ID A0A0M2PMQ1_9BACI Unreviewed; 402 AA.
AC A0A0M2PMQ1;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
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 ORFNames=WQ54_01485 {ECO:0000313|EMBL:KKI93754.1};
OS Bacillus sp. SA1-12.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1455638 {ECO:0000313|EMBL:KKI93754.1, ECO:0000313|Proteomes:UP000034887};
RN [1] {ECO:0000313|EMBL:KKI93754.1, ECO:0000313|Proteomes:UP000034887}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA1-12 {ECO:0000313|EMBL:KKI93754.1,
RC ECO:0000313|Proteomes:UP000034887};
RA Kumar A., Mathan Kumar R., Kaur N., Kumar N., Singh N.K., Kaur G.,
RA Mayilraj S.;
RT "Taxonomic description and genome sequence of Bacillus tuticoriensis sp.
RT nov., a novel member of the genus Bacillus isolated from solar saltern.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01539}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKI93754.1}.
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DR EMBL; LATZ01000002; KKI93754.1; -; Genomic_DNA.
DR RefSeq; WP_046511075.1; NZ_LATZ01000002.1.
DR AlphaFoldDB; A0A0M2PMQ1; -.
DR PATRIC; fig|1455638.3.peg.315; -.
DR OrthoDB; 9769796at2; -.
DR Proteomes; UP000034887; Unassembled WGS sequence.
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 101
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01539"
FT BINDING 162
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01539"
FT BINDING 187
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01539"
SQ SEQUENCE 402 AA; 46069 MW; 7099B77AF3C33A51 CRC64;
MNALGLVVEY NPFHNGHYYH LTQSIKETNA DIVIAVMSGN FLQRGEPAII SKWERTKMAL
HSGIDIVIEL PYAFATQKAE TFASGAVSIL GALKCHSLCF GSESGDIFPF LEANEFLLQN
KEQYDLLIQK YMKTGVSYPS ALTRAFQEIS NGRDILDLSL PNNILGFHYV KAIYRQNAKI
KPYTIKRTAA GYHEQNFVSP SIASATSIRK ALFENKGPIT NYVPNETLQI MDQYKNQYGL
LHNWEHYFDY LKYSIMTMSS EELLTIYEAE EGLENRIKRI VPSSESFLHF MEQLKTKRYT
WTRLQRLCTH ILTRTTKQQI SFINKDQTAP YIRLLGMSKK GQEYLSSVKK QTELPIISKL
STIQHPLLEI DIKASSAYNI IFPEPLRSKH LKAEYATPPI RL
//
