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Database: UniProt
Entry: R5YQL4_9MOLU
LinkDB: R5YQL4_9MOLU
Original site: R5YQL4_9MOLU 
ID   R5YQL4_9MOLU            Unreviewed;       310 AA.
AC   R5YQL4;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 45.
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=BN735_00878 {ECO:0000313|EMBL:CDA23721.1};
OS   Mycoplasma sp. CAG:611.
OC   Bacteria; Mycoplasmatota; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=1262905 {ECO:0000313|EMBL:CDA23721.1, ECO:0000313|Proteomes:UP000018049};
RN   [1] {ECO:0000313|EMBL:CDA23721.1, ECO:0000313|Proteomes:UP000018049}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:611 {ECO:0000313|Proteomes:UP000018049};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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:CDA23721.1}.
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DR   EMBL; CBBK010000092; CDA23721.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5YQL4; -.
DR   STRING; 1262905.BN735_00878; -.
DR   Proteomes; UP000018049; 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; 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:UP000018049};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00182}.
FT   DOMAIN          5..179
FT                   /note="Formyl transferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00551"
FT   DOMAIN          204..299
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   310 AA;  35116 MW;  03AC53EC71521760 CRC64;
     MKDKKVVFMG TPKFSLNVLE SLIENCNVIA VVTQPDKEVG RKHVLTISPV KALALKHNIK
     VLQPRKLRNE YQDIIDLNPD VIITCAYGQI LPYELLSYPK YKTINVHASL LPKLRGGAPI
     QRAIMDGYKK TGVTIMRTEV GMDDGDMISS YEIEIKDDDT YETLSSKLSI VGKELLIKTL
     PSIFDGTCKY IKQNEDEVTF AKIIKKEDEY LNFNDTTINI YNKIRGLSPE PCCYFNLNNE
     RVKIYNAKIG NFKASSYGKI TNISKEGLGI STNDGEIIIT KLQFPGKKVM EFKDYLNGIK
     KEDLINKKIN
//
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