ID A0A4V1E1B4_9RHOB Unreviewed; 298 AA.
AC A0A4V1E1B4;
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=EOK75_17705 {ECO:0000313|EMBL:QCO57544.1};
OS Pseudorhodobacter turbinis.
OG Plasmid unnamed1 {ECO:0000313|EMBL:QCO57544.1,
OG ECO:0000313|Proteomes:UP000298631}.
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Rhodobacterales; Paracoccaceae; Pseudorhodobacter.
OX NCBI_TaxID=2500533 {ECO:0000313|EMBL:QCO57544.1, ECO:0000313|Proteomes:UP000298631};
RN [1] {ECO:0000313|EMBL:QCO57544.1, ECO:0000313|Proteomes:UP000298631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S12M18 {ECO:0000313|EMBL:QCO57544.1,
RC ECO:0000313|Proteomes:UP000298631};
RC PLASMID=unnamed1 {ECO:0000313|EMBL:QCO57544.1,
RC ECO:0000313|Proteomes:UP000298631};
RA Jeong Y.-S., Kang W.-R., Bae J.-W.;
RT "Pseudorhodobacter turbinis sp. nov., isolated from the gut of the Korean
RT turban shell.";
RL Submitted (MAY-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}.
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DR EMBL; CP039965; QCO57544.1; -; Genomic_DNA.
DR RefSeq; WP_137195338.1; NZ_CP039965.1.
DR AlphaFoldDB; A0A4V1E1B4; -.
DR KEGG; pseb:EOK75_17705; -.
DR OrthoDB; 9802815at2; -.
DR Proteomes; UP000298631; Plasmid unnamed1.
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 Plasmid {ECO:0000313|EMBL:QCO57544.1};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00182}; Reference proteome {ECO:0000313|Proteomes:UP000298631};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00182}.
FT DOMAIN 1..178
FT /note="Formyl transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00551"
FT DOMAIN 200..291
FT /note="Formyl transferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02911"
FT REGION 30..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 298 AA; 31772 MW; F829DE75007CCAFC CRC64;
MRVIFMGTPD FSVPVLEALA EKHEVVAVYS QPPRPAGRGK KDRPSPVHQR AEALGLPVHT
PASLRNEEAA KTFADLGADV AVVVAYGLIL PQNILDMPQH GCLNIHASLL PRWRGAAPIH
RAIMAGDKAT GVCIMQMEAG LDTGPVLLRA QTPIDATETT QDLHDRLSTM GAGLIVDALD
ELPSLTPTQQ PDAGVTYAAK IDKAEARVDW SQPAETVDRQ IRGLSPFPGA WCDVAGERVK
LLRSRLGNGQ GAPGQVLDGF TVACGSGAVE ILTAQREGKR PAEAQDILRG FSLPERLS
//
