ID A0A1S2L701_9BACI Unreviewed; 314 AA.
AC A0A1S2L701;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 28-JAN-2026, entry version 33.
DE RecName: Full=Methionyl-tRNA formyltransferase {ECO:0000256|ARBA:ARBA00016014, 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=AWH56_017025 {ECO:0000313|EMBL:QOY34416.1}, AWH56_19835
GN {ECO:0000313|EMBL:OIJ08161.1};
OS Anaerobacillus isosaccharinicus.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC Anaerobacillus.
OX NCBI_TaxID=1532552 {ECO:0000313|EMBL:OIJ08161.1, ECO:0000313|Proteomes:UP000180175};
RN [1] {ECO:0000313|EMBL:OIJ08161.1, ECO:0000313|Proteomes:UP000180175}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NB2006 {ECO:0000313|EMBL:OIJ08161.1,
RC ECO:0000313|Proteomes:UP000180175};
RA Bassil N.M., Lloyd J.R.;
RT "Draft genome sequences of four alkaliphilic bacteria belonging to the
RT Anaerobacillus genus.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QOY34416.1, ECO:0000313|Proteomes:UP000180175}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NB2006 {ECO:0000313|EMBL:QOY34416.1,
RC ECO:0000313|Proteomes:UP000180175};
RX PubMed=28104661;
RA Bassil N.M., Lloyd J.R.;
RT "Draft Genome Sequences of Four Alkaliphilic Bacteria Belonging to the
RT Anaerobacillus Genus.";
RL Genome Announc. 5:e01493-e01416(2017).
RN [3] {ECO:0000313|EMBL:QOY34416.1, ECO:0000313|Proteomes:UP000180175}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NB2006 {ECO:0000313|EMBL:QOY34416.1,
RC ECO:0000313|Proteomes:UP000180175};
RX PubMed=29580368;
RA Bassil N.M., Lloyd J.R.;
RT "Anaerobacillus isosaccharinicus sp. nov., an alkaliphilic bacterium which
RT degrades isosaccharinic acid.";
RL Int. J. Syst. Evol. Microbiol. 69:3666-3671(2019).
RN [4] {ECO:0000313|EMBL:QOY34416.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NB2006 {ECO:0000313|EMBL:QOY34416.1};
RA Bassil N.M., Lloyd J.R.;
RL Submitted (OCT-2020) 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|ARBA:ARBA00002606,
CC ECO:0000256|HAMAP-Rule:MF_00182}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-methionyl-tRNA(fMet) + (6R)-10-formyltetrahydrofolate = N-
CC formyl-L-methionyl-tRNA(fMet) + (6S)-5,6,7,8-tetrahydrofolate + H(+);
CC Xref=Rhea:RHEA:24380, Rhea:RHEA-COMP:9952, Rhea:RHEA-COMP:9953,
CC 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|ARBA:ARBA00048558, ECO:0000256|HAMAP-
CC 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; LQXD01000165; OIJ08161.1; -; Genomic_DNA.
DR EMBL; CP063356; QOY34416.1; -; Genomic_DNA.
DR RefSeq; WP_071318697.1; NZ_CP063356.2.
DR AlphaFoldDB; A0A1S2L701; -.
DR KEGG; aia:AWH56_017025; -.
DR OrthoDB; 9802815at2; -.
DR Proteomes; UP000180175; Chromosome.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
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 FunFam; 3.40.50.12230:FF:000001; Methionyl-tRNA formyltransferase; 1.
DR FunFam; 3.40.50.170:FF:000004; Methionyl-tRNA formyltransferase; 1.
DR Gene3D; 3.10.25.10; Formyl transferase, C-terminal domain; 1.
DR Gene3D; 3.40.50.170; Formyl transferase, N-terminal domain; 1.
DR HAMAP; MF_00182; Formyl_trans; 1.
DR InterPro; IPR005794; Fmt.
DR InterPro; IPR005793; Formyl_trans_C.
DR InterPro; IPR037022; Formyl_trans_C_sf.
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}; Reference proteome {ECO:0000313|Proteomes:UP000180175};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00182}.
FT DOMAIN 1..178
FT /note="Formyl transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00551"
FT DOMAIN 203..302
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 314 AA; 34714 MW; E9465B2A0B9D3F71 CRC64;
MRVVFMGTPD FSVPVLRRLI EEGYEIVGVV TQPDRPKGRK KELTPPPVKV EAVNHGLPII
QPEKLKRPED LQQVLDLQPD LVITAAFGQI LPKQLLDTPK FGCINVHASL LPEYRGGAPI
HQAIVDGKKE TGITIMYMVE KLDAGDILTQ AKVNIEEEDH VGSLHNKLSV IGAELLSHTI
PNLIAGKLTP IKQEDEKVTF APNISREKEK INWAANGEAI YNQIRGLHPW PVAYTLLNDQ
PLKVWWAQKV SKQNGDHSPG TIVAIESDGF IVSTGNETYI KVTDLQPSGK KRMLAEQFLR
GATEDLTVGT KLGE
//
