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Database: UniProt
Entry: A0A2M9BYI2_9MICO
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Original site: A0A2M9BYI2_9MICO 
ID   A0A2M9BYI2_9MICO        Unreviewed;       306 AA.
AC   A0A2M9BYI2;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   24-JAN-2024, entry version 22.
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=CLV54_0800 {ECO:0000313|EMBL:PJJ63144.1};
OS   Compostimonas suwonensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Compostimonas.
OX   NCBI_TaxID=1048394 {ECO:0000313|EMBL:PJJ63144.1, ECO:0000313|Proteomes:UP000230161};
RN   [1] {ECO:0000313|EMBL:PJJ63144.1, ECO:0000313|Proteomes:UP000230161}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25625 {ECO:0000313|EMBL:PJJ63144.1,
RC   ECO:0000313|Proteomes:UP000230161};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): From Individual Species to Whole Genera.";
RL   Submitted (NOV-2017) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PJJ63144.1}.
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DR   EMBL; PGFB01000002; PJJ63144.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2M9BYI2; -.
DR   OrthoDB; 9802815at2; -.
DR   Proteomes; UP000230161; Unassembled WGS sequence.
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:UP000230161};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00182}.
FT   DOMAIN          1..172
FT                   /note="Formyl transferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00551"
FT   DOMAIN          205..297
FT                   /note="Formyl transferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02911"
FT   BINDING         108..111
FT                   /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:57453"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00182"
SQ   SEQUENCE   306 AA;  32064 MW;  CD529FC4EC516E48 CRC64;
     MRLVFAGTPD AAVPSLRALH ASAHEVHAVV TRQDAPLGRK KVLTPSPVAR AADELGLPVL
     KANRLDEEAT ERIGALWPEL GVIVAYGGLI REPLLSTPTH GWINLHFSVL PRWRGAAPVQ
     RAIMAGDPVL GASVFQLVAG LDEGPVFATL ERPALPAETA GDALTDLAGR GAALLADVVD
     AIAAGTARST QQRGESNYAA KLGIDDARID WTRSAQEVSQ RVRGVTPEPG AFTTIDEERF
     KILAIGGAHD TVTLAPGAIE SRDGAVLVGT GTVALELALV QPAGKRPMEA AAWWRGHAAS
     ETVVAR
//
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