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Database: UniProt
Entry: A0A146G852_TERSA
LinkDB: A0A146G852_TERSA
Original site: A0A146G852_TERSA 
ID   A0A146G852_TERSA        Unreviewed;       315 AA.
AC   A0A146G852;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 35.
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=TSACC_22310 {ECO:0000313|EMBL:GAT33889.1};
OS   Terrimicrobium sacchariphilum.
OC   Bacteria; Verrucomicrobiota; Terrimicrobiia; Terrimicrobiales;
OC   Terrimicrobiaceae; Terrimicrobium.
OX   NCBI_TaxID=690879 {ECO:0000313|EMBL:GAT33889.1, ECO:0000313|Proteomes:UP000076023};
RN   [1] {ECO:0000313|Proteomes:UP000076023}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NM-5 {ECO:0000313|Proteomes:UP000076023};
RA   Qiu Y., Matsuura N., Ohashi A., Tourlousse M.D., Sekiguchi Y.;
RT   "Draft genome sequence of Terrimicrobium sacchariphilum strain NM-5.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000076023}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NM-5 {ECO:0000313|Proteomes:UP000076023};
RA   Qiu Y.-L., Tourlousse D.M., Matsuura N., Ohashi A., Sekiguchi Y.;
RT   "Draft genome sequence of Terrimicrobium sacchariphilum NM-5(T), a
RT   facultative anaerobic soil bacterium of the class Spartobacteria.";
RL   Genome Announc. 0:0-0(2017).
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=(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|ARBA:ARBA00036072, 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}.
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:GAT33889.1}.
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DR   EMBL; BDCO01000002; GAT33889.1; -; Genomic_DNA.
DR   RefSeq; WP_075079570.1; NZ_BDCO01000002.1.
DR   AlphaFoldDB; A0A146G852; -.
DR   STRING; 690879.TSACC_22310; -.
DR   InParanoid; A0A146G852; -.
DR   OrthoDB; 9802815at2; -.
DR   Proteomes; UP000076023; 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; 3.10.25.10; 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};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00182}.
FT   DOMAIN          5..183
FT                   /note="Formyl transferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00551"
FT   DOMAIN          206..306
FT                   /note="Formyl transferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02911"
FT   BINDING         112..115
FT                   /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:57453"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00182"
SQ   SEQUENCE   315 AA;  33975 MW;  48B52EDB0D8DC738 CRC64;
     MSQLRIVFMG TGGIGVPSLR ALVAEGHDVV AVYTQPDRPA GRDMKLRPSP VKLVAQELGV
     PVLQPERIRL PEEIEQLKAL RADLAVVVAY GQILPKTVLE TPRHGCWNIH ASLLPRHRGA
     APIQAAILAG DSQSGVTIMQ MDEGLDTGPI LVQEAFDLHR HETGGSLHDR LGVQAPSLLL
     QVLAKLQAGT LQMTPQDSEL STYAPKLSRE NGRIDWTHSA REIDRQIRAF TPWPGAFTTI
     DQGGQAVVLK IHRSALTRNL RGEPGTVLKA DRRGILVAAG EGGILLLQVQ APGGKRLAAH
     QYLLGHPLTV GSRLG
//
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