ID A0A4R7K3B5_9GAMM Unreviewed; 313 AA.
AC A0A4R7K3B5;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 02-APR-2025, entry version 22.
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 ORFNames=DES49_0188 {ECO:0000313|EMBL:TDT44089.1};
OS Halospina denitrificans.
OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Halospina.
OX NCBI_TaxID=332522 {ECO:0000313|EMBL:TDT44089.1, ECO:0000313|Proteomes:UP000295830};
RN [1] {ECO:0000313|EMBL:TDT44089.1, ECO:0000313|Proteomes:UP000295830}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15505 {ECO:0000313|EMBL:TDT44089.1,
RC ECO:0000313|Proteomes:UP000295830};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (MAR-2019) 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|HAMAP-Rule:MF_00182}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-methionyl-tRNA(fMet) + (6R)-10-formyltetrahydrofolate = N-
CC formyl-L-methionyl-tRNA(fMet) + (6S)-5,6,7,8-tetrahydrofolate + H(+);
CC Xref=Rhea:RHEA:24380, Rhea:RHEA-COMP:9952, Rhea:RHEA-COMP:9953,
CC 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 -!- 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:TDT44089.1}.
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DR EMBL; SOAX01000001; TDT44089.1; -; Genomic_DNA.
DR RefSeq; WP_133734513.1; NZ_SOAX01000001.1.
DR AlphaFoldDB; A0A4R7K3B5; -.
DR OrthoDB; 9802815at2; -.
DR Proteomes; UP000295830; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
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 FunFam; 3.40.50.12230:FF:000001; Methionyl-tRNA formyltransferase; 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; 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:UP000295830};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00182}.
FT DOMAIN 1..180
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 109..112
FT /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57453"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00182"
SQ SEQUENCE 313 AA; 33411 MW; 1633ABD5CF532551 CRC64;
MRVVFAGTPD FAAASLRALL DAGHEVAAVY TQPDRPSGRG RHARPGPVAS LAREHGIALE
QPESLRNAEA RARLASYEPE VMVVAAYGLI LPQAVLDIPE FGCLNVHASL LPRWRGAAPI
QWAIASGDAE TGITIMQMDA GLDTGDILLS KRLTIHPDET GGSLHDRLAP LGGEALLEAL
QQLQAGSLRA EPQDSHHATY ARKLERADSP VDWHQSAATL ARHIRAFNPW PVCTTHVGET
TLKLLFAEAV NDEAATEAPG TVIERNRDGA LIQCGEGLLN LTRLQLPGGK PQTVGDLING
GKPLLEPGQR LGK
//
