ID FMT_PROMS Reviewed; 328 AA. AC A2BRA1; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 20-FEB-2007, sequence version 1. DT 03-AUG-2022, entry version 81. 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=A9601_10281; OS Prochlorococcus marinus (strain AS9601). OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae; OC Prochlorococcus. OX NCBI_TaxID=146891; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AS9601; RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231; RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S., RA Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M., RA Richardson P., Chisholm S.W.; RT "Patterns and implications of gene gain and loss in the evolution of RT Prochlorococcus."; RL PLoS Genet. 3:2515-2528(2007). 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000551; ABM70312.1; -; Genomic_DNA. DR RefSeq; WP_011818464.1; NC_008816.1. DR AlphaFoldDB; A2BRA1; -. DR SMR; A2BRA1; -. DR STRING; 146891.A9601_10281; -. DR EnsemblBacteria; ABM70312; ABM70312; A9601_10281. DR KEGG; pmb:A9601_10281; -. DR eggNOG; COG0223; Bacteria. DR HOGENOM; CLU_033347_1_1_3; -. DR OMA; CCPVVAY; -. DR OrthoDB; 2009156at2; -. DR Proteomes; UP000002590; 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; Transferase. FT CHAIN 1..328 FT /note="Methionyl-tRNA formyltransferase" FT /id="PRO_1000020126" 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 328 AA; 37090 MW; 4AA5388674349BEB CRC64; MRIIFWGTPE YSIASLDIFI KSKHEVIGVV SQPDKKRSRG NKLISSPVKS FAEQESIKIY TPVKIRDNIH FINELKSLSC DLFIVIAYGK ILPKEILEIP KFGCWNAHAS LLPRWRGAAP IQWSLIKGDK FTGVGIMKMN EGLDTGDLLL EEKIKIGNED NLNTLSEKLS ILSAKLFLKA ASLLEENFYK NTKSQLTKQN SLGREITYAR MIEKSDFRVD WGNQAIAISQ KIKGLYPRAN TIFRGKNLKI LKIKVLSSDE IKNEKYLFMS DYSRPGIILA VIEDEGIIIS TKTDPIILLE AKLEGKNISS KKQLIQQLKP SVGEYLSD //