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Database: UniProt
Entry: Q4KKR0
LinkDB: Q4KKR0
Original site: Q4KKR0 
ID   FMT_PSEF5               Reviewed;         319 AA.
AC   Q4KKR0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   19-FEB-2014, entry version 57.
DE   RecName: Full=Methionyl-tRNA formyltransferase;
DE            EC=2.1.2.9;
GN   Name=fmt; OrderedLocusNames=PFL_0021;
OS   Pseudomonas fluorescens (strain Pf-5 / ATCC BAA-477).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=220664;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pf-5 / ATCC BAA-477;
RX   PubMed=15980861; DOI=10.1038/nbt1110;
RA   Paulsen I.T., Press C.M., Ravel J., Kobayashi D.Y., Myers G.S.A.,
RA   Mavrodi D.V., DeBoy R.T., Seshadri R., Ren Q., Madupu R., Dodson R.J.,
RA   Durkin A.S., Brinkac L.M., Daugherty S.C., Sullivan S.A.,
RA   Rosovitz M.J., Gwinn M.L., Zhou L., Schneider D.J., Cartinhour S.W.,
RA   Nelson W.C., Weidman J., Watkins K., Tran K., Khouri H., Pierson E.A.,
RA   Pierson L.S. III, Thomashow L.S., Loper J.E.;
RT   "Complete genome sequence of the plant commensal Pseudomonas
RT   fluorescens Pf-5.";
RL   Nat. Biotechnol. 23:873-878(2005).
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; CP000076; AAY95439.1; -; Genomic_DNA.
DR   RefSeq; YP_257173.1; NC_004129.6.
DR   ProteinModelPortal; Q4KKR0; -.
DR   SMR; Q4KKR0; 2-312.
DR   STRING; 220664.PFL_0021; -.
DR   EnsemblBacteria; AAY95439; AAY95439; PFL_0021.
DR   GeneID; 3480621; -.
DR   KEGG; pfl:PFL_0021; -.
DR   PATRIC; 19869147; VBIPseFlu72549_0021.
DR   eggNOG; COG0223; -.
DR   HOGENOM; HOG000261177; -.
DR   KO; K00604; -.
DR   OMA; KVWKAEV; -.
DR   OrthoDB; EOG6B09WV; -.
DR   ProtClustDB; PRK00005; -.
DR   BioCyc; PFLU220664:GIX8-21-MONOMER; -.
DR   GO; GO:0004479; F:methionyl-tRNA formyltransferase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:GOC.
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; 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; Transferase.
FT   CHAIN         1    319       Methionyl-tRNA formyltransferase.
FT                                /FTId=PRO_1000020131.
FT   REGION      113    116       Tetrahydrofolate (THF) binding (By
FT                                similarity).
SQ   SEQUENCE   319 AA;  33862 MW;  FB754897B2979334 CRC64;
     MTEPLRIVFA GTPEFAAEHL KALLDSPYQI VAVYTQPDRP AGRGQKLMPS PVKQLALEND
     IPVLQPPTLR NAEAQAELAA LKPDLMVVVA YGLILPQAVL DIPRLGCINS HASLLPRWRG
     AAPIQRAVQA GDAQSGVTVM RMEAGLDTGP MLLKVSTPIS AEDTGGSLHD RLAEMGPPAV
     LQAIEGLAAG TLEGEVQDDS LATYAHKLNK DEARIDWSRP AVELERLVRA FNPWPICHSS
     LNGEALKVLA ATLAEGKGAP GEILGASKDG LIVACGEQAL CLTRLQLPGG KALNFSDLFN
     SRREKFAIGT VLGQTADAQ
//
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