ID FMT_BACAN Reviewed; 314 AA. AC Q81WH2; Q6HUM0; Q6KNV4; DT 04-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 24-JAN-2024, entry version 136. 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=BA_4004, GBAA_4004, BAS3717; OS Bacillus anthracis. OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=1392; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ames / isolate Porton; RX PubMed=12721629; DOI=10.1038/nature01586; RA Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., RA Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., RA Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., RA Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L., RA DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C., RA Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y., RA Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M., RA Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E., RA White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., RA Hanna P.C., Kolstoe A.-B., Fraser C.M.; RT "The genome sequence of Bacillus anthracis Ames and comparison to closely RT related bacteria."; RL Nature 423:81-86(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ames ancestor; RX PubMed=18952800; DOI=10.1128/jb.01347-08; RA Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D., RA Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.; RT "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'."; RL J. Bacteriol. 191:445-446(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Sterne; RA Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., RA Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., RA Richardson P., Rubin E., Tice H.; RT "Complete genome sequence of Bacillus anthracis Sterne."; RL Submitted (JAN-2004) 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=(6R)-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:78530, CC ChEBI:CHEBI:78844, ChEBI:CHEBI:195366; 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; AE016879; AAP27732.1; -; Genomic_DNA. DR EMBL; AE017334; AAT33120.1; -; Genomic_DNA. DR EMBL; AE017225; AAT56019.1; -; Genomic_DNA. DR RefSeq; NP_846246.1; NC_003997.3. DR RefSeq; WP_000598790.1; NZ_WXXJ01000026.1. DR RefSeq; YP_029968.1; NC_005945.1. DR PDB; 4IQF; X-ray; 2.40 A; A/B/C/D=1-314. DR PDBsum; 4IQF; -. DR AlphaFoldDB; Q81WH2; -. DR SMR; Q81WH2; -. DR STRING; 261594.GBAA_4004; -. DR DNASU; 1086742; -. DR GeneID; 45023695; -. DR KEGG; ban:BA_4004; -. DR KEGG; bar:GBAA_4004; -. DR KEGG; bat:BAS3717; -. DR PATRIC; fig|198094.11.peg.3974; -. DR eggNOG; COG0223; Bacteria. DR HOGENOM; CLU_033347_1_1_9; -. DR OMA; CCPVVAY; -. DR OrthoDB; 9802815at2; -. DR Proteomes; UP000000427; Chromosome. DR Proteomes; UP000000594; 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 Gene3D; 3.10.25.10; Formyl transferase, C-terminal domain; 1. DR Gene3D; 3.40.50.170; Formyl transferase, N-terminal domain; 1. DR HAMAP; MF_00182; Formyl_trans; 1. DR InterPro; IPR005794; Fmt. DR InterPro; IPR005793; Formyl_trans_C. DR InterPro; IPR037022; Formyl_trans_C_sf. 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 NCBIfam; TIGR00460; fmt; 1. DR PANTHER; PTHR11138; METHIONYL-TRNA FORMYLTRANSFERASE; 1. DR PANTHER; PTHR11138:SF5; METHIONYL-TRNA FORMYLTRANSFERASE, MITOCHONDRIAL; 1. DR Pfam; PF02911; Formyl_trans_C; 1. DR Pfam; PF00551; Formyl_trans_N; 1. DR SUPFAM; SSF50486; FMT C-terminal domain-like; 1. DR SUPFAM; SSF53328; Formyltransferase; 1. DR PROSITE; PS00373; GART; 1. PE 1: Evidence at protein level; KW 3D-structure; Protein biosynthesis; Reference proteome; Transferase. FT CHAIN 1..314 FT /note="Methionyl-tRNA formyltransferase" FT /id="PRO_0000082910" 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" FT STRAND 3..8 FT /evidence="ECO:0007829|PDB:4IQF" FT HELIX 13..22 FT /evidence="ECO:0007829|PDB:4IQF" FT STRAND 26..31 FT /evidence="ECO:0007829|PDB:4IQF" FT TURN 39..42 FT /evidence="ECO:0007829|PDB:4IQF" FT HELIX 48..55 FT /evidence="ECO:0007829|PDB:4IQF" FT HELIX 69..78 FT /evidence="ECO:0007829|PDB:4IQF" FT STRAND 81..87 FT /evidence="ECO:0007829|PDB:4IQF" FT HELIX 94..97 FT /evidence="ECO:0007829|PDB:4IQF" FT STRAND 104..110 FT /evidence="ECO:0007829|PDB:4IQF" FT STRAND 114..118 FT /evidence="ECO:0007829|PDB:4IQF" FT HELIX 120..126 FT /evidence="ECO:0007829|PDB:4IQF" FT STRAND 130..138 FT /evidence="ECO:0007829|PDB:4IQF" FT STRAND 148..155 FT /evidence="ECO:0007829|PDB:4IQF" FT HELIX 162..185 FT /evidence="ECO:0007829|PDB:4IQF" FT HELIX 196..198 FT /evidence="ECO:0007829|PDB:4IQF" FT HELIX 207..210 FT /evidence="ECO:0007829|PDB:4IQF" FT HELIX 218..226 FT /evidence="ECO:0007829|PDB:4IQF" FT TURN 227..232 FT /evidence="ECO:0007829|PDB:4IQF" FT STRAND 234..238 FT /evidence="ECO:0007829|PDB:4IQF" FT STRAND 241..252 FT /evidence="ECO:0007829|PDB:4IQF" FT STRAND 261..265 FT /evidence="ECO:0007829|PDB:4IQF" FT STRAND 270..272 FT /evidence="ECO:0007829|PDB:4IQF" FT STRAND 275..287 FT /evidence="ECO:0007829|PDB:4IQF" FT HELIX 295..301 FT /evidence="ECO:0007829|PDB:4IQF" SQ SEQUENCE 314 AA; 34736 MW; 8E81D02492DABEE2 CRC64; MIKVVFMGTP DFSVPVLRRL IEDGYDVIGV VTQPDRPVGR KKVLTPTPVK VEAEKHGIPV LQPLRIREKD EYEKVLALEP DLIVTAAFGQ IVPNEILEAP KYGCINVHAS LLPELRGGAP IHYAIMEGKE KTGITIMYMV EKLDAGDILT QVEVEIEERE TTGSLFDKLS EAGAHLLSKT VPLLIQGKLE PIKQNEEEVT FAYNIKREQE KIDWTKTGEE VYNHIRGLNP WPVAYTTLAG QVVKVWWGEK VPVTKSAEAG TIVAIEEDGF VVATGNETGV KITELQPSGK KRMSCSQFLR GTKPEIGTKL GENA //