ID K0ADX8_EXIAB Unreviewed; 383 AA.
AC K0ADX8;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=tRNA(Met) cytidine acetate ligase {ECO:0000256|HAMAP-Rule:MF_01539};
DE EC=6.3.4.- {ECO:0000256|HAMAP-Rule:MF_01539};
GN Name=tmcAL {ECO:0000256|HAMAP-Rule:MF_01539};
GN OrderedLocusNames=Eab7_1824 {ECO:0000313|EMBL:AFS70932.1};
OS Exiguobacterium antarcticum (strain B7).
OC Bacteria; Bacillota; Bacilli; Bacillales;
OC Bacillales Family XII. Incertae Sedis; Exiguobacterium.
OX NCBI_TaxID=1087448 {ECO:0000313|EMBL:AFS70932.1, ECO:0000313|Proteomes:UP000006274};
RN [1] {ECO:0000313|EMBL:AFS70932.1, ECO:0000313|Proteomes:UP000006274}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B7 {ECO:0000313|Proteomes:UP000006274};
RX PubMed=23144424; DOI=10.1128/JB.01791-12;
RA Carneiro A.R., Ramos R.T., Dall'Agnol H., Pinto A.C., de Castro Soares S.,
RA Santos A.R., Guimaraes L.C., Almeida S.S., Barauna R.A., das Gracas D.A.,
RA Franco L.C., Ali A., Hassan S.S., Nunes C.I., Barbosa M.S., Fiaux K.K.,
RA Aburjaile F.F., Barbosa E.G., Bakhtiar S.M., Vilela D., Nobrega F.,
RA Dos Santos A.L., Carepo M.S., Azevedo V., Schneider M.P., Pellizari V.H.,
RA Silva A.;
RT "Genome sequence of Exiguobacterium antarcticum B7, isolated from a biofilm
RT in Ginger Lake, King George Island, Antarctica.";
RL J. Bacteriol. 194:6689-6690(2012).
CC -!- FUNCTION: Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at
CC the wobble position of elongator tRNA(Met), using acetate and ATP as
CC substrates. First activates an acetate ion to form acetyladenylate (Ac-
CC AMP) and then transfers the acetyl group to tRNA to form ac(4)C34.
CC {ECO:0000256|HAMAP-Rule:MF_01539}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetate + ATP + cytidine(34) in elongator tRNA(Met) = AMP +
CC diphosphate + N(4)-acetylcytidine(34) in elongator tRNA(Met);
CC Xref=Rhea:RHEA:58144, Rhea:RHEA-COMP:10693, Rhea:RHEA-COMP:10694,
CC ChEBI:CHEBI:30089, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:74900, ChEBI:CHEBI:82748, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01539};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01539}.
CC -!- SIMILARITY: Belongs to the TmcAL family. {ECO:0000256|HAMAP-
CC Rule:MF_01539}.
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DR EMBL; CP003063; AFS70932.1; -; Genomic_DNA.
DR RefSeq; WP_014970777.1; NC_018665.1.
DR AlphaFoldDB; K0ADX8; -.
DR STRING; 1087448.Eab7_1824; -.
DR KEGG; ean:Eab7_1824; -.
DR PATRIC; fig|1087448.3.peg.1880; -.
DR eggNOG; COG1323; Bacteria.
DR HOGENOM; CLU_038915_0_2_9; -.
DR Proteomes; UP000006274; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016879; F:ligase activity, forming carbon-nitrogen bonds; IEA:UniProtKB-UniRule.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006400; P:tRNA modification; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR HAMAP; MF_01539; TmcAL; 1.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR008513; tRNA(Met)_cyd_acetate_ligase.
DR PANTHER; PTHR37825; TRNA(MET) CYTIDINE ACETATE LIGASE; 1.
DR PANTHER; PTHR37825:SF1; TRNA(MET) CYTIDINE ACETATE LIGASE; 1.
DR Pfam; PF05636; HIGH_NTase1; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01539};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01539};
KW Ligase {ECO:0000256|HAMAP-Rule:MF_01539};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01539};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01539};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_01539}; tRNA-binding {ECO:0000256|HAMAP-Rule:MF_01539}.
FT BINDING 7..20
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01539"
FT BINDING 102
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01539"
FT BINDING 160
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01539"
FT BINDING 181..182
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01539"
SQ SEQUENCE 383 AA; 42794 MW; 7E407D54B7BECDEE CRC64;
MRMTAIISEY NPFHNGHLYQ AKIARHETGA DLIVAIMSGT FTQRGEPAFT DKWSRAQAAV
ASGEIDLVLE LPFYFAVQRA DRFALGGVTI AETIGAHTLS FGSECGEVTP FITAASENHE
ANPRYKELLQ QRLAQGLSSA TAASQAFQAM TTTLDLTTPN NTLGYYYARA ASSIALHTTK
RIGSGYHDLS VGDVMSATAI RAYYTQHQSL IGLPEATAET LQDAVFASFD TYYPFIRHRL
LTTSLADLTQ FNGMDASLAP RLIDGARRHD SFEGFMSFVK TRRYTRTSLQ RALIYLLTST
MKREIDGLPF DQIDYVRPLA FNEIGRTALR QIKQRVPIIS TFEKHPWLIK ESQVTAAYAV
PLARYQQLEE HRRFAYFSGK ASR
//
