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Protein

Methionyl-tRNA formyltransferase

Gene

fmt

Organism
Escherichia coli O103:H2 (strain 12009 / EHEC)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

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.UniRule annotationSAAS annotation

Catalytic activityi

10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) = tetrahydrofolate + N-formylmethionyl-tRNA(fMet).UniRule annotationSAAS annotation

GO - Molecular functioni

  1. methionyl-tRNA formyltransferase activity Source: UniProtKB-HAMAP
  2. methyltransferase activity Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

TransferaseUniRule annotationSAAS annotation

Keywords - Biological processi

Protein biosynthesisUniRule annotationSAAS annotation

Enzyme and pathway databases

BioCyciECOL585395:GJA9-4164-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Methionyl-tRNA formyltransferaseUniRule annotationSAAS annotation (EC:2.1.2.9UniRule annotationSAAS annotation)
Gene namesi
Name:fmtUniRule annotationImported
Ordered Locus Names:ECO103_4019Imported
OrganismiEscherichia coli O103:H2 (strain 12009 / EHEC)Imported
Taxonomic identifieri585395 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000959: Chromosome

Interactioni

Protein-protein interaction databases

STRINGi585395.ECO103_4019.

Structurei

3D structure databases

ProteinModelPortaliC8TXR7.
SMRiC8TXR7. Positions 2-315.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni113 – 1164Tetrahydrofolate (THF) bindingUniRule annotation

Sequence similaritiesi

Belongs to the Fmt family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0223.
HOGENOMiHOG000261177.
KOiK00604.
OMAiKVWQSRV.
OrthoDBiEOG6B09WV.

Family and domain databases

Gene3Di3.10.25.10. 1 hit.
3.40.50.170. 1 hit.
HAMAPiMF_00182. Formyl_trans.
InterProiIPR005794. 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]
PANTHERiPTHR11138. PTHR11138. 1 hit.
PfamiPF02911. Formyl_trans_C. 1 hit.
PF00551. Formyl_trans_N. 1 hit.
[Graphical view]
SUPFAMiSSF50486. SSF50486. 1 hit.
SSF53328. SSF53328. 1 hit.
TIGRFAMsiTIGR00460. fmt. 1 hit.
PROSITEiPS00373. GART. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

C8TXR7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSESLRIIFA GTPDFAARHL DALLSSGHNV VGVFTQPDRP AGRGKKLMPS
60 70 80 90 100
PVKVLAEEKG LPVFQPVSLR PQENQQLVAD LQADVMVVVA YGLILPKAVL
110 120 130 140 150
EMPRLGCINV HGSLLPRWRG AAPIQRSLWA GDAETGVTIM QMDVGLDTGD
160 170 180 190 200
MLYKLSCPIT AEDTSGTLYD KLAELGPQGL ITTLKQLADG TAKPEVQDET
210 220 230 240 250
LVTYAEKLSK EEARIDWSLS AAQLERCIRA FNPWPMSWLE IEGQPVKVWK
260 270 280 290 300
ASVIDTATNA APGTILEANK QGIQVATGDG ILNLLSLQPA GKKAMSAQDL
310
LNSRREWFVP GNRLV
Length:315
Mass (Da):34,154
Last modified:November 3, 2009 - v1
Checksum:i318CFA5BB2A77B1B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP010958 Genomic DNA. Translation: BAI32729.1.
RefSeqiYP_003223863.1. NC_013353.1.

Genome annotation databases

EnsemblBacteriaiBAI32729; BAI32729; ECO103_4019.
GeneIDi8475055.
KEGGieoh:ECO103_4019.
PATRICi32100113. VBIEscCol146794_4204.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP010958 Genomic DNA. Translation: BAI32729.1.
RefSeqiYP_003223863.1. NC_013353.1.

3D structure databases

ProteinModelPortaliC8TXR7.
SMRiC8TXR7. Positions 2-315.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi585395.ECO103_4019.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAI32729; BAI32729; ECO103_4019.
GeneIDi8475055.
KEGGieoh:ECO103_4019.
PATRICi32100113. VBIEscCol146794_4204.

Phylogenomic databases

eggNOGiCOG0223.
HOGENOMiHOG000261177.
KOiK00604.
OMAiKVWQSRV.
OrthoDBiEOG6B09WV.

Enzyme and pathway databases

BioCyciECOL585395:GJA9-4164-MONOMER.

Family and domain databases

Gene3Di3.10.25.10. 1 hit.
3.40.50.170. 1 hit.
HAMAPiMF_00182. Formyl_trans.
InterProiIPR005794. 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]
PANTHERiPTHR11138. PTHR11138. 1 hit.
PfamiPF02911. Formyl_trans_C. 1 hit.
PF00551. Formyl_trans_N. 1 hit.
[Graphical view]
SUPFAMiSSF50486. SSF50486. 1 hit.
SSF53328. SSF53328. 1 hit.
TIGRFAMsiTIGR00460. fmt. 1 hit.
PROSITEiPS00373. GART. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Comparative genomics reveal the mechanism of the parallel evolution of O157 and non-O157 enterohemorrhagic Escherichia coli."
    Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K., Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M., Hayashi T.
    Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 12009 / EHECImported.

Entry informationi

Entry nameiC8TXR7_ECO10
AccessioniPrimary (citable) accession number: C8TXR7
Entry historyi
Integrated into UniProtKB/TrEMBL: November 3, 2009
Last sequence update: November 3, 2009
Last modified: February 4, 2015
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.