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A0L3X7 (FMT_MAGSM) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Methionyl-tRNA formyltransferase

EC=2.1.2.9
Gene names
Name:fmt
Ordered Locus Names:Mmc1_0143
OrganismMagnetococcus sp. (strain MC-1) [Complete proteome] [HAMAP]
Taxonomic identifier156889 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaMagnetococcalesMagnetococcaceaeMagnetococcus

Protein attributes

Sequence length312 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Modifies the free amino group of the aminoacyl moiety of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by: (I) promoting its recognition by IF2 and (II) impairing its binding to EFTu-GTP By similarity. HAMAP-Rule MF_00182

Catalytic activity

10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) = tetrahydrofolate + N-formylmethionyl-tRNA(fMet). HAMAP-Rule MF_00182

Sequence similarities

Belongs to the Fmt family.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Molecular functionTransferase
   Technical termComplete proteome
Gene Ontology (GO)
   Molecular_functionmethionyl-tRNA formyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 312312Methionyl-tRNA formyltransferase HAMAP-Rule MF_00182
PRO_1000098416

Regions

Region112 – 1154Tetrahydrofolate (THF) binding By similarity

Sequences

Sequence LengthMass (Da)Tools
A0L3X7 [UniParc].

Last modified December 12, 2006. Version 1.
Checksum: 65CF1B00BBCB1028

FASTA31233,499
        10         20         30         40         50         60 
MTAWRVVFMG TPDFATGTLQ ALLDGPDTVV AVFTQPDKPV GRGMKMQKTP VKQLAEQHGI 

        70         80         90        100        110        120 
PVYQPNRLRE AEAVTALRAL RPDVVVVVAY GQILSREVLE IPTHGCINVH ASLLPRWRGA 

       130        140        150        160        170        180 
APIQRAILAG DAQSGVTIMA MEEGLDTGPM YSTVVQSIDN HTTGGQLHDQ LMAAGGGLLV 

       190        200        210        220        230        240 
ETLARIKHEG LTPQIQPEQG VTYAAKLKKE EGLVDWSQPA IQIQRAVQAF DPWPCAFTLW 

       250        260        270        280        290        300 
QGKPLKLFAA SVVVGHGTPG EVIEVEKDGF VVACGDGALR VAQVQAAGKK RMSSGEWLRG 

       310 
HGVKQGERLG EG 

« Hide

References

[1]"Complete sequence of Magnetococcus sp. MC-1."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Kiss H., Goodwin L.A., Brettin T., Bruce D., Han C., Tapia R., Gilna P. expand/collapse author list , Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.
Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MC-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000471 Genomic DNA. Translation: ABK42670.1.
RefSeqYP_864076.1. NC_008576.1.

3D structure databases

ProteinModelPortalA0L3X7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING156889.Mmc1_0143.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABK42670; ABK42670; Mmc1_0143.
GeneID4480997.
KEGGmgm:Mmc1_0143.
PATRIC22426740. VBIMagSp23654_0141.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0223.
HOGENOMHOG000261177.
KOK00604.
OMAVRGMNPF.
OrthoDBEOG6B09WV.

Enzyme and pathway databases

BioCycMSP156889:GH36-144-MONOMER.

Family and domain databases

Gene3D3.10.25.10. 1 hit.
3.40.50.170. 1 hit.
HAMAPMF_00182. Formyl_trans.
InterProIPR005794. Fmt.
IPR005793. Formyl_trans_C.
IPR002376. Formyl_transf_N.
IPR011034. Formyl_transferase_C-like.
IPR015518. Met_tRNA_Form_TA-like.
[Graphical view]
PANTHERPTHR11138. PTHR11138. 1 hit.
PfamPF02911. Formyl_trans_C. 1 hit.
PF00551. Formyl_trans_N. 1 hit.
[Graphical view]
SUPFAMSSF50486. SSF50486. 1 hit.
SSF53328. SSF53328. 1 hit.
TIGRFAMsTIGR00460. fmt. 1 hit.
ProtoNetSearch...

Entry information

Entry nameFMT_MAGSM
AccessionPrimary (citable) accession number: A0L3X7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: December 12, 2006
Last modified: April 16, 2014
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families