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Protein

Methionyl-tRNA formyltransferase

Gene

fmt

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

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.

Catalytic activityi

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

GO - Molecular functioni

  • methionyl-tRNA formyltransferase activity Source: EcoCyc

GO - Biological processi

  • charged-tRNA amino acid modification Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Protein biosynthesis

Enzyme and pathway databases

BioCyciEcoCyc:EG11268-MONOMER.
ECOL316407:JW3249-MONOMER.
MetaCyc:EG11268-MONOMER.
BRENDAi2.1.2.9. 2026.

Names & Taxonomyi

Protein namesi
Recommended name:
Methionyl-tRNA formyltransferase (EC:2.1.2.9)
Gene namesi
Name:fmt
Synonyms:yhdD
Ordered Locus Names:b3288, JW3249
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11268. fmt.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved
ChainiPRO_00000829592 – 315Methionyl-tRNA formyltransferaseAdd BLAST314

Proteomic databases

EPDiP23882.
PaxDbiP23882.
PRIDEiP23882.

2D gel databases

SWISS-2DPAGEP23882.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

DIPiDIP-9668N.
IntActiP23882. 12 interactors.
STRINGi511145.b3288.

Structurei

Secondary structure

1315
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 11Combined sources6
Helixi14 – 25Combined sources12
Beta strandi29 – 34Combined sources6
Beta strandi42 – 44Combined sources3
Helixi51 – 58Combined sources8
Beta strandi69 – 71Combined sources3
Helixi72 – 80Combined sources9
Beta strandi84 – 90Combined sources7
Helixi97 – 101Combined sources5
Beta strandi107 – 114Combined sources8
Turni115 – 118Combined sources4
Beta strandi119 – 121Combined sources3
Helixi123 – 130Combined sources8
Beta strandi133 – 141Combined sources9
Beta strandi144 – 147Combined sources4
Beta strandi151 – 158Combined sources8
Helixi165 – 189Combined sources25
Helixi199 – 201Combined sources3
Helixi210 – 213Combined sources4
Helixi221 – 230Combined sources10
Turni231 – 235Combined sources5
Beta strandi237 – 241Combined sources5
Beta strandi244 – 254Combined sources11
Beta strandi264 – 269Combined sources6
Beta strandi272 – 276Combined sources5
Beta strandi278 – 289Combined sources12
Helixi297 – 303Combined sources7
Helixi305 – 307Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FMTX-ray2.00A/B2-315[»]
2FMTX-ray2.80A/B2-315[»]
ProteinModelPortaliP23882.
SMRiP23882.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP23882.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 189N-terminal domainAdd BLAST188
Regioni113 – 116Tetrahydrofolate (THF) binding4
Regioni210 – 315C-terminal domainAdd BLAST106

Domaini

Composed of an N- and a C-terminal domain. The N-terminal domain carries the tetrahydrofolate (THF)-binding site and the C-terminal domain is presumably involved in positioning the Met-tRNA substrate for the formylation reaction.

Sequence similaritiesi

Belongs to the Fmt family.Curated

Phylogenomic databases

eggNOGiENOG4105CAE. Bacteria.
COG0223. LUCA.
HOGENOMiHOG000261177.
InParanoidiP23882.
KOiK00604.
OMAiGCINSHA.
PhylomeDBiP23882.

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P23882-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSESLRIIFA GTPDFAARHL DALLSSGHNV VGVFTQPDRP AGRGKKLMPS
60 70 80 90 100
PVKVLAEEKG LPVFQPVSLR PQENQQLVAE 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):34,168
Last modified:January 23, 2007 - v4
Checksum:i1AE14C808F04A126
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X63666 Genomic DNA. Translation: CAA45207.1.
X77091 Genomic DNA. Translation: CAA54368.1.
U18997 Genomic DNA. Translation: AAA58085.1.
U00096 Genomic DNA. Translation: AAC76313.1.
AP009048 Genomic DNA. Translation: BAE78004.1.
X00767 Genomic DNA. Translation: CAA25339.1. Sequence problems.
Y10307 Genomic DNA. Translation: CAA71358.1.
PIRiS23108.
RefSeqiNP_417746.1. NC_000913.3.
WP_000004473.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76313; AAC76313; b3288.
BAE78004; BAE78004; BAE78004.
GeneIDi947779.
KEGGiecj:JW3249.
eco:b3288.
PATRICi32122008. VBIEscCol129921_3381.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X63666 Genomic DNA. Translation: CAA45207.1.
X77091 Genomic DNA. Translation: CAA54368.1.
U18997 Genomic DNA. Translation: AAA58085.1.
U00096 Genomic DNA. Translation: AAC76313.1.
AP009048 Genomic DNA. Translation: BAE78004.1.
X00767 Genomic DNA. Translation: CAA25339.1. Sequence problems.
Y10307 Genomic DNA. Translation: CAA71358.1.
PIRiS23108.
RefSeqiNP_417746.1. NC_000913.3.
WP_000004473.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FMTX-ray2.00A/B2-315[»]
2FMTX-ray2.80A/B2-315[»]
ProteinModelPortaliP23882.
SMRiP23882.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-9668N.
IntActiP23882. 12 interactors.
STRINGi511145.b3288.

2D gel databases

SWISS-2DPAGEP23882.

Proteomic databases

EPDiP23882.
PaxDbiP23882.
PRIDEiP23882.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76313; AAC76313; b3288.
BAE78004; BAE78004; BAE78004.
GeneIDi947779.
KEGGiecj:JW3249.
eco:b3288.
PATRICi32122008. VBIEscCol129921_3381.

Organism-specific databases

EchoBASEiEB1247.
EcoGeneiEG11268. fmt.

Phylogenomic databases

eggNOGiENOG4105CAE. Bacteria.
COG0223. LUCA.
HOGENOMiHOG000261177.
InParanoidiP23882.
KOiK00604.
OMAiGCINSHA.
PhylomeDBiP23882.

Enzyme and pathway databases

BioCyciEcoCyc:EG11268-MONOMER.
ECOL316407:JW3249-MONOMER.
MetaCyc:EG11268-MONOMER.
BRENDAi2.1.2.9. 2026.

Miscellaneous databases

EvolutionaryTraceiP23882.
PROiP23882.

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_ECOLI
AccessioniPrimary (citable) accession number: P23882
Secondary accession number(s): P77040, Q2M6V2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 153 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.