ID A0A1M4XD35_9RHOB Unreviewed; 302 AA.
AC A0A1M4XD35;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 30.
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=SAMN05444273_103132 {ECO:0000313|EMBL:SHE91388.1};
OS Litoreibacter ascidiaceicola.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Litoreibacter.
OX NCBI_TaxID=1486859 {ECO:0000313|EMBL:SHE91388.1, ECO:0000313|Proteomes:UP000184144};
RN [1] {ECO:0000313|EMBL:SHE91388.1, ECO:0000313|Proteomes:UP000184144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 100566 {ECO:0000313|EMBL:SHE91388.1,
RC ECO:0000313|Proteomes:UP000184144};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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=(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}.
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DR EMBL; FQUV01000003; SHE91388.1; -; Genomic_DNA.
DR RefSeq; WP_073142051.1; NZ_FQUV01000003.1.
DR AlphaFoldDB; A0A1M4XD35; -.
DR STRING; 1486859.SAMN05444273_103132; -.
DR OrthoDB; 9802815at2; -.
DR Proteomes; UP000184144; 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; 3.40.50.12230; -; 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};
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 201..292
FT /note="Formyl transferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02911"
FT REGION 31..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 302 AA; 31888 MW; 9714DD2A1E92C5B5 CRC64;
MKIVFMGTPE FSVPVLEALV GAGHEIVAVY SQPPRPAGRG KKDRPSPVQA RAEELGLAVR
HPVSLKGAHE QAEFAGLGAD VAVVVAYGLI LPQAVLDAPK HGCLNIHASL LPRWRGAAPI
HRAIMAGDAE TGVCIMQMEA GLDTGPVLLR QATEIGATET TGQLHDWLSA IGAKMIVEAL
ARLDKLVPEP QPEDGVTYAA KIDKAEARID WMRGAAEIVC QINGLSPFPG AWTEADGERI
KCLRAEVADR DLPVGEVIVS KDSLDVGCGD GAVSVLTLQR AGKKAGEASV VTQGWTPPKR
FS
//
