ID   Q1MQA7_LAWIP            Unreviewed;       322 AA.
AC   Q1MQA7;
DT   30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   30-MAY-2006, sequence version 1.
DT   27-MAR-2024, entry version 103.
DE   RecName: Full=Methionyl-tRNA formyltransferase {ECO:0000256|ARBA:ARBA00016014, 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   ECO:0000313|EMBL:CAJ54820.1};
GN   OrderedLocusNames=LI0766 {ECO:0000313|EMBL:CAJ54820.1};
OS   Lawsonia intracellularis (strain PHE/MN1-00).
OC   Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC   Desulfovibrionaceae; Lawsonia.
OX   NCBI_TaxID=363253 {ECO:0000313|EMBL:CAJ54820.1, ECO:0000313|Proteomes:UP000002430};
RN   [1] {ECO:0000313|EMBL:CAJ54820.1, ECO:0000313|Proteomes:UP000002430}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PHE/MN1-00 {ECO:0000313|EMBL:CAJ54820.1,
RC   ECO:0000313|Proteomes:UP000002430};
RA   Kaur K., Zhang Q., Beckler D., Munir S., Li L., Kinsley K., Herron L.,
RA   Peterson A., May B., Singh S., Gebhart C., Kapur V.;
RT   "The complete genome sequence of Lawsonia intracellularis: the causative
RT   agent of proliferative enteropathy.";
RL   Submitted (NOV-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:0000256|ARBA:ARBA00002606,
CC       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|ARBA:ARBA00036072, ECO:0000256|HAMAP-
CC         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; AM180252; CAJ54820.1; -; Genomic_DNA.
DR   RefSeq; WP_011526849.1; NC_008011.1.
DR   AlphaFoldDB; Q1MQA7; -.
DR   STRING; 363253.LI0766; -.
DR   KEGG; lip:LI0766; -.
DR   eggNOG; COG0223; Bacteria.
DR   HOGENOM; CLU_033347_1_1_7; -.
DR   OrthoDB; 9802815at2; -.
DR   Proteomes; UP000002430; 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; 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:UP000002430};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00182}.
FT   DOMAIN          9..186
FT                   /note="Formyl transferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00551"
FT   DOMAIN          212..321
FT                   /note="Formyl transferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02911"
FT   BINDING         117..120
FT                   /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:57453"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00182"
SQ   SEQUENCE   322 AA;  35502 MW;  E9DB9BE81986FC4B CRC64;
     MILQNKPLRI VFMGTPEFAA IILQKIVASG KVDIIASYCQ PDRPVGRGHK VQFSAVKILS
     NSLRIPVYQP VNFKSEYEIE KLYALKPDLL VVAAYGLILP QSVLDIPAIS PLNVHASLLP
     CYRGAAPIQR ALMNNDKKTG VTIIRMEKGL DTGAMFTHEE IPINMEDTAA TMHEKLAQLG
     GKLLINIFEQ IIQGTLSDPT PQDDIQATYA PKLTKSDGCI YWDMPAENVH AVVRGVTPWP
     GAQTSFKLVN RNPINILFQP GEIGSNELFK YNEGDSPLPG SILGLKGNAI AIACKDVPYL
     IYTLRPEGRK TMTAKDFWNG YL
//