ID A0A3Q9HRL7_9FIRM Unreviewed; 314 AA.
AC A0A3Q9HRL7;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
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=BBF96_05890 {ECO:0000313|EMBL:AZR72965.1};
OS Anoxybacter fermentans.
OC Bacteria; Bacillota; Clostridia; Halanaerobiales; Anoxybacter.
OX NCBI_TaxID=1323375 {ECO:0000313|EMBL:AZR72965.1, ECO:0000313|Proteomes:UP000267250};
RN [1] {ECO:0000313|EMBL:AZR72965.1, ECO:0000313|Proteomes:UP000267250}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY22613 {ECO:0000313|EMBL:AZR72965.1,
RC ECO:0000313|Proteomes:UP000267250};
RA Zeng X., Shao Z.;
RT "Genome and transcriptome analysis of iron-reducing fermentative bacteria
RT Anoxybacter fermentans.";
RL Submitted (JUL-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; CP016379; AZR72965.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3Q9HRL7; -.
DR KEGG; aft:BBF96_05890; -.
DR OrthoDB; 9802815at2; -.
DR Proteomes; UP000267250; Chromosome.
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:UP000267250};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00182}.
FT DOMAIN 1..181
FT /note="Formyl transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00551"
FT DOMAIN 204..303
FT /note="Formyl transferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02911"
FT BINDING 110..113
FT /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57453"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00182"
SQ SEQUENCE 314 AA; 34970 MW; 270E6FE69B6C261E CRC64;
MRVVFMGTPD FAAICLKGLL NADFIDVIGV VTQPDRARGR GYKVTYSPVK KVALEANLPV
YQPENVNDSE FVDKLEGMNL DAIVVVAYGQ LLKERLLNLT PYGCINVHAS LLPKYRGAGP
IHRVIINGET KTGITTMYMD KGWDTGDMIL QKEVEIGSEM TVGELHDILA ELGSEVLVET
LRQIKNGTAP RIPQQHEKAT YAPKIKKEDG EIDWNQPARK IYNLVRGMDP WPGAYTWYKG
EIFKIWKTRI EENLTGGIPG QVMDVDLKKG ILVQTKEGGL WLTEVQSANS RRMDVGAFLN
GHNVKKGEVF GNAK
//
