ID E7MM05_9FIRM Unreviewed; 373 AA.
AC E7MM05;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=HMPREF9430_00568 {ECO:0000313|EMBL:EFW24846.1};
OS Solobacterium moorei F0204.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae; Solobacterium.
OX NCBI_TaxID=706433 {ECO:0000313|EMBL:EFW24846.1, ECO:0000313|Proteomes:UP000004097};
RN [1] {ECO:0000313|EMBL:EFW24846.1, ECO:0000313|Proteomes:UP000004097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0204 {ECO:0000313|EMBL:EFW24846.1,
RC ECO:0000313|Proteomes:UP000004097};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (AUG-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 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:EFW24846.1}.
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DR EMBL; AECQ01000008; EFW24846.1; -; Genomic_DNA.
DR RefSeq; WP_006525408.1; NZ_GL637649.1.
DR AlphaFoldDB; E7MM05; -.
DR STRING; 706433.HMPREF9430_00568; -.
DR eggNOG; COG1323; Bacteria.
DR HOGENOM; CLU_038915_0_2_9; -.
DR OrthoDB; 9769796at2; -.
DR Proteomes; UP000004097; 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 Reference proteome {ECO:0000313|Proteomes:UP000004097};
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 147
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01539"
FT BINDING 170
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01539"
SQ SEQUENCE 373 AA; 42763 MW; 38FADC643667AEAA CRC64;
MKVCGIIAEY NPFHNGHRYQ IEQARKQSGC DMVIAVMSGN FVQRGEPAII DKWKRAKVAI
ENGVDLVIEL PYFYATQSAS KFAYGAVELL KIAKVDYISF GSECANLENL QEIADTSLNP
DNLRESMQTG MSFPRAYSLL TGSMEPNDIL AVSYLKYLKG SNIQPVIVQR TSSYLNPEIS
ENASALAIRK ALKNNERLAS STPMEEILKE STLVYPEQFY PYLRTYLLTS SRKQLENLFL
FNEGIENHLR KCAADNDTYE GFLQDATTYR YTSNRIRRSI LQAMVQLTKY EAQRLPALDH
LRILAFNDTG KKWLHDMRKE DMRICSKFAD VPFPWRTLEY RSTLLYTSVL PSEERKHLLK
LEISGAHYIS SEH
//
