FMT_RUMCH
ID FMT_RUMCH Reviewed; 312 AA.
AC B8I255;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Methionyl-tRNA formyltransferase {ECO:0000255|HAMAP-Rule:MF_00182};
DE EC=2.1.2.9 {ECO:0000255|HAMAP-Rule:MF_00182};
GN Name=fmt {ECO:0000255|HAMAP-Rule:MF_00182}; OrderedLocusNames=Ccel_1529;
OS Ruminiclostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 /
OS H10) (Clostridium cellulolyticum).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Oscillospiraceae;
OC Ruminiclostridium.
OX NCBI_TaxID=394503;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35319 / DSM 5812 / JCM 6584 / H10;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Saunders E., Brettin T.,
RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Ivanova N., Zhou J., Richardson P.;
RT "Complete sequence of Clostridium cellulolyticum H10.";
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Attaches a formyl group to the free amino group of methionyl-
CC tRNA(fMet). The formyl group appears to play a dual role in the
CC initiator identity of N-formylmethionyl-tRNA by promoting its
CC recognition by IF2 and preventing the misappropriation of this tRNA by
CC the elongation apparatus. {ECO:0000255|HAMAP-Rule:MF_00182}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) =
CC (6S)-5,6,7,8-tetrahydrofolate + H(+) + N-formyl-L-methionyl-
CC tRNA(fMet); Xref=Rhea:RHEA:24380, Rhea:RHEA-COMP:9952, Rhea:RHEA-
CC COMP:9953, ChEBI:CHEBI:15378, ChEBI:CHEBI:57453, ChEBI:CHEBI:57454,
CC ChEBI:CHEBI:78530, ChEBI:CHEBI:78844; EC=2.1.2.9;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00182};
CC -!- SIMILARITY: Belongs to the Fmt family. {ECO:0000255|HAMAP-
CC Rule:MF_00182}.
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DR EMBL; CP001348; ACL75881.1; -; Genomic_DNA.
DR RefSeq; WP_015925022.1; NC_011898.1.
DR AlphaFoldDB; B8I255; -.
DR SMR; B8I255; -.
DR STRING; 394503.Ccel_1529; -.
DR EnsemblBacteria; ACL75881; ACL75881; Ccel_1529.
DR KEGG; cce:Ccel_1529; -.
DR eggNOG; COG0223; Bacteria.
DR HOGENOM; CLU_033347_1_1_9; -.
DR OMA; CCPVVAY; -.
DR OrthoDB; 2009156at2; -.
DR Proteomes; UP000001349; Chromosome.
DR GO; GO:0004479; F:methionyl-tRNA formyltransferase activity; IEA:UniProtKB-UniRule.
DR CDD; cd08646; FMT_core_Met-tRNA-FMT_N; 1.
DR CDD; cd08704; Met_tRNA_FMT_C; 1.
DR HAMAP; MF_00182; Formyl_trans; 1.
DR InterPro; IPR005794; Fmt.
DR InterPro; IPR005793; Formyl_trans_C.
DR InterPro; IPR002376; Formyl_transf_N.
DR InterPro; IPR036477; Formyl_transf_N_sf.
DR InterPro; IPR011034; Formyl_transferase-like_C_sf.
DR InterPro; IPR001555; GART_AS.
DR InterPro; IPR044135; Met-tRNA-FMT_C.
DR InterPro; IPR041711; Met-tRNA-FMT_N.
DR Pfam; PF02911; Formyl_trans_C; 1.
DR Pfam; PF00551; Formyl_trans_N; 1.
DR SUPFAM; SSF50486; SSF50486; 1.
DR SUPFAM; SSF53328; SSF53328; 1.
DR TIGRFAMs; TIGR00460; fmt; 1.
DR PROSITE; PS00373; GART; 1.
PE 3: Inferred from homology;
KW Protein biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..312
FT /note="Methionyl-tRNA formyltransferase"
FT /id="PRO_1000190017"
FT BINDING 109..112
FT /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57453"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00182"
SQ SEQUENCE 312 AA; 34438 MW; BD3E49F5EE7C5C6A CRC64;
MKIIFMGTPE FAVPSLEMLI NEGYNVIAVV TQPDKPKGRG KKLAAPPVKE FALEHGIKVL
QPAKIKTPEF VEQIRELGPD LLITAAYGKI ISKDMLDVPP LGCINVHGSL LPAYRGAAPI
HWSIINGEKV TGITTMFTDV GLDTGDMLLK RELEISSDMT AGELHDEMAI LGAEVLKDTL
IHLKNGTLVR SPQDDALSSY APIITKEVGL IDWNKTVQQV HNLVRGTNPW PGAFTFINES
KMRVWKTCIV DFGNSQEHCP GEIVSVDDKG ILVKCCDGYI MIKELQFDSS KRMKVRDYIR
GNKIDTGEKL GK
