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

Q98D53 (FMT_RHILO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 71. 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:mll4854
OrganismRhizobium loti (strain MAFF303099) (Mesorhizobium loti) [Complete proteome] [HAMAP]
Taxonomic identifier266835 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesPhyllobacteriaceaeMesorhizobium

Protein attributes

Sequence length317 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 – 317317Methionyl-tRNA formyltransferase HAMAP-Rule MF_00182
PRO_0000083021

Regions

Region112 – 1154Tetrahydrofolate (THF) binding By similarity

Sequences

Sequence LengthMass (Da)Tools
Q98D53 [UniParc].

Last modified October 1, 2001. Version 1.
Checksum: 47A099815954E92C

FASTA31733,903
        10         20         30         40         50         60 
MPLRVIFMGT PEFSVPTLRA IAKAGHEISA VYTQPPRAAG RRGLELTPSP VQREAERLGI 

        70         80         90        100        110        120 
EVRTPTSLKG EAEQAAFNAL RADIAVVVAY GLLLPKVILD APRLGCINGH ASLLPRWRGA 

       130        140        150        160        170        180 
APIQRAIMAG DLESGMMVMR MEEGLDTGPV GLLEKCAIDP DMTAGDLHDR LMRVGAALMV 

       190        200        210        220        230        240 
EALARLAKNT LTFTAQAAEG VTYARKIDKS ETRVDWTRPA AEVHNHLRGL SPFPGAWSEI 

       250        260        270        280        290        300 
DIGGRMERLK LLRSTLSDGL SPSEDLGESG GILDDRLTVA CGAGAIRLVE VQRAGGKPAA 

       310 
ASEFLRGAKI VKGMKFS 

« Hide

References

[1]"Complete genome structure of the nitrogen-fixing symbiotic bacterium Mesorhizobium loti."
Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S., Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y., Nakayama S. expand/collapse author list , Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M., Tabata S.
DNA Res. 7:331-338(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MAFF303099.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000012 Genomic DNA. Translation: BAB51418.1.
RefSeqNP_105632.1. NC_002678.2.

3D structure databases

ProteinModelPortalQ98D53.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING266835.mll4854.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB51418; BAB51418; BAB51418.
GeneID1228293.
KEGGmlo:mll4854.
PATRIC22481904. VBIMesLot2464_3835.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycMLOT266835:GJ9L-3779-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_RHILO
AccessionPrimary (citable) accession number: Q98D53
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2002
Last sequence update: October 1, 2001
Last modified: April 16, 2014
This is version 71 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