ID A0A0M4MB63_9ACTN Unreviewed; 318 AA.
AC A0A0M4MB63;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
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:VHN99534.1};
GN ORFNames=AL705_00355 {ECO:0000313|EMBL:ALE18437.1}, LC603019_00076
GN {ECO:0000313|EMBL:VHN99534.1};
OS Lawsonella clevelandensis.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Lawsonellaceae;
OC Lawsonella.
OX NCBI_TaxID=1528099 {ECO:0000313|EMBL:ALE18437.1, ECO:0000313|Proteomes:UP000068137};
RN [1] {ECO:0000313|EMBL:ALE18437.1, ECO:0000313|Proteomes:UP000068137}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=X1698 {ECO:0000313|EMBL:ALE18437.1,
RC ECO:0000313|Proteomes:UP000068137};
RX PubMed=26659691;
RA Nicholson A.C., Bell M., Humrighouse B.W., McQuiston J.R.;
RT "Complete Genome Sequences for Two Strains of a Novel Fastidious, Partially
RT Acid-Fast, Gram-Positive Corynebacterineae Bacterium, Derived from Human
RT Clinical Samples.";
RL Genome Announc. 3:e01462-15(2015).
RN [2] {ECO:0000313|EMBL:ALE18437.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=X1698 {ECO:0000313|EMBL:ALE18437.1};
RX PubMed=27130323; DOI=10.1099/ijsem.0.001122;
RA Bell M.E., Bernard K.A., Harrington S.M., Patel N.B., Tucker T.A.,
RA Metcalfe M.G., McQuiston J.R.;
RT "Lawsonella clevelandensis gen. nov., sp. nov., a new member of the
RT suborder Corynebacterineae isolated from human abscesses.";
RL Int. J. Syst. Evol. Microbiol. 66:2929-2935(2016).
RN [3] {ECO:0000313|EMBL:VHN99534.1, ECO:0000313|Proteomes:UP000324288}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USB-603019 {ECO:0000313|EMBL:VHN99534.1};
RA Seth-Smith MB H., Seth-Smith H.;
RL Submitted (APR-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=(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; CP012390; ALE18437.1; -; Genomic_DNA.
DR EMBL; LR584267; VHN99534.1; -; Genomic_DNA.
DR RefSeq; WP_053961320.1; NZ_LR584267.1.
DR AlphaFoldDB; A0A0M4MB63; -.
DR STRING; 1528099.AL705_00355; -.
DR GeneID; 84894086; -.
DR KEGG; cbq:AL705_00355; -.
DR PATRIC; fig|1528099.3.peg.75; -.
DR OrthoDB; 9802815at2; -.
DR Proteomes; UP000068137; Chromosome.
DR Proteomes; UP000324288; Chromosome 1.
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:UP000068137};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00182}.
FT DOMAIN 2..180
FT /note="Formyl transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00551"
FT DOMAIN 204..309
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 318 AA; 34097 MW; F6B22FDE7C02C537 CRC64;
MRLVFAGTPE AAVPSLQALC DSPRHQVVAV ITQPDAPYGR GRKLRPSPVA LCAEEHGISV
LKPHSASDPE FLTQLASYRP DCCPVVAYGQ LLRPAVLEIP QHGWVNLHFS LLPQWRGAAP
VQSAIAAGDE LTGATTFRLD EGMDTGPIFG TVTETIRPTD TSDTLMQRLA EQGARLLIDT
MDGIAEGSLT PLPQPHDGVS YTSKISTEDA RIRWSLPTHL VDRHIRAMTP TPGAWTMLGE
VRLKIGSVEP LHPTAVHRLS SSGVALAPGQ LFFTGKHVLV GTATGVIQLA AIQVPGKKMM
NAADWARGAH LCGDEVMQ
//
