(data stored in ACNUC7421 zone)

SWISSPROT: FMT_PSEHT

ID   FMT_PSEHT               Reviewed;         321 AA.
AC   Q3IDI3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   08-MAY-2019, entry version 90.
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=PSHAa0022;
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125;
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N.,
RA   Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G.,
RA   Ho C., Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C.,
RA   Rouy Z., Sekowska A., Tutino M.L., Vallenet D., von Heijne G.,
RA   Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
CC   -!- FUNCTION: Attaches a formyl group to the free amino group of
CC       methionyl-tRNA(fMet). The formyl group appears to play a dual role
CC       in the initiator identity of N-formylmethionyl-tRNA by promoting
CC       its recognition by IF2 and preventing the misappropriation of this
CC       tRNA by the elongation apparatus. {ECO:0000255|HAMAP-
CC       Rule:MF_00182}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6S)-10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) =
CC         (6S)-5,6,7,8-tetrahydrofolate + H(+) + N-formyl-L-methionyl-
CC         tRNA(fMet); Xref=Rhea:RHEA:24380, Rhea:RHEA-COMP:9952,
CC         Rhea:RHEA-COMP:9953, ChEBI:CHEBI:15378, ChEBI:CHEBI:57453,
CC         ChEBI:CHEBI:57454, ChEBI:CHEBI:78530, ChEBI:CHEBI:78844;
CC         EC=2.1.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00182};
CC   -!- SIMILARITY: Belongs to the Fmt family. {ECO:0000255|HAMAP-
CC       Rule:MF_00182}.
DR   EMBL; CR954246; CAI85136.1; -; Genomic_DNA.
DR   RefSeq; WP_011326754.1; NC_007481.1.
DR   SMR; Q3IDI3; -.
DR   STRING; 326442.PSHAa0022; -.
DR   PRIDE; Q3IDI3; -.
DR   EnsemblBacteria; CAI85136; CAI85136; PSHAa0022.
DR   KEGG; pha:PSHAa0022; -.
DR   PATRIC; fig|326442.8.peg.24; -.
DR   eggNOG; ENOG4105CAE; Bacteria.
DR   eggNOG; COG0223; LUCA.
DR   HOGENOM; HOG000261177; -.
DR   KO; K00604; -.
DR   OMA; GITTMLM; -.
DR   OrthoDB; 2009156at2; -.
DR   BioCyc; PHAL326442:PSHA_RS00110-MONOMER; -.
DR   Proteomes; UP000006843; Chromosome I.
DR   GO; GO:0004479; F:methionyl-tRNA formyltransferase activity; IEA:UniProtKB-UniRule.
DR   CDD; cd08646; FMT_core_Met-tRNA-FMT_N; 1.
DR   Gene3D; 3.10.25.10; -; 1.
DR   HAMAP; MF_00182; Formyl_trans; 1.
DR   InterPro; IPR005794; Fmt.
DR   InterPro; IPR005793; Formyl_trans_C.
DR   InterPro; IPR037022; Formyl_trans_C_sf.
DR   InterPro; IPR002376; Formyl_transf_N.
DR   InterPro; IPR036477; Formyl_transf_N_sf.
DR   InterPro; IPR011034; Formyl_transferase-like_C_sf.
DR   InterPro; IPR001555; GART_AS.
DR   InterPro; IPR041711; Met-tRNA-FMT_N.
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;
DR   PRODOM; Q3IDI3.
DR   SWISS-2DPAGE; Q3IDI3.
KW   Complete proteome; Protein biosynthesis; Reference proteome;
KW   Transferase.
FT   CHAIN         1    321       Methionyl-tRNA formyltransferase.
FT                                /FTId=PRO_1000020132.
FT   REGION      113    116       Tetrahydrofolate (THF) binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_00182}.
SQ   SEQUENCE   321 AA;  34885 MW;  C360FE10C9BDFFD7 CRC64;
     MTQPLRIIFA GTPDFAARHL QALIQSEHQI VGVYSQPDRP AGRGKKLKAS EVKELALEHN
     LPVFQPQSLK TEDALNELTR LNADIMIVVA YGLILPKAIL DAPRLGCLNV HGSILPRWRG
     AAPIQRAIWA GDEQTGVTIM QMNEGLDTGD MLHISRCPIS ATETSASLYT KLADLGPGAL
     IDTINNLANG KITPEPQNDA AANYAKKLSK DEANIDWSMS AAQIERNIRA FNPWPVCFTQ
     MGGQPVKIYQ AHVVEQSSSQ PDNNGRVLSS DKNGVIVGCG EHALCITQLQ PQGKKPMAIN
     DFLNGRSDWV TPGTILGENN E
//

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