FMT_PSEAE
ID FMT_PSEAE Reviewed; 314 AA.
AC O85732;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 131.
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=PA0018;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10499278; DOI=10.1111/j.1574-6968.1999.tb08690.x;
RA Newton D.T., Niemkiewicz M., Lo R.Y.C., Mangroo D.;
RT "Recognition of the initiator tRNA by the Pseudomonas aeruginosa methionyl-
RT tRNA formyltransferase: importance of the base-base mismatch at the end of
RT the acceptor stem.";
RL FEMS Microbiol. Lett. 178:289-298(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(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}.
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DR EMBL; AF073952; AAC26787.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG03408.1; -; Genomic_DNA.
DR PIR; G83643; G83643.
DR RefSeq; NP_248708.1; NC_002516.2.
DR RefSeq; WP_003114642.1; NZ_QZGE01000012.1.
DR PDB; 5UAI; X-ray; 2.75 A; A/B/C/D=1-314.
DR PDBsum; 5UAI; -.
DR AlphaFoldDB; O85732; -.
DR SMR; O85732; -.
DR STRING; 287.DR97_2971; -.
DR PaxDb; O85732; -.
DR PRIDE; O85732; -.
DR EnsemblBacteria; AAG03408; AAG03408; PA0018.
DR GeneID; 879258; -.
DR KEGG; pae:PA0018; -.
DR PATRIC; fig|208964.12.peg.17; -.
DR PseudoCAP; PA0018; -.
DR HOGENOM; CLU_033347_1_2_6; -.
DR InParanoid; O85732; -.
DR OMA; CCPVVAY; -.
DR PhylomeDB; O85732; -.
DR BioCyc; PAER208964:G1FZ6-18-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004479; F:methionyl-tRNA formyltransferase activity; ISS:PseudoCAP.
DR GO; GO:0071951; P:conversion of methionyl-tRNA to N-formyl-methionyl-tRNA; IBA:GO_Central.
DR GO; GO:0022898; P:regulation of transmembrane transporter activity; IMP:PseudoCAP.
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..314
FT /note="Methionyl-tRNA formyltransferase"
FT /id="PRO_0000083017"
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..11
FT /evidence="ECO:0007829|PDB:5UAI"
FT HELIX 14..24
FT /evidence="ECO:0007829|PDB:5UAI"
FT STRAND 26..34
FT /evidence="ECO:0007829|PDB:5UAI"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:5UAI"
FT HELIX 51..58
FT /evidence="ECO:0007829|PDB:5UAI"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:5UAI"
FT HELIX 72..79
FT /evidence="ECO:0007829|PDB:5UAI"
FT STRAND 84..90
FT /evidence="ECO:0007829|PDB:5UAI"
FT HELIX 97..100
FT /evidence="ECO:0007829|PDB:5UAI"
FT STRAND 107..113
FT /evidence="ECO:0007829|PDB:5UAI"
FT TURN 115..118
FT /evidence="ECO:0007829|PDB:5UAI"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:5UAI"
FT HELIX 123..129
FT /evidence="ECO:0007829|PDB:5UAI"
FT STRAND 133..141
FT /evidence="ECO:0007829|PDB:5UAI"
FT STRAND 151..158
FT /evidence="ECO:0007829|PDB:5UAI"
FT HELIX 165..188
FT /evidence="ECO:0007829|PDB:5UAI"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:5UAI"
FT TURN 210..213
FT /evidence="ECO:0007829|PDB:5UAI"
FT HELIX 221..230
FT /evidence="ECO:0007829|PDB:5UAI"
FT TURN 231..235
FT /evidence="ECO:0007829|PDB:5UAI"
FT STRAND 237..241
FT /evidence="ECO:0007829|PDB:5UAI"
FT STRAND 244..254
FT /evidence="ECO:0007829|PDB:5UAI"
FT STRAND 262..267
FT /evidence="ECO:0007829|PDB:5UAI"
FT STRAND 270..274
FT /evidence="ECO:0007829|PDB:5UAI"
FT STRAND 276..286
FT /evidence="ECO:0007829|PDB:5UAI"
FT HELIX 295..299
FT /evidence="ECO:0007829|PDB:5UAI"
FT HELIX 304..306
FT /evidence="ECO:0007829|PDB:5UAI"
SQ SEQUENCE 314 AA; 33028 MW; EA1570CDCD61F269 CRC64;
MSQALRIVFA GTPEFAAEHL KALLDTPHRI VAVYTQPDRP AGRGQKLMPS AVKSLALEHG
LPVMQPQSLR NAEAQAELAA LRADLMVVVA YGLILPQAVL DIPRLGCINS HASLLPRWRG
AAPIQRAVEA GDAESGVTVM QMEAGLDTGP MLLKVSTPIS AADTGGSLHD RLAALGPKAV
IEAIAGLAAG TLHGEIQDDA LATYAHKLNK DEARLDWSRP AVELERQVRA FTPWPVCHTS
LADAPLKVLG ASLGQGSGAP GTILEASRDG LLVACGEGAL RLTRLQLPGG KPLAFADLYN
SRREQFAAGQ VLGQ
