(data stored in ACNUC7421 zone)

SWISSPROT: FMT_SINFN

ID   FMT_SINFN               Reviewed;         311 AA.
AC   C3MF25;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   07-JUN-2017, entry version 53.
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=NGR_c00580;
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234;
RX   PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of
RT   secretion systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
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; CP001389; ACP23862.1; -; Genomic_DNA.
DR   RefSeq; WP_012706647.1; NC_012587.1.
DR   RefSeq; YP_002824615.1; NC_012587.1.
DR   ProteinModelPortal; C3MF25; -.
DR   SMR; C3MF25; -.
DR   STRING; 394.NGR_c00580; -.
DR   EnsemblBacteria; ACP23862; ACP23862; NGR_c00580.
DR   GeneID; 7790637; -.
DR   KEGG; rhi:NGR_c00580; -.
DR   PATRIC; fig|394.7.peg.2851; -.
DR   eggNOG; ENOG4105CAE; Bacteria.
DR   eggNOG; COG0223; LUCA.
DR   HOGENOM; HOG000261177; -.
DR   KO; K00604; -.
DR   OMA; LRIVFMG; -.
DR   OrthoDB; POG091H01YM; -.
DR   Proteomes; UP000001054; 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; C3MF25.
DR   SWISS-2DPAGE; C3MF25.
KW   Complete proteome; Protein biosynthesis; Reference proteome;
KW   Transferase.
FT   CHAIN         1    311       Methionyl-tRNA formyltransferase.
FT                                /FTId=PRO_1000190035.
FT   REGION      112    115       Tetrahydrofolate (THF) binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_00182}.
SQ   SEQUENCE   311 AA;  33008 MW;  16F61F3BF28C6CAF CRC64;
     MPLRIIFMGT PEFSVPTLAA LVEAGHEIAA VYTQPPRPGG RRGLDLQKSP VHQAAELLGV
     PVLTPVNFKD AADRQAFRDF NADVAVVVAY GLLLPEEILS GTRYGCYNGH ASLLPRWRGA
     APIQRAIMAG DRETGMMVMK MDKGLDTGPV ALTKTVPIGE TMTAGELHDK LMHAGAALMK
     EAMVKLELGE LPLTPQPQEG VLYAAKISKD ETRIDFTKPA ADVHNHIRGL APFPGAWFEL
     ETAGRTERIK VLGSEPAAGA GAPGTILDDA LTIACGDGAV RPTRLQRAGG KPLATPDFLR
     GSPIAAGTRI C
//

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