FMT_VIBCH
ID FMT_VIBCH Reviewed; 315 AA.
AC Q9KVU4;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 125.
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=VC_0045;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
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, ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE003852; AAF93223.1; -; Genomic_DNA.
DR PIR; H82372; H82372.
DR RefSeq; NP_229704.1; NC_002505.1.
DR RefSeq; WP_000083540.1; NZ_LT906614.1.
DR PDB; 3Q0I; X-ray; 1.89 A; A=1-315.
DR PDBsum; 3Q0I; -.
DR AlphaFoldDB; Q9KVU4; -.
DR SMR; Q9KVU4; -.
DR STRING; 243277.VC_0045; -.
DR DNASU; 2614441; -.
DR EnsemblBacteria; AAF93223; AAF93223; VC_0045.
DR GeneID; 57741454; -.
DR KEGG; vch:VC_0045; -.
DR PATRIC; fig|243277.26.peg.44; -.
DR eggNOG; COG0223; Bacteria.
DR HOGENOM; CLU_033347_1_2_6; -.
DR OMA; CCPVVAY; -.
DR BioCyc; VCHO:VC0045-MON; -.
DR EvolutionaryTrace; Q9KVU4; -.
DR Proteomes; UP000000584; Chromosome 1.
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; IPR001555; GART_AS.
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.
DR PROSITE; PS00373; GART; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Protein biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..315
FT /note="Methionyl-tRNA formyltransferase"
FT /id="PRO_0000083080"
FT BINDING 113..116
FT /ligand="(6S)-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57453"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00182"
FT STRAND 6..10
FT /evidence="ECO:0007829|PDB:3Q0I"
FT HELIX 14..24
FT /evidence="ECO:0007829|PDB:3Q0I"
FT STRAND 26..34
FT /evidence="ECO:0007829|PDB:3Q0I"
FT HELIX 51..58
FT /evidence="ECO:0007829|PDB:3Q0I"
FT HELIX 72..79
FT /evidence="ECO:0007829|PDB:3Q0I"
FT STRAND 84..90
FT /evidence="ECO:0007829|PDB:3Q0I"
FT HELIX 97..100
FT /evidence="ECO:0007829|PDB:3Q0I"
FT STRAND 107..114
FT /evidence="ECO:0007829|PDB:3Q0I"
FT TURN 115..118
FT /evidence="ECO:0007829|PDB:3Q0I"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:3Q0I"
FT HELIX 123..130
FT /evidence="ECO:0007829|PDB:3Q0I"
FT STRAND 133..141
FT /evidence="ECO:0007829|PDB:3Q0I"
FT STRAND 144..147
FT /evidence="ECO:0007829|PDB:3Q0I"
FT STRAND 151..158
FT /evidence="ECO:0007829|PDB:3Q0I"
FT HELIX 165..188
FT /evidence="ECO:0007829|PDB:3Q0I"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:3Q0I"
FT HELIX 210..213
FT /evidence="ECO:0007829|PDB:3Q0I"
FT HELIX 221..230
FT /evidence="ECO:0007829|PDB:3Q0I"
FT TURN 231..235
FT /evidence="ECO:0007829|PDB:3Q0I"
FT STRAND 238..241
FT /evidence="ECO:0007829|PDB:3Q0I"
FT STRAND 244..254
FT /evidence="ECO:0007829|PDB:3Q0I"
FT STRAND 264..269
FT /evidence="ECO:0007829|PDB:3Q0I"
FT STRAND 272..276
FT /evidence="ECO:0007829|PDB:3Q0I"
FT STRAND 278..288
FT /evidence="ECO:0007829|PDB:3Q0I"
FT HELIX 297..304
FT /evidence="ECO:0007829|PDB:3Q0I"
FT TURN 305..308
FT /evidence="ECO:0007829|PDB:3Q0I"
SQ SEQUENCE 315 AA; 34200 MW; D4244B566330CFB1 CRC64;
MSQSLRIVFA GTPDFAARHL AALLSSEHEI IAVYTQPERP AGRGKKLTAS PVKTLALEHN
VPVYQPENFK SDESKQQLAA LNADLMVVVA YGLLLPKVVL DTPKLGCINV HGSILPRWRG
AAPIQRSIWA GDSETGVTIM QMDVGLDTGD MLKIATLPIE ASDTSASMYD KLAELGPQAL
LECLQDIAQG TAVAVKQDDG LANYAHKLSK EEARINWSDA ATHIERCIRA FNPWPMSHFE
VAENSIKVWQ ARVETRAVTQ TPGTIIQADK SGIYVATGQD VLVLESLQIP GKKALPVQDI
LNARADWFSV GSQLS
