ID D1C2Z5_SPHTD Unreviewed; 314 AA. AC D1C2Z5; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 27-MAR-2024, entry version 81. DE RecName: Full=Methionyl-tRNA formyltransferase {ECO:0000256|ARBA:ARBA00012261, ECO:0000256|HAMAP-Rule:MF_00182}; DE EC=2.1.2.9 {ECO:0000256|ARBA:ARBA00012261, ECO:0000256|HAMAP-Rule:MF_00182}; GN Name=fmt {ECO:0000256|HAMAP-Rule:MF_00182}; GN OrderedLocusNames=Sthe_1176 {ECO:0000313|EMBL:ACZ38612.1}; OS Sphaerobacter thermophilus (strain DSM 20745 / S 6022). OC Bacteria; Thermomicrobiota; Thermomicrobia; Sphaerobacterales; OC Sphaerobacterineae; Sphaerobacteraceae; Sphaerobacter. OX NCBI_TaxID=479434 {ECO:0000313|EMBL:ACZ38612.1, ECO:0000313|Proteomes:UP000002027}; RN [1] {ECO:0000313|Proteomes:UP000002027} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49802 / DSM 20745 / S 6022 RC {ECO:0000313|Proteomes:UP000002027}; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N., RA Mikhailova N., LaButti K.M., Clum A., Sun H.I., Brettin T., Detter J.C., RA Han C., Larimer F., Land M., Hauser L., Markowitz V., Cheng J.F., RA Hugenholtz P., Woyke T., Wu D., Steenblock K., Schneider S., Pukall R., RA Goeker M., Klenk H.P., Eisen J.A.; RT "The complete chromosome 1 of Sphaerobacter thermophilus DSM 20745."; RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ACZ38612.1, ECO:0000313|Proteomes:UP000002027} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49802 / DSM 20745 / S 6022 RC {ECO:0000313|Proteomes:UP000002027}; RX PubMed=21304676; RA Spring S., Nolan M., Lapidus A., Glavina Del Rio T., Copeland A., Tice H., RA Cheng J.F., Lucas S., Land M., Chen F., Bruce D., Goodwin L., Pitluck S., RA Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K., RA Hauser L., Chang Y.J., Jeffries C.D., Munk C., Kiss H., Chain P., Han C., RA Brettin T., Detter J.C., Schuler E., Goker M., Rohde M., Bristow J., RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of Desulfohalobium retbaense type strain RT (HR(100))."; RL Stand. Genomic Sci. 2:38-48(2010). 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:0000256|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:0000256|HAMAP-Rule:MF_00182}; CC -!- SIMILARITY: Belongs to the Fmt family. {ECO:0000256|ARBA:ARBA00010699, CC ECO:0000256|HAMAP-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; CP001823; ACZ38612.1; -; Genomic_DNA. DR RefSeq; WP_012871659.1; NC_013523.1. DR AlphaFoldDB; D1C2Z5; -. DR STRING; 479434.Sthe_1176; -. DR KEGG; sti:Sthe_1176; -. DR eggNOG; COG0223; Bacteria. DR HOGENOM; CLU_033347_1_1_0; -. DR InParanoid; D1C2Z5; -. DR OrthoDB; 9802815at2; -. DR Proteomes; UP000002027; Chromosome 1. 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; 3.40.50.12230; -; 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 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. PE 3: Inferred from homology; KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP- KW Rule:MF_00182}; Reference proteome {ECO:0000313|Proteomes:UP000002027}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00182}. FT DOMAIN 6..183 FT /note="Formyl transferase N-terminal" FT /evidence="ECO:0000259|Pfam:PF00551" FT DOMAIN 207..302 FT /note="Formyl transferase C-terminal" FT /evidence="ECO:0000259|Pfam:PF02911" FT BINDING 112..115 FT /ligand="(6S)-5,6,7,8-tetrahydrofolate" FT /ligand_id="ChEBI:CHEBI:57453" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00182" SQ SEQUENCE 314 AA; 33662 MW; 3BBACF9AA3D417ED CRC64; MAISVVFLGS PAFAVPSLRA LALDARFTIP LVVTQPDRPA GRGRRPRPPA VKDAAIELGL PVFQPETLRD PAAVERLAAA VPDVLVVVAY GEILRQSVLD LAPLGCLNVH PSLLPRYRGS SPVQAAILNG DTETGISIIK LVRRMDAGPI VAQRRVPLDG TETAGTLSER LANLAAEMLP DVVAAWVAGE LEAEPQDDAA ATYTRELTTA DARIDWGKDA AEIERLVRAM QPWPKAWSIL EGRRLAVLAC DISHKPSTEP PGTINVSARP PRVATGTTDL VLLRVQPEGK REMAAEDWAR GARLPHGARF APVE //