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-MAY-2013, entry version 50.
DE RecName: Full=Methionyl-tRNA formyltransferase;
DE EC=2.1.2.9;
GN Name=fmt; 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 (By similarity).
CC -!- CATALYTIC ACTIVITY: 10-formyltetrahydrofolate + L-methionyl-
CC tRNA(fMet) = tetrahydrofolate + N-formylmethionyl-tRNA(fMet).
CC -!- SIMILARITY: Belongs to the fmt family.
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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; GITLMQM; -.
DR ProtClustDB; PRK00005; -.
DR GO; GO:0004479; F:methionyl-tRNA formyltransferase activity; IEA:HAMAP.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006413; P:translational initiation; IEA:GOC.
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; FMT_C_like; 1.
DR SUPFAM; SSF53328; formyl_transf; 1.
DR TIGRFAMs; TIGR00460; fmt; 1.
DR PROSITE; PS00373; GART; 1.
PE 3: Inferred from homology;
KW Complete proteome; Methyltransferase; Protein biosynthesis;
KW Transferase.
FT CHAIN 1 336 Methionyl-tRNA formyltransferase.
FT /FTId=PRO_1000020200.
FT REGION 112 115 Tetrahydrofolate (THF) binding (By
FT similarity).
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
//
