ID A0A1G7BDJ2_9ACTN Unreviewed; 308 AA.
AC A0A1G7BDJ2;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
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=SAMN04489747_2920 {ECO:0000313|EMBL:SDE25093.1};
OS Auraticoccus monumenti.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Auraticoccus.
OX NCBI_TaxID=675864 {ECO:0000313|EMBL:SDE25093.1, ECO:0000313|Proteomes:UP000198546};
RN [1] {ECO:0000313|EMBL:SDE25093.1, ECO:0000313|Proteomes:UP000198546}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MON 2.2 {ECO:0000313|EMBL:SDE25093.1,
RC ECO:0000313|Proteomes:UP000198546};
RA de Groot N.N.;
RL Submitted (OCT-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; LT629688; SDE25093.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G7BDJ2; -.
DR STRING; 675864.SAMN04489747_2920; -.
DR OrthoDB; 9802815at2; -.
DR Proteomes; UP000198546; Chromosome i.
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; 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:UP000198546};
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..297
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 308 AA; 32143 MW; 2A0C6282F6E1C743 CRC64;
MRLVFAGTPD VAVPSLDALL ASSHEVVAVV TRPDAPAGRG KRLTASPVGL RAEEAGIPVL
KPEHPRDEDF VTALTELAPD CCPVVAYGAL VPQRVLDVPA HGWVNLHFSL LPAWRGAAPV
QHAVLAGDEV TGASTFRLVR EMDAGPVFGT VTDTIAPTDT SGDLLQRLSL SGAELLVRTL
DEIEAGTATP VEQPTEGVTL APKITVADAQ ISWDRPAEEI DRLVRGCQPA PGAWTTFRGE
RFKVVSAALS EESLAPGRIE GGRKSVLVGT GTTALQLGLV QPPGKKAMAA ADWSRGVQLD
ADEGLGAG
//
