FMT_CHLAA
ID FMT_CHLAA Reviewed; 310 AA.
AC A9WAR0;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Methionyl-tRNA formyltransferase {ECO:0000255|HAMAP-Rule:MF_00182};
DE EC=2.1.2.9 {ECO:0000255|HAMAP-Rule:MF_00182};
GN Name=fmt {ECO:0000255|HAMAP-Rule:MF_00182}; OrderedLocusNames=Caur_0033;
OS Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl).
OC Bacteria; Chloroflexi; Chloroflexia; Chloroflexales; Chloroflexineae;
OC Chloroflexaceae; Chloroflexus.
OX NCBI_TaxID=324602;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29366 / DSM 635 / J-10-fl;
RX PubMed=21714912; DOI=10.1186/1471-2164-12-334;
RA Tang K.H., Barry K., Chertkov O., Dalin E., Han C.S., Hauser L.J.,
RA Honchak B.M., Karbach L.E., Land M.L., Lapidus A., Larimer F.W.,
RA Mikhailova N., Pitluck S., Pierson B.K., Blankenship R.E.;
RT "Complete genome sequence of the filamentous anoxygenic phototrophic
RT bacterium Chloroflexus aurantiacus.";
RL BMC Genomics 12:334-334(2011).
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:0000255|HAMAP-Rule:MF_00182}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-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:57454,
CC ChEBI:CHEBI:78530, ChEBI:CHEBI:78844; EC=2.1.2.9;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00182};
CC -!- SIMILARITY: Belongs to the Fmt family. {ECO:0000255|HAMAP-
CC Rule:MF_00182}.
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DR EMBL; CP000909; ABY33288.1; -; Genomic_DNA.
DR RefSeq; WP_012255944.1; NC_010175.1.
DR RefSeq; YP_001633677.1; NC_010175.1.
DR AlphaFoldDB; A9WAR0; -.
DR SMR; A9WAR0; -.
DR STRING; 324602.Caur_0033; -.
DR EnsemblBacteria; ABY33288; ABY33288; Caur_0033.
DR KEGG; cau:Caur_0033; -.
DR PATRIC; fig|324602.8.peg.36; -.
DR eggNOG; COG0223; Bacteria.
DR HOGENOM; CLU_033347_1_1_0; -.
DR InParanoid; A9WAR0; -.
DR OMA; CCPVVAY; -.
DR Proteomes; UP000002008; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004479; F:methionyl-tRNA formyltransferase activity; IBA:GO_Central.
DR GO; GO:0071951; P:conversion of methionyl-tRNA to N-formyl-methionyl-tRNA; IBA:GO_Central.
DR CDD; cd08646; FMT_core_Met-tRNA-FMT_N; 1.
DR CDD; cd08704; Met_tRNA_FMT_C; 1.
DR Gene3D; 3.10.25.10; -; 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; IPR044135; Met-tRNA-FMT_C.
DR InterPro; IPR041711; Met-tRNA-FMT_N.
DR Pfam; PF02911; Formyl_trans_C; 1.
DR Pfam; PF00551; Formyl_trans_N; 1.
DR SUPFAM; SSF50486; SSF50486; 1.
DR SUPFAM; SSF53328; SSF53328; 1.
DR TIGRFAMs; TIGR00460; fmt; 1.
PE 3: Inferred from homology;
KW Protein biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..310
FT /note="Methionyl-tRNA formyltransferase"
FT /id="PRO_1000118473"
FT BINDING 109..112
FT /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57453"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00182"
SQ SEQUENCE 310 AA; 33137 MW; C238A6878775B27A CRC64;
MRILFLGSPS FAVHALEALV AAGHEIVGVV TQPDRPAGRD RRLTPPPVKI AAMAHNLPVL
QPETLRDPTV VETLSALQPE VGVVAAYGEI LRRAVLSIPP LGYLNIHPSL LPLYRGPTPV
AGAILAGETV TGVTIMLLDP SMDSGPILAQ AVVDLPPTAR AGQLTDELFR IGADLLVQVL
PRYARGEIEP RPQDHSRATV TKMLKKEDGR IDWSLPAIVI ERMTRAYDPW PGAYTFWRGQ
PLRIIKAAVA SADGTNVPGT VIGRSGSGHP LVQTGSDALE LIEVQPASRR PMSGSAWLAG
VHADNIRLGE