(data stored in ACNUC7421 zone)

SWISSPROT: FMT_SHESH

ID   FMT_SHESH               Reviewed;         329 AA.
AC   A8FP74;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   07-JUN-2017, entry version 62.
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=Ssed_0034;
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000821; ABV34647.1; -; Genomic_DNA.
DR   RefSeq; WP_012004173.1; NC_009831.1.
DR   ProteinModelPortal; A8FP74; -.
DR   SMR; A8FP74; -.
DR   STRING; 425104.Ssed_0034; -.
DR   EnsemblBacteria; ABV34647; ABV34647; Ssed_0034.
DR   KEGG; sse:Ssed_0034; -.
DR   eggNOG; ENOG4105CAE; Bacteria.
DR   eggNOG; COG0223; LUCA.
DR   HOGENOM; HOG000261177; -.
DR   KO; K00604; -.
DR   OMA; LRIVFMG; -.
DR   OrthoDB; POG091H01YM; -.
DR   Proteomes; UP000002015; 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; A8FP74.
DR   SWISS-2DPAGE; A8FP74.
KW   Complete proteome; Protein biosynthesis; Transferase.
FT   CHAIN         1    329       Methionyl-tRNA formyltransferase.
FT                                /FTId=PRO_1000077322.
FT   REGION      112    115       Tetrahydrofolate (THF) binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_00182}.
SQ   SEQUENCE   329 AA;  35602 MW;  31EA9AEDAB596A77 CRC64;
     MKPLNIIFAG TPDFAARHLQ ALIDSEHNII GVYSQPDRPA GRGKKLQASP VKSLAIEHNL
     PVFQPKSLRD EQAQAELANL NADIMVVVAY GLILPKVVLD TPKLGCINVH GSILPRWRGA
     APIQRALWAG DTETGVTIMQ MDIGLDTGDM LLKTRLPIED NDTSASLYEK LALQGPDALI
     EALTGLAKGE LTAEKQDESL ANYAEKLSKE EAELDWSKSA LELWREIRAF NPWPISHFTH
     QDASIKVRES AVSNLSSDAP AGTIISAGKQ GIDIATGDGV LTLLNMQLPG KKPLSVGDIL
     NSRGEWFTPG TLLNSKKLIG KEPAVKEAE
//

If you have problems or comments...

PBIL Back to PBIL home page