ID FMT_COXBU Reviewed; 314 AA.
AC Q83AA8;
DT 04-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 116.
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=CBU_1997;
OS Coxiella burnetii (strain RSA 493 / Nine Mile phase I).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC Coxiella.
OX NCBI_TaxID=227377;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RSA 493 / Nine Mile phase I;
RX PubMed=12704232; DOI=10.1073/pnas.0931379100;
RA Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C.,
RA Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T.,
RA Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M.,
RA Lee K.H., Carty H.A., Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E.,
RA Fraser C.M., Heidelberg J.F.;
RT "Complete genome sequence of the Q-fever pathogen, Coxiella burnetii.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003).
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=(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: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; AE016828; AAO91486.1; -; Genomic_DNA.
DR RefSeq; NP_820972.1; NC_002971.3.
DR RefSeq; WP_010958586.1; NZ_CCYB01000066.1.
DR PDB; 3TQQ; X-ray; 2.00 A; A=1-314.
DR PDBsum; 3TQQ; -.
DR AlphaFoldDB; Q83AA8; -.
DR SMR; Q83AA8; -.
DR STRING; 227377.CBU_1997; -.
DR DNASU; 1209910; -.
DR EnsemblBacteria; AAO91486; AAO91486; CBU_1997.
DR GeneID; 1209910; -.
DR KEGG; cbu:CBU_1997; -.
DR PATRIC; fig|227377.7.peg.1984; -.
DR eggNOG; COG0223; Bacteria.
DR HOGENOM; CLU_033347_1_2_6; -.
DR OrthoDB; 9802815at2; -.
DR Proteomes; UP000002671; 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; 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 1: Evidence at protein level;
KW 3D-structure; Protein biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..314
FT /note="Methionyl-tRNA formyltransferase"
FT /id="PRO_0000082955"
FT BINDING 111..114
FT /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57453"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00182"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:3TQQ"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:3TQQ"
FT HELIX 15..23
FT /evidence="ECO:0007829|PDB:3TQQ"
FT STRAND 24..32
FT /evidence="ECO:0007829|PDB:3TQQ"
FT HELIX 49..56
FT /evidence="ECO:0007829|PDB:3TQQ"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:3TQQ"
FT HELIX 70..77
FT /evidence="ECO:0007829|PDB:3TQQ"
FT STRAND 82..88
FT /evidence="ECO:0007829|PDB:3TQQ"
FT HELIX 95..98
FT /evidence="ECO:0007829|PDB:3TQQ"
FT STRAND 105..111
FT /evidence="ECO:0007829|PDB:3TQQ"
FT TURN 113..116
FT /evidence="ECO:0007829|PDB:3TQQ"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:3TQQ"
FT HELIX 121..128
FT /evidence="ECO:0007829|PDB:3TQQ"
FT STRAND 131..139
FT /evidence="ECO:0007829|PDB:3TQQ"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:3TQQ"
FT STRAND 149..156
FT /evidence="ECO:0007829|PDB:3TQQ"
FT HELIX 163..187
FT /evidence="ECO:0007829|PDB:3TQQ"
FT HELIX 197..199
FT /evidence="ECO:0007829|PDB:3TQQ"
FT HELIX 208..211
FT /evidence="ECO:0007829|PDB:3TQQ"
FT HELIX 219..228
FT /evidence="ECO:0007829|PDB:3TQQ"
FT TURN 229..233
FT /evidence="ECO:0007829|PDB:3TQQ"
FT STRAND 236..239
FT /evidence="ECO:0007829|PDB:3TQQ"
FT STRAND 242..252
FT /evidence="ECO:0007829|PDB:3TQQ"
FT STRAND 263..267
FT /evidence="ECO:0007829|PDB:3TQQ"
FT STRAND 270..274
FT /evidence="ECO:0007829|PDB:3TQQ"
FT STRAND 276..286
FT /evidence="ECO:0007829|PDB:3TQQ"
FT HELIX 295..302
FT /evidence="ECO:0007829|PDB:3TQQ"
FT HELIX 303..305
FT /evidence="ECO:0007829|PDB:3TQQ"
FT TURN 308..310
FT /evidence="ECO:0007829|PDB:3TQQ"
SQ SEQUENCE 314 AA; 34288 MW; 11A4B3CCB9ED0AD8 CRC64;
MSLKIVFAGT PQFAVPTLRA LIDSSHRVLA VYTQPDRPSG RGQKIMESPV KEIARQNEIP
IIQPFSLRDE VEQEKLIAMN ADVMVVVAYG LILPKKALNA FRLGCVNVHA SLLPRWRGAA
PIQRAILAGD RETGISIMQM NEGLDTGDVL AKSACVISSE DTAADLHDRL SLIGADLLLE
SLAKLEKGDI KLEKQDEASA TYASKIQKQE ALIDWRKSAV EIARQVRAFN PTPIAFTYFE
GQPMRIWRAT VVDEKTDFEP GVLVDADKKG ISIAAGSGIL RLHQLQLPGK RVCSAGDFIN
AHGDKLIPGK TVFG
//
