARPAMQALIA
     AVAPHGQGDA ELAMLAAWAF QGRADDWLAR RLSLSGARQV DAWRRRSVAR WLEAANLSKN
     EDGR
//
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