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Database: UniProt
Entry: Q114P5
LinkDB: Q114P5
Original site: Q114P5 
ID   FMT_TRIEI               Reviewed;         336 AA.
AC   Q114P5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   01-OCT-2014, entry version 58.
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=Tery_1769;
OS   Trichodesmium erythraeum (strain IMS101).
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales;
OC   Trichodesmium.
OX   NCBI_TaxID=203124;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMS101;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Kiss H., Munk A.C., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Richardson P.;
RT   "Complete sequence of Trichodesmium erythraeum IMS101.";
RL   Submitted (JUN-2006) 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}.
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DR   EMBL; CP000393; ABG51029.1; -; Genomic_DNA.
DR   RefSeq; YP_721502.1; NC_008312.1.
DR   ProteinModelPortal; Q114P5; -.
DR   STRING; 203124.Tery_1769; -.
DR   EnsemblBacteria; ABG51029; ABG51029; Tery_1769.
DR   GeneID; 4242234; -.
DR   KEGG; ter:Tery_1769; -.
DR   PATRIC; 23987613; VBITriEry99848_2241.
DR   eggNOG; COG0223; -.
DR   HOGENOM; HOG000261177; -.
DR   KO; K00604; -.
DR   OMA; QRFKIYE; -.
DR   OrthoDB; EOG6B09WV; -.
DR   BioCyc; TERY203124:GJDR-1781-MONOMER; -.
DR   GO; GO:0004479; F:methionyl-tRNA formyltransferase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:InterPro.
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   InterPro; IPR015518; Met_tRNA_Form_TA-like.
DR   PANTHER; PTHR11138; PTHR11138; 1.
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;
KW   Complete proteome; Protein biosynthesis; Reference proteome;
KW   Transferase.
FT   CHAIN         1    336       Methionyl-tRNA formyltransferase.
FT                                /FTId=PRO_1000020200.
FT   REGION      112    115       Tetrahydrofolate (THF) binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_00182}.
SQ   SEQUENCE   336 AA;  37076 MW;  E5CAFA7CF39AACFF CRC64;
     MMKIIFFGTP LFAVPTLKKL LDNPKIEVTA VVTQPDKRRG RGNKLIPSPV KSVAVAHNIP
     VWQPRRVKKN PETLNLLREA QADVFVVVAY GQILSTEILE MPKLGCVNVH GSILPKYRGA
     APIQWSIYHG EAETGNTTML MDVGMDTGPM LLKSIIPIGL LDNAVSIAEI LAKDGADLLL
     ETLLRLEDKE IEPIPQDNSL ATYAPLIQNS DYEIDWSRSA LDIHNQIRGF FPNCFTSFRG
     QSLKVMATIP VGTEYWSELP PELQKLEKVW SSESEVVGNI GEVVKVIKGL GPVVQTGSGW
     LLLWQVQLAG KKVVSGWDFA NGTRLLVGEV SEVFSR
//
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