ID B6W7R2_9FIRM Unreviewed; 398 AA.
AC B6W7R2;
DT 20-JAN-2009, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2009, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=ANHYDRO_00611 {ECO:0000313|EMBL:EEB36311.1};
OS Anaerococcus hydrogenalis DSM 7454.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Anaerococcus.
OX NCBI_TaxID=561177 {ECO:0000313|EMBL:EEB36311.1, ECO:0000313|Proteomes:UP000005451};
RN [1] {ECO:0000313|EMBL:EEB36311.1, ECO:0000313|Proteomes:UP000005451}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7454 {ECO:0000313|EMBL:EEB36311.1,
RC ECO:0000313|Proteomes:UP000005451};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EEB36311.1, ECO:0000313|Proteomes:UP000005451}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7454 {ECO:0000313|EMBL:EEB36311.1,
RC ECO:0000313|Proteomes:UP000005451};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Anaerococcus hydrogenalis (DSM 7454).";
RL Submitted (OCT-2008) 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: 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:EEB36311.1}.
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DR EMBL; ABXA01000019; EEB36311.1; -; Genomic_DNA.
DR AlphaFoldDB; B6W7R2; -.
DR STRING; 561177.ANHYDRO_00611; -.
DR eggNOG; COG1323; Bacteria.
DR Proteomes; UP000005451; 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 13..26
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01539"
FT BINDING 106
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01539"
FT BINDING 164
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01539"
FT BINDING 189..190
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01539"
SQ SEQUENCE 398 AA; 46539 MW; AFA91A5A3F76854B CRC64;
MFLGDFMKKL AIISEYNPFH NGHNFIQKKA RELTNADLII SIMSGDFVQR GEPSLIDKYK
RADSAMISAD LIIEMPSFIS LQSANLFARK NIEILDKLKI DYLAFGIENI SEEDFFKSVE
NILNNNENID KKTKYFLDKG LSFSKASYEA SKTYALNQKF FSANNILALE YVRALKNSNS
KIKAIPIKRI KSMNKDKNLD KKTFASSTAI RNNINNSNIK SYLPKSSLEN IEKFKHQYNN
FPDMERLYEL FRYKILIEDI NMSNILCYEE GMDNYLKKLA EKNFLYNDFI NEASSLRFTK
SRIKRLMINY LLENTIDFNN LEINFIKVLA FNKKSTRFFK DQAVSILIQK KDEKKLKDNE
KIIYDQMIKA SNLYSFLINR NMNSDFTQKI TIKKSSNK
//
