ID FMT_GEOSL Reviewed; 317 AA.
AC Q74GW4;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 01-MAY-2013, entry version 58.
DE RecName: Full=Methionyl-tRNA formyltransferase;
DE EC=2.1.2.9;
GN Name=fmt; OrderedLocusNames=GSU0130;
OS Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Geobacteraceae; Geobacter.
OX NCBI_TaxID=243231;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51573 / DSM 12127 / PCA;
RX PubMed=14671304; DOI=10.1126/science.1088727;
RA Methe B.A., Nelson K.E., Eisen J.A., Paulsen I.T., Nelson W.C.,
RA Heidelberg J.F., Wu D., Wu M., Ward N.L., Beanan M.J., Dodson R.J.,
RA Madupu R., Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S.,
RA Gwinn M.L., Kolonay J.F., Sullivan S.A., Haft D.H., Selengut J.,
RA Davidsen T.M., Zafar N., White O., Tran B., Romero C., Forberger H.A.,
RA Weidman J.F., Khouri H.M., Feldblyum T.V., Utterback T.R.,
RA Van Aken S.E., Lovley D.R., Fraser C.M.;
RT "Genome of Geobacter sulfurreducens: metal reduction in subsurface
RT environments.";
RL Science 302:1967-1969(2003).
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; AE017180; AAR33465.1; -; Genomic_DNA.
DR RefSeq; NP_951192.1; NC_002939.5.
DR ProteinModelPortal; Q74GW4; -.
DR STRING; 243231.GSU0130; -.
DR EnsemblBacteria; AAR33465; AAR33465; GSU0130.
DR GeneID; 2687945; -.
DR KEGG; gsu:GSU0130; -.
DR PATRIC; 22023008; VBIGeoSul17553_0131.
DR eggNOG; COG0223; -.
DR HOGENOM; HOG000261177; -.
DR KO; K00604; -.
DR OMA; GITLMQM; -.
DR ProtClustDB; CLSK827657; -.
DR BioCyc; GSUL243231:GH27-149-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; 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; FALSE_NEG.
PE 3: Inferred from homology;
KW Complete proteome; Methyltransferase; Protein biosynthesis;
KW Reference proteome; Transferase.
FT CHAIN 1 317 Methionyl-tRNA formyltransferase.
FT /FTId=PRO_0000082969.
FT REGION 112 115 Tetrahydrofolate (THF) binding (By
FT similarity).
SQ SEQUENCE 317 AA; 34668 MW; BAF582625EF358A2 CRC64;
MAGLRIIFMG TPEFACPTLR KLIERGEEVI AVVTQPDRPK GRGQKLVPPP VKALAQEHDI
PVLQPLKVRT PESVDEIRRL APDLIVVVAF GQILPQSLLD IPKHGCINIH ASLLPRYRGA
APLNWCLING ETETGITTMM MDAGLDTGDM LVKRAIPIGP DEDAQSLHDR LSQLGAETID
ETLDLLLAGK LVREKQDDSL TCYAPMLKKE DGLVDWTREP VQVKNQVRGF TPWPGAYTFL
DGKTLKLYRV AVAGETGEPG EILRVGREGI LVGCGSGSIL IQELQLEGRK RLPTAEFLAG
FRLEPGTRLG EAGSVEH
//
