ID A5TW94_FUSNP Unreviewed; 395 AA.
AC A5TW94;
DT 10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 10-JUL-2007, sequence version 1.
DT 24-JAN-2024, entry version 45.
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=FNP_1387 {ECO:0000313|EMBL:EDK89169.1};
OS Fusobacterium polymorphum ATCC 10953.
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae;
OC Fusobacterium.
OX NCBI_TaxID=393480 {ECO:0000313|EMBL:EDK89169.1};
RN [1] {ECO:0000313|EMBL:EDK89169.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10953 {ECO:0000313|EMBL:EDK89169.1};
RA Qin X., Weinstock G.M.;
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDK89169.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10953 {ECO:0000313|EMBL:EDK89169.1};
RA Karpathy S.E., Xiang Q., Gioia J., Jiang H., Liu Y., Petrosino J.F.,
RA Yerrapragada S., Fox G.E., Kinder Haake S., Weinstock G.M.,
RA Highlander S.K.;
RT "Genome sequence of Fusobacterium nucleatum subspecies polymorphum - a
RT genetically tractable Fusobacterium.";
RL Submitted (MAY-2007) 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}.
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DR EMBL; CM000440; EDK89169.1; -; Genomic_DNA.
DR RefSeq; WP_005897867.1; NZ_CM000440.1.
DR AlphaFoldDB; A5TW94; -.
DR GeneID; 45635284; -.
DR eggNOG; COG1323; Bacteria.
DR HOGENOM; CLU_038915_0_0_0; -.
DR Proteomes; UP000001921; 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:0016740; F:transferase activity; IEA:UniProtKB-KW.
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 Transferase {ECO:0000313|EMBL:EDK89169.1};
KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_01539};
KW tRNA-binding {ECO:0000256|HAMAP-Rule:MF_01539}.
FT BINDING 9..22
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01539"
FT BINDING 103
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01539"
FT BINDING 154
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01539"
FT BINDING 179
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01539"
SQ SEQUENCE 395 AA; 45919 MW; C75029C9188BFC1E CRC64;
MFKNVIGLIV EYNPFHNGHL HHIQEIDRLF EDNIKIAVMS GDFVQRGEPS LINKFEKIKI
ALSQGIDIVI ELPAFYSTQS AEIFAKGSVN LLNKLSCSHI VFGSESNDLD KLKRIATISL
TKEFELSLRE FLAEGFSYPT AFSKALFDEK LGSNDILAME YLKAIKVINP KIEACSIKRE
KTGYYDDEKD NFSSATYIRK ILLDCNEKKE DKLNKIKNLV PEFSYKILEE NFGVFSCLSD
FYDLIKYNII KNYSELKNIQ DLEVGLENRL YKYSLENLSF EDFFDEVLTK RITISRLQRI
LLHSLFGLTK TITEKIKNKV PFVKILGFSE RGQEYLNYLK KAENYNERKI LTSNRNLKEI
LNEEEIELFN FNELCSQIYC IKSSYINIGY PIIKK
//
