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Database: UniProt
Entry: A0A0Q9F5C3_9GAMM
LinkDB: A0A0Q9F5C3_9GAMM
Original site: A0A0Q9F5C3_9GAMM 
ID   A0A0Q9F5C3_9GAMM        Unreviewed;       307 AA.
AC   A0A0Q9F5C3;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 32.
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   ORFNames=ASE45_01290 {ECO:0000313|EMBL:KRD71569.1};
OS   Lysobacter sp. Root96.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Lysobacter.
OX   NCBI_TaxID=1736612 {ECO:0000313|EMBL:KRD71569.1, ECO:0000313|Proteomes:UP000050805};
RN   [1] {ECO:0000313|EMBL:KRD71569.1, ECO:0000313|Proteomes:UP000050805}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root96 {ECO:0000313|EMBL:KRD71569.1,
RC   ECO:0000313|Proteomes:UP000050805};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRD71569.1, ECO:0000313|Proteomes:UP000050805}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root96 {ECO:0000313|EMBL:KRD71569.1,
RC   ECO:0000313|Proteomes:UP000050805};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRD71569.1}.
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DR   EMBL; LMJN01000001; KRD71569.1; -; Genomic_DNA.
DR   RefSeq; WP_056305250.1; NZ_LMJN01000001.1.
DR   AlphaFoldDB; A0A0Q9F5C3; -.
DR   STRING; 1736612.ASE45_01290; -.
DR   OrthoDB; 9802815at2; -.
DR   Proteomes; UP000050805; Unassembled WGS sequence.
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   3: Inferred from homology;
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00182}; Reference proteome {ECO:0000313|Proteomes:UP000050805};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00182}.
FT   DOMAIN          1..176
FT                   /note="Formyl transferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00551"
FT   DOMAIN          203..300
FT                   /note="Formyl transferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02911"
FT   BINDING         108..111
FT                   /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:57453"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00182"
SQ   SEQUENCE   307 AA;  32866 MW;  0805AB5869B4A0ED CRC64;
     MRIVFAGTPD FAVPSLRAAA RHNEVVAVYT QPDRPAGRGR ELTPSPVKRE ALLRGIPVLQ
     PENFKAAISR QALRALQPDL MIVVAYGLIL PQSVLDIPTH GCWNVHASLL PRWRGAAPIQ
     RAIEAGDRET GVCLMQMEKG LDTGPVLLAQ TTEIGETETG GQLHDRLAEI GASVLSDGLG
     LLRAELRPQP WVQPEEGVTY AHKLDKAEAR LDWNQPAVAL AAKVRAFNPW PMAEAVVAGE
     RVRLHGAIAL PLAHGAAPGT LLQAGREGID IACGEGALRI RVLQRDGGKA ITAADYLNGR
     RDLAVGA
//
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