Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

B7V0Q3 (FMT_PSEA8) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 37. 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:PLES_00171
OrganismPseudomonas aeruginosa (strain LESB58) [Complete proteome] [HAMAP]
Taxonomic identifier557722 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length314 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

methyltransferase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 314314Methionyl-tRNA formyltransferase HAMAP-Rule MF_00182
PRO_1000118485

Regions

Region113 – 1164Tetrahydrofolate (THF) binding By similarity

Sequences

Sequence LengthMass (Da)Tools
B7V0Q3 [UniParc].

Last modified February 10, 2009. Version 1.
Checksum: E5E640CDC94BC269

FASTA31433,055
        10         20         30         40         50         60 
MSQALRIVFA GTPEFAAEHL KALLDTPHRI VAVYTQPDRP AGRGQKLMPS AVKNLALEHG 

        70         80         90        100        110        120 
LPVMQPQSLR NAEAQAELAA LRADLMVVVA YGLILPQAVL DIPRLGCINS HASLLPRWRG 

       130        140        150        160        170        180 
AAPIQRAVEA GDAESGVTVM QMEAGLDTGP MLLKVSTPIS AADTGGSLHD RLAALGPKAV 

       190        200        210        220        230        240 
IEAIAGLAAG TLHGEIQDDA LATYAHKLNK DEARLDWSRP AVELERQVRA FTPWPVCHTS 

       250        260        270        280        290        300 
LADAPLKVLG ASLGQGSGAP GTILEASRDG LLVACGEGAL RLTRLQLPGG KPLAFADLYN 

       310 
SRREQFAAGQ VLGQ 

« Hide

References

[1]"Newly introduced genomic prophage islands are critical determinants of in vivo competitiveness in the Liverpool epidemic strain of Pseudomonas aeruginosa."
Winstanley C., Langille M.G.I., Fothergill J.L., Kukavica-Ibrulj I., Paradis-Bleau C., Sanschagrin F., Thomson N.R., Winsor G.L., Quail M.A., Lennard N., Bignell A., Clarke L., Seeger K., Saunders D., Harris D., Parkhill J., Hancock R.E.W., Brinkman F.S.L., Levesque R.C.
Genome Res. 19:12-23(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LESB58.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FM209186 Genomic DNA. Translation: CAW24745.1.
RefSeqYP_002437628.1. NC_011770.1.

3D structure databases

ProteinModelPortalB7V0Q3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING557722.PLES_00171.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAW24745; CAW24745; PLES_00171.
GeneID7175163.
KEGGpag:PLES_00171.
PATRIC19809486. VBIPseAer113719_0017.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0223.
HOGENOMHOG000261177.
KOK00604.
OMAKVWKAEV.
OrthoDBEOG6B09WV.
ProtClustDBPRK00005.

Enzyme and pathway databases

BioCycPAER557722:GHJW-18-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.
IPR001555. GART_AS.
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.
PROSITEPS00373. GART. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFMT_PSEA8
AccessionPrimary (citable) accession number: B7V0Q3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: February 10, 2009
Last modified: April 16, 2014
This is version 37 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