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Protein

Methionyl-tRNA formyltransferase

Gene

fmt

Organism
Burkholderia cenocepacia (strain MC0-3)
Status
Reviewed-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 annotation

Catalytic activityi

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

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Protein biosynthesis

Names & Taxonomyi

Protein namesi
Recommended name:
Methionyl-tRNA formyltransferaseUniRule annotation (EC:2.1.2.9UniRule annotation)
Gene namesi
Name:fmtUniRule annotation
Ordered Locus Names:Bcenmc03_3142
OrganismiBurkholderia cenocepacia (strain MC0-3)
Taxonomic identifieri406425 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex
Proteomesi
  • UP000002169 Componenti: Chromosome 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000983841 – 330Methionyl-tRNA formyltransferaseAdd BLAST330

Structurei

3D structure databases

ProteinModelPortaliB1K0J5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni121 – 124Tetrahydrofolate (THF) bindingUniRule annotation4

Sequence similaritiesi

Belongs to the Fmt family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000261177.
KOiK00604.
OMAiGCINSHA.
OrthoDBiPOG091H01YM.

Family and domain databases

Gene3Di3.10.25.10. 1 hit.
3.40.50.170. 1 hit.
HAMAPiMF_00182. Formyl_trans. 1 hit.
InterProiIPR005794. Fmt.
IPR005793. Formyl_trans_C.
IPR002376. Formyl_transf_N.
IPR011034. Formyl_transferase_C-like.
IPR001555. GART_AS.
[Graphical view]
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.

B1K0J5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTHTLRVIFA GTPEFAAAAL AAIHKAGFPV PLVLTQPDRP AGRGMKLQAS
60 70 80 90 100
AVKRYAVEHG MAVAQPPSLR RAGKYPAEAA DAIELLRTTP HDVMVVAAYG
110 120 130 140 150
LLLPQEVLDI PRAGCINIHA SLLPRWRGAA PIHRAIEAGD AETGVTLMQM
160 170 180 190 200
DVGLDTGAMI EEARIAIAPD DTTATLHDRL AAAGARLIVD ALVRLERDGT
210 220 230 240 250
LPATPQPADG VTYAEKIGKH EAALDWRKPA DVLARQVRAF DPFPGGVATL
260 270 280 290 300
DGAAIKLWAA EPVAAHGTIA TAAPGTIVEA APEGVVVACG SGALRVTQLQ
310 320 330
KPGGKRLPAR EFLAGSPLAA GQRFALPDVD
Length:330
Mass (Da):34,405
Last modified:April 29, 2008 - v1
Checksum:iC12C58BD62CD8345
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000958 Genomic DNA. Translation: ACA92300.1.
RefSeqiWP_012329437.1. NC_010508.1.

Genome annotation databases

EnsemblBacteriaiACA92300; ACA92300; Bcenmc03_3142.
KEGGibcm:Bcenmc03_3142.
PATRICi19093578. VBIBurCen61509_3268.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000958 Genomic DNA. Translation: ACA92300.1.
RefSeqiWP_012329437.1. NC_010508.1.

3D structure databases

ProteinModelPortaliB1K0J5.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACA92300; ACA92300; Bcenmc03_3142.
KEGGibcm:Bcenmc03_3142.
PATRICi19093578. VBIBurCen61509_3268.

Phylogenomic databases

HOGENOMiHOG000261177.
KOiK00604.
OMAiGCINSHA.
OrthoDBiPOG091H01YM.

Family and domain databases

Gene3Di3.10.25.10. 1 hit.
3.40.50.170. 1 hit.
HAMAPiMF_00182. Formyl_trans. 1 hit.
InterProiIPR005794. Fmt.
IPR005793. Formyl_trans_C.
IPR002376. Formyl_transf_N.
IPR011034. Formyl_transferase_C-like.
IPR001555. GART_AS.
[Graphical view]
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...

Entry informationi

Entry nameiFMT_BURCC
AccessioniPrimary (citable) accession number: B1K0J5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: April 29, 2008
Last modified: November 2, 2016
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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 one 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.