FMT_SYNS9
ID FMT_SYNS9 Reviewed; 338 AA.
AC Q3AXQ4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
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};
GN OrderedLocusNames=Syncc9902_1168;
OS Synechococcus sp. (strain CC9902).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=316279;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC9902;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Martinez M., Schmutz J., Larimer F.,
RA Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Synechococcus sp. CC9902.";
RL Submitted (AUG-2005) 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; CP000097; ABB26132.1; -; Genomic_DNA.
DR RefSeq; WP_011359959.1; NC_007513.1.
DR AlphaFoldDB; Q3AXQ4; -.
DR SMR; Q3AXQ4; -.
DR STRING; 316279.Syncc9902_1168; -.
DR EnsemblBacteria; ABB26132; ABB26132; Syncc9902_1168.
DR KEGG; sye:Syncc9902_1168; -.
DR eggNOG; COG0223; Bacteria.
DR HOGENOM; CLU_033347_1_1_3; -.
DR OMA; CCPVVAY; -.
DR OrthoDB; 2009156at2; -.
DR Proteomes; UP000002712; 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; 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.
PE 3: Inferred from homology;
KW Protein biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..338
FT /note="Methionyl-tRNA formyltransferase"
FT /id="PRO_1000020193"
FT BINDING 110..113
FT /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57453"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00182"
SQ SEQUENCE 338 AA; 37142 MW; ED292FA43CAA9694 CRC64;
MKILYWGTPE YAVPTLLALH AAGHEIVGVV TQPDRRRGRG KQLMPSAIKV CAQSLGLAVF
TPERIKTDVG CQKELADLNA DVSVVVAFGQ ILPKSVLEQP PLGCWNGHGS LLPRWRGAGP
IQWALLEGDS ETGVGIMAME EGLDTGPVLL EQRLPISLDQ NSHDLGEKLS QLTATLMVEA
VDLILKAGVG TEPERLERLN VRYQGQEMSY ARMLKKEDFQ IKWGDPALRT HRRVMGLYPS
AMTGWRNKRL KVLETEPLIE RLSDEISEEA RALLGRWRTG EDHPGTVLGC INNVGIVVST
SGCPILIREA QLEGKGRCRA QGLVQQLAAS VGDRFQSF
