(data stored in ACNUC7421 zone)

SWISSPROT: FMT_PSEAB

ID   FMT_PSEAB               Reviewed;         314 AA.
AC   Q02V63;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   07-JUN-2017, entry version 66.
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};
GN   OrderedLocusNames=PA14_00190;
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14;
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L.,
RA   Grills G., Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(2006).
CC   -!- FUNCTION: Modifies the free amino group of the aminoacyl moiety of
CC       methionyl-tRNA(fMet). The formyl group appears to play a dual role
CC       in the initiator identity of N-formylmethionyl-tRNA by: (I)
CC       promoting its recognition by IF2 and (II) impairing its binding to
CC       EFTu-GTP. {ECO:0000255|HAMAP-Rule:MF_00182}.
CC   -!- CATALYTIC ACTIVITY: 10-formyltetrahydrofolate + L-methionyl-
CC       tRNA(fMet) = tetrahydrofolate + N-formylmethionyl-tRNA(fMet).
CC       {ECO:0000255|HAMAP-Rule:MF_00182}.
CC   -!- SIMILARITY: Belongs to the Fmt family. {ECO:0000255|HAMAP-
CC       Rule:MF_00182}.
DR   EMBL; CP000438; ABJ14974.1; -; Genomic_DNA.
DR   RefSeq; WP_003142204.1; NC_008463.1.
DR   ProteinModelPortal; Q02V63; -.
DR   SMR; Q02V63; -.
DR   PRIDE; Q02V63; -.
DR   EnsemblBacteria; ABJ14974; ABJ14974; PA14_00190.
DR   KEGG; pau:PA14_00190; -.
DR   HOGENOM; HOG000261177; -.
DR   KO; K00604; -.
DR   OMA; LRIVFMG; -.
DR   Proteomes; UP000000653; Chromosome.
DR   GO; GO:0004479; F:methionyl-tRNA formyltransferase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.10.25.10; -; 1.
DR   Gene3D; 3.40.50.170; -; 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; IPR011034; Formyl_transferase_C-like.
DR   InterPro; IPR001555; GART_AS.
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   3: Inferred from homology;
DR   PRODOM; Q02V63.
DR   SWISS-2DPAGE; Q02V63.
KW   Complete proteome; Protein biosynthesis; Transferase.
FT   CHAIN         1    314       Methionyl-tRNA formyltransferase.
FT                                /FTId=PRO_1000020129.
FT   REGION      113    116       Tetrahydrofolate (THF) binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_00182}.
SQ   SEQUENCE   314 AA;  33032 MW;  F41570CEC2D1D8E8 CRC64;
     MSQALRIVFA GTPEFAAEHL KALLDTPHRI VAVYTQPDRP AGRGQKLMPS AVKSLALEHG
     LPVMQPQSLR NAEAQAELAA LRADLMVVVA YGLILPQAVL DIPRLGCINS HASLLPRWRG
     AAPIQRAVEA GDAESGVTVM QMEAGLDTGP MLLKVSTPIS AADTGGSLHD RLAALGPKAV
     VEAIAGLAAG TLHGEDQDDA LATYAHKLNK DEARLDWSRP AVELERQVRA FTPWPVCHTS
     LADAPLKVLG ASLGQGSGAP GTILEASRDG LLVACGEGAL RLTRLQVPGG KPLAFADLYN
     SRREQFATGQ VLGQ
//

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