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B3DRM9 (FMT_BIFLD) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 36. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Methionyl-tRNA formyltransferase

EC=2.1.2.9
Gene names
Name:fmt
Ordered Locus Names:BLD_1966
OrganismBifidobacterium longum (strain DJO10A) [Complete proteome] [HAMAP]
Taxonomic identifier205913 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeBifidobacterialesBifidobacteriaceaeBifidobacterium

Protein attributes

Sequence length328 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 functionMethyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processtranslational initiation

Inferred from electronic annotation. Source: GOC

   Molecular_functionmethionyl-tRNA formyltransferase activity

Inferred from electronic annotation. Source: HAMAP

methyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 328328Methionyl-tRNA formyltransferase HAMAP-Rule MF_00182
PRO_1000098377

Regions

Region110 – 1134Tetrahydrofolate (THF) binding By similarity

Sequences

Sequence LengthMass (Da)Tools
B3DRM9 [UniParc].

Last modified July 22, 2008. Version 1.
Checksum: C82757C165D55361

FASTA32834,765
        10         20         30         40         50         60 
MLKLVFAGTP DVAVPSLKAF AADPRFDVVG VITRPDAPTG RGRKLTPSPV KATALELGLP 

        70         80         90        100        110        120 
VIDLKPRSPE FMEALNNLHA DIAAVIAYGN ILPKNVLDAV PMGWYNLHFS NLPKWRGAAP 

       130        140        150        160        170        180 
AQRAIWAGDP TTGADVFKVG EGLDDGPIVA SLTIELTGRE TSGELLDRLA EEGAPMYVDA 

       190        200        210        220        230        240 
LAAVGEGTAT FTAQPAEGLE YAHKITVEDA RISWTDEAEA IDRQVRACTP HPGAWTELFA 

       250        260        270        280        290        300 
EGPIADNDEP AAKPLTLHIL AAQPADQSNP NTPAELQPGE LKVGKKNVWV GTGSTPLELT 

       310        320 
QVKAQGKKAM RAADWARGAR LSPAACVR 

« Hide

References

[1]"Comparative genomic analysis of the gut bacterium Bifidobacterium longum reveals loci susceptible to deletion during pure culture growth."
Lee J.H., Karamychev V.N., Kozyavkin S.A., Mills D., Pavlov A.R., Pavlova N.V., Polouchine N.N., Richardson P.M., Shakhova V.V., Slesarev A.I., Weimer B., O'Sullivan D.J.
BMC Genomics 9:247-247(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DJO10A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000605 Genomic DNA. Translation: ACD99411.1.
RefSeqYP_001955909.1. NC_010816.1.

3D structure databases

ProteinModelPortalB3DRM9.
ModBaseSearch...

Protein-protein interaction databases

STRING205913.BLD_1966.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACD99411; ACD99411; BLD_1966.
GeneID6363715.
KEGGblj:BLD_1966.
PATRIC21116978. VBIBifLon134794_1985.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0223.
HOGENOMHOG000261177.
KOK00604.
OMAGITLMQM.
ProtClustDBCLSK573224.

Enzyme and pathway databases

BioCycBLON205913:GJB4-2036-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. FMT_C_like. 1 hit.
SSF53328. formyl_transf. 1 hit.
TIGRFAMsTIGR00460. fmt. 1 hit.
PROSITEPS00373. GART. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFMT_BIFLD
AccessionPrimary (citable) accession number: B3DRM9
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: July 22, 2008
Last modified: May 1, 2013
This is version 36 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