(data stored in SCRATCH zone)

SWISSPROT: C6AZ60_RHILS

ID   C6AZ60_RHILS            Unreviewed;       311 AA.
AC   C6AZ60;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   07-JUN-2017, entry version 56.
DE   RecName: Full=Methionyl-tRNA formyltransferase {ECO:0000256|HAMAP-Rule:MF_00182, ECO:0000256|SAAS:SAAS00656934};
DE            EC=2.1.2.9 {ECO:0000256|HAMAP-Rule:MF_00182, ECO:0000256|SAAS:SAAS00650543};
GN   Name=fmt {ECO:0000256|HAMAP-Rule:MF_00182};
GN   OrderedLocusNames=Rleg_0075 {ECO:0000313|EMBL:ACS54386.1};
OS   Rhizobium leguminosarum bv. trifolii (strain WSM1325).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=395491 {ECO:0000313|EMBL:ACS54386.1, ECO:0000313|Proteomes:UP000002256};
RN   [1] {ECO:0000313|EMBL:ACS54386.1, ECO:0000313|Proteomes:UP000002256}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM1325 {ECO:0000313|EMBL:ACS54386.1,
RC   ECO:0000313|Proteomes:UP000002256};
RX   PubMed=21304718;
RA   Reeve W., O'Hara G., Chain P., Ardley J., Brau L., Nandesena K.,
RA   Tiwari R., Copeland A., Nolan M., Han C., Brettin T., Land M.,
RA   Ovchinikova G., Ivanova N., Mavromatis K., Markowitz V., Kyrpides N.,
RA   Melino V., Denton M., Yates R., Howieson J.;
RT   "Complete genome sequence of Rhizobium leguminosarum bv. trifolii
RT   strain WSM1325, an effective microsymbiont of annual Mediterranean
RT   clovers.";
RL   Stand. Genomic Sci. 2:347-356(2010).
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. {ECO:0000256|HAMAP-Rule:MF_00182,
CC       ECO:0000256|SAAS:SAAS00656940}.
CC   -!- CATALYTIC ACTIVITY: 10-formyltetrahydrofolate + L-methionyl-
CC       tRNA(fMet) = tetrahydrofolate + N-formylmethionyl-tRNA(fMet).
CC       {ECO:0000256|HAMAP-Rule:MF_00182, ECO:0000256|SAAS:SAAS00650545}.
CC   -!- SIMILARITY: Belongs to the Fmt family. {ECO:0000256|HAMAP-
CC       Rule:MF_00182, ECO:0000256|SAAS:SAAS00650538}.
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DR   EMBL; CP001622; ACS54386.1; -; Genomic_DNA.
DR   RefSeq; WP_012755816.1; NC_012850.1.
DR   ProteinModelPortal; C6AZ60; -.
DR   EnsemblBacteria; ACS54386; ACS54386; Rleg_0075.
DR   KEGG; rlg:Rleg_0075; -.
DR   HOGENOM; HOG000261177; -.
DR   KO; K00604; -.
DR   OMA; LRIVFMG; -.
DR   OrthoDB; POG091H01YM; -.
DR   Proteomes; UP000002256; Chromosome.
DR   GO; GO:0004479; F:methionyl-tRNA formyltransferase activity; IEA:UniProtKB-HAMAP.
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   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; C6AZ60.
DR   SWISS-2DPAGE; C6AZ60.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002256};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00182,
KW   ECO:0000256|SAAS:SAAS00650549};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00182,
KW   ECO:0000256|SAAS:SAAS00650558, ECO:0000313|EMBL:ACS54386.1}.
FT   DOMAIN        4    182       Formyl_trans_N. {ECO:0000259|Pfam:
FT                                PF00551}.
FT   DOMAIN      206    302       Formyl_trans_C. {ECO:0000259|Pfam:
FT                                PF02911}.
FT   REGION      112    115       Tetrahydrofolate (THF) binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00182}.
SQ   SEQUENCE   311 AA;  33251 MW;  C97614624C62B155 CRC64;
     MSLRIIFMGT PEFSVPTLRL LVDAGHRIVA VYTQPPRPGG RRGLDLQKSP VHQAAELLGL
     PVFTPVNFKD PEERERFRGL NADVGVVVAY GLLLPEAILN GTRDGCYNGH ASLLPRWRGA
     APIQRAIMAG DAKTGMMVMK MDKGLDTGAV ALTREVEIGP NMTAGELHDR LMLVGAKAMA
     EAMVKLEMND LPLTPQPEDG VLYAAKIDKA ETRIDFSRNA GDVHNHIRGL APFPGAWFEL
     EIGGKPERVK VLASELAEGQ GAAGLLLTDD LVIACGSGAL RLTRLQKAGG KPLAAADFLR
     GTPLAAGTRL T
//

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