ID A0A0M3Q9Q5_9CORY Unreviewed; 312 AA.
AC A0A0M3Q9Q5;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 08-NOV-2023, entry version 33.
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 ECO:0000313|EMBL:ALC06003.1};
GN ORFNames=CDES_07990 {ECO:0000313|EMBL:ALC06003.1};
OS Corynebacterium deserti GIMN1.010.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=931089 {ECO:0000313|EMBL:ALC06003.1, ECO:0000313|Proteomes:UP000068067};
RN [1] {ECO:0000313|EMBL:ALC06003.1, ECO:0000313|Proteomes:UP000068067}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GIMN1.010 {ECO:0000313|EMBL:ALC06003.1,
RC ECO:0000313|Proteomes:UP000068067};
RA Ruckert C., Albersmeier A., Kalinowski J.;
RT "Complete genome sequence of Corynebacterium deserti GIMN1.010 (=DSM
RT 45689), isolated from desert sand in western China.";
RL Submitted (AUG-2014) 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; CP009220; ALC06003.1; -; Genomic_DNA.
DR RefSeq; WP_053545003.1; NZ_CP009220.1.
DR AlphaFoldDB; A0A0M3Q9Q5; -.
DR STRING; 931089.CDES_07990; -.
DR KEGG; cdx:CDES_07990; -.
DR PATRIC; fig|931089.4.peg.1612; -.
DR OrthoDB; 9802815at2; -.
DR Proteomes; UP000068067; 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};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00182}.
FT DOMAIN 2..183
FT /note="Formyl transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00551"
FT DOMAIN 207..303
FT /note="Formyl transferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02911"
FT BINDING 114..117
FT /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57453"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00182"
SQ SEQUENCE 312 AA; 33376 MW; CDCE0CBE49C2E2A7 CRC64;
MRLVFAGTPE PAVVALEKLI NSNHEVVAVL TQPDARRGRG RSLHPSAVAE LAEKHGIEVL
KPTSLKADTE DGQAVRTRLA ELEPDCLPVV AYGQLITKDL LDVAPHGWVN LHFSLLPAWR
GAAPVQASIR EGDEVTGATT FRIDEGLDTG VILSTLEEQI LSTDTADDLL TRLAYSGGDL
LVSTMDGLEA GTITPHPQEG EATYASKIST EDARIDWTKP AEVIDRHIRA HTPGPGAWTT
LVDARLKLGP ITHPGEVSQV PPGQIVAEKN SVLVGTGTTA VALNFIQPPG KKMMNAADWA
RGVHLETEAT FQ
//
