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Protein

Methionyl-tRNA formyltransferase

Gene

fmt

Organism
Bifidobacterium longum (strain NCC 2705)
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

Keywordsi

Molecular functionTransferase
Biological processProtein 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:BL1789
OrganismiBifidobacterium longum (strain NCC 2705)
Taxonomic identifieri206672 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaBifidobacterialesBifidobacteriaceaeBifidobacterium
Proteomesi
  • UP000000439 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000829231 – 328Methionyl-tRNA formyltransferaseAdd BLAST328

Interactioni

Protein-protein interaction databases

STRINGi206672.BL1789.

Structurei

3D structure databases

ProteinModelPortaliQ8G3H1.
SMRiQ8G3H1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni110 – 113Tetrahydrofolate (THF) bindingUniRule annotation4

Sequence similaritiesi

Belongs to the Fmt family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CAE. Bacteria.
COG0223. LUCA.
HOGENOMiHOG000261177.
KOiK00604.
OMAiLRIVFMG.
PhylomeDBiQ8G3H1.

Family and domain databases

Gene3Di3.10.25.10. 1 hit.
3.40.50.170. 1 hit.
HAMAPiMF_00182. Formyl_trans. 1 hit.
InterProiView protein in InterPro
IPR005794. Fmt.
IPR005793. Formyl_trans_C.
IPR002376. Formyl_transf_N.
IPR011034. Formyl_transferase_C-like.
PfamiView protein in Pfam
PF02911. Formyl_trans_C. 1 hit.
PF00551. Formyl_trans_N. 1 hit.
SUPFAMiSSF50486. SSF50486. 1 hit.
SSF53328. SSF53328. 1 hit.
TIGRFAMsiTIGR00460. fmt. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8G3H1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLKLVFAGTP DVAVPSLKAF AADPRFDVVG VITRPDAPTG RGRKLTPSPV
60 70 80 90 100
KATALELGLP VIDLKPRSPE FMEALNNLHA DIAAVIAYGN ILPKNVLDAV
110 120 130 140 150
PMGWYNLHFS NLPKWRGAAP AQRAIWAGDP TTGADVFKVG EGLDDGPIVA
160 170 180 190 200
SLTIELTGRE TSGELLDRLA EEGAPMYVDA LAAVGEGTAT FTAQPAEGLE
210 220 230 240 250
YAHKITVEDA RISWTDEAEA IDRQVRACTP HPGAWTELFA EGPIADNDEP
260 270 280 290 300
AAKPLTLHIL AAQPADQSNP NTPAELQPGE LKVGKKNVWV GTGSTPLELT
310 320
QVKAQGKKAM RAADWARGAR LSPAACVR
Length:328
Mass (Da):34,765
Last modified:March 1, 2003 - v1
Checksum:iC82757C165D55361
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014295 Genomic DNA. Translation: AAN25572.1.
RefSeqiNP_696936.1. NC_004307.2.
WP_007053160.1. NC_004307.2.

Genome annotation databases

EnsemblBacteriaiAAN25572; AAN25572; BL1789.
GeneIDi1022106.
KEGGiblo:BL1789.
PATRICifig|206672.9.peg.1842.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014295 Genomic DNA. Translation: AAN25572.1.
RefSeqiNP_696936.1. NC_004307.2.
WP_007053160.1. NC_004307.2.

3D structure databases

ProteinModelPortaliQ8G3H1.
SMRiQ8G3H1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi206672.BL1789.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAN25572; AAN25572; BL1789.
GeneIDi1022106.
KEGGiblo:BL1789.
PATRICifig|206672.9.peg.1842.

Phylogenomic databases

eggNOGiENOG4105CAE. Bacteria.
COG0223. LUCA.
HOGENOMiHOG000261177.
KOiK00604.
OMAiLRIVFMG.
PhylomeDBiQ8G3H1.

Family and domain databases

Gene3Di3.10.25.10. 1 hit.
3.40.50.170. 1 hit.
HAMAPiMF_00182. Formyl_trans. 1 hit.
InterProiView protein in InterPro
IPR005794. Fmt.
IPR005793. Formyl_trans_C.
IPR002376. Formyl_transf_N.
IPR011034. Formyl_transferase_C-like.
PfamiView protein in Pfam
PF02911. Formyl_trans_C. 1 hit.
PF00551. Formyl_trans_N. 1 hit.
SUPFAMiSSF50486. SSF50486. 1 hit.
SSF53328. SSF53328. 1 hit.
TIGRFAMsiTIGR00460. fmt. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiFMT_BIFLO
AccessioniPrimary (citable) accession number: Q8G3H1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 4, 2003
Last sequence update: March 1, 2003
Last modified: June 7, 2017
This is version 82 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference 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.