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 29-MAY-2013, entry version 42. DE RecName: Full=Methionyl-tRNA formyltransferase; DE EC=2.1.2.9; GN Name=fmt; OrderedLocusNames=A9601_10281; OS Prochlorococcus marinus (strain AS9601). OC Bacteria; Cyanobacteria; Prochlorales; 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., RA Rodrigue S., Chen F., Lapidus A., Ferriera S., Johnson J., RA Steglich C., Church G.M., 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: Modifies the free amino group of the aminoacyl moiety of CC methionyl-tRNA(fMet). The formyl group appears to play a dual role CC in the initiator identity of N-formylmethionyl-tRNA by: (I) CC promoting its recognition by IF2 and (II) impairing its binding to CC EFTu-GTP (By similarity). CC -!- CATALYTIC ACTIVITY: 10-formyltetrahydrofolate + L-methionyl- CC tRNA(fMet) = tetrahydrofolate + N-formylmethionyl-tRNA(fMet). CC -!- SIMILARITY: Belongs to the Fmt family. 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; YP_001009419.1; NC_008816.1. DR ProteinModelPortal; A2BRA1; -. DR STRING; 146891.A9601_10281; -. DR EnsemblBacteria; ABM70312; ABM70312; A9601_10281. DR GeneID; 4717739; -. DR KEGG; pmb:A9601_10281; -. DR PATRIC; 22983559; VBIProMar75723_1035. DR eggNOG; COG0223; -. DR HOGENOM; HOG000261177; -. DR KO; K00604; -. DR OMA; PLGCWNG; -. DR ProtClustDB; CLSK921992; -. DR BioCyc; PMAR146891:GH90-1048-MONOMER; -. DR GO; GO:0004479; F:methionyl-tRNA formyltransferase activity; IEA:HAMAP. DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW. DR GO; GO:0006413; P:translational initiation; IEA:GOC. DR Gene3D; 3.10.25.10; -; 1. DR Gene3D; 3.40.50.170; -; 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; IPR011034; Formyl_transferase_C-like. DR InterPro; IPR015518; Met_tRNA_Form_TA-like. DR PANTHER; PTHR11138; PTHR11138; 1. DR Pfam; PF02911; Formyl_trans_C; 1. DR Pfam; PF00551; Formyl_trans_N; 1. DR SUPFAM; SSF50486; FMT_C_like; 1. DR SUPFAM; SSF53328; formyl_transf; 1. DR TIGRFAMs; TIGR00460; fmt; 1. DR PROSITE; PS00373; GART; FALSE_NEG. PE 3: Inferred from homology; KW Complete proteome; Protein biosynthesis; Transferase. FT CHAIN 1 328 Methionyl-tRNA formyltransferase. FT /FTId=PRO_1000020126. FT REGION 110 113 Tetrahydrofolate (THF) binding (By FT similarity). 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 //