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Database: UniProt/TrEMBL
Entry: F8FU69_PSEPU
LinkDB: F8FU69_PSEPU
Original site: F8FU69_PSEPU 
ID   F8FU69_PSEPU            Unreviewed;       310 AA.
AC   F8FU69;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   03-APR-2013, entry version 13.
DE   RecName: Full=Methionyl-tRNA formyltransferase;
DE            EC=2.1.2.9;
GN   Name=fmt; ORFNames=PPS_0030;
OS   Pseudomonas putida S16.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1042876;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=S16;
RX   PubMed=21914868; DOI=10.1128/JB.05663-11;
RA   Yu H., Tang H., Wang L., Yao Y., Wu G., Xu P.;
RT   "Complete Genome Sequence of the Nicotine-Degrading Pseudomonas putida
RT   Strain S16.";
RL   J. Bacteriol. 193:5541-5542(2011).
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; CP002870; AEJ10619.1; -; Genomic_DNA.
DR   RefSeq; YP_004699499.1; NC_015733.1.
DR   EnsemblBacteria; AEJ10619; AEJ10619; PPS_0030.
DR   GeneID; 10935702; -.
DR   KEGG; ppt:PPS_0030; -.
DR   KO; K00604; -.
DR   BioCyc; PPUT1042876:GH0R-30-MONOMER; -.
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   Methyltransferase; Protein biosynthesis; Transferase.
FT   REGION      109    112       Tetrahydrofolate (THF) binding (By
FT                                similarity).
SQ   SEQUENCE   310 AA;  32926 MW;  B7242087AE8C26EA CRC64;
     MRIVFAGTPE FAAEHLKALL DSPYEIVAVY TQPDRPAGRG QKLMPSPVKQ LAVAHDIPVF
     QPPTLRNAEA QAELAALKPD LMVVVAYGLI LPQVVLDIPR LGCINSHASL LPRWRGAAPI
     QRAVEAGDAE SGVTVMRMEA GLDTGPMLLK VVTPISAEDT GGSLHDRLAE MGPPAVVQAI
     AGLADGSLQG EVQDDALATY AHKLNKDEAR IDWSRPAVEL ERLIRAFNPW PVCHSTLDGE
     SVKVLAANLS TATGTPGEIL SASKDGLVVA CGDQALSLTR LQLPGGKALN FSDLFNSRRE
     KFASGKVLGQ
//
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