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A1ALC4 (FMT_PELPD) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 40. 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:Ppro_0513
OrganismPelobacter propionicus (strain DSM 2379) [Complete proteome] [HAMAP]
Taxonomic identifier338966 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfuromonadalesPelobacteraceaePelobacter

Protein attributes

Sequence length319 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 – 319319Methionyl-tRNA formyltransferase HAMAP-Rule MF_00182
PRO_1000020120

Regions

Region112 – 1154Tetrahydrofolate (THF) binding By similarity

Sequences

Sequence LengthMass (Da)Tools
A1ALC4 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: 26D0863B8A86E267

FASTA31934,234
        10         20         30         40         50         60 
MSSRSIVFMG TPEFACPTLQ ALIDRGERLL AVVTQPDRPK GRGHKLMPPP VKELALAHDI 

        70         80         90        100        110        120 
PVLQPHRVRA SAFVESIRQL APELIVVVAF GQILPKALLD IPPLGCVNVH ASLLPRYRGA 

       130        140        150        160        170        180 
APLNWCIING ETETGVTTML MDTGLDTGPM LLKRSTPIDE NEDIVSLHDR MASLGAELLA 

       190        200        210        220        230        240 
ETLDGLREGR IEPQPQNDSL SCYAPLLKKE HGLIDWQRPA RQIHNQVRGL AAWPGAQTLL 

       250        260        270        280        290        300 
NGHALKLFRT RVADGAGAPG TVLCSTGGQL EVACLDGSLL IQELQLAGKK RLDSASFLAG 

       310 
CPIAEGTLLG GAATERPIP 

« Hide

References

[1]"Complete sequence of chromosome of Pelobacter propionicus DSM 2379."
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., Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F. expand/collapse author list , Land M., Hauser L., Kyrpides N., Kim E., Lovley D., Richardson P.
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 2379.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000482 Genomic DNA. Translation: ABK98144.1.
RefSeqYP_900202.1. NC_008609.1.

3D structure databases

ProteinModelPortalA1ALC4.
ModBaseSearch...

Protein-protein interaction databases

STRING338966.Ppro_0513.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABK98144; ABK98144; Ppro_0513.
GeneID4572884.
KEGGppd:Ppro_0513.
PATRIC22894063. VBIPelPro64470_0670.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0223.
HOGENOMHOG000261177.
KOK00604.
OMADWNKSAR.
ProtClustDBCLSK827657.

Enzyme and pathway databases

BioCycPPRO338966:GHL0-580-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_PELPD
AccessionPrimary (citable) accession number: A1ALC4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 23, 2007
Last modified: May 1, 2013
This is version 40 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