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Protein

Methionyl-tRNA formyltransferase

Gene

fmt

Organism
Prosthecochloris aestuarii (strain DSM 271 / SK 413)
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:Paes_1570
OrganismiProsthecochloris aestuarii (strain DSM 271 / SK 413)
Taxonomic identifieri290512 [NCBI]
Taxonomic lineageiBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeProsthecochloris
Proteomesi
  • UP000002725 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000984271 – 317Methionyl-tRNA formyltransferaseAdd BLAST317

Interactioni

Protein-protein interaction databases

STRINGi290512.Paes_1570.

Structurei

3D structure databases

ProteinModelPortaliB4S9B8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni111 – 114Tetrahydrofolate (THF) bindingUniRule annotation4

Sequence similaritiesi

Belongs to the Fmt family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CAE. Bacteria.
COG0223. LUCA.
HOGENOMiHOG000261177.
KOiK00604.
OMAiQRDKPFG.
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.
[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.

Sequencei

Sequence statusi: Complete.

B4S9B8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRIIFMGTPD FAVPSLKAIA AMDGDFEVQL VVTGKDKPRR SKRSEPEPTP
60 70 80 90 100
VKKAARELGI PVMEVDDVKD ERFVDTVARY RPDVLVVAAF RILPPAVYEQ
110 120 130 140 150
ARLGAFNLHA SILPRYRGAA PVNWAIINGE RESGVTTFFL RKSVDTGNMI
160 170 180 190 200
LQEKTPVYPE ENAGELAARL AEIGAGAVVK TLELIRDGRV EPLLQNDTLA
210 220 230 240 250
TRAPKLSTEN TRIDWVQPVD ALCDFIRGLA PRPAAWAIFN HKKVKIFKAS
260 270 280 290 300
VADFHQPEAE EQSAIPGRIA VENNRLFVMG LDGWIEILSL QMEGKKVMQS
310
HEFCCGFRCD EECPVFS
Length:317
Mass (Da):35,272
Last modified:September 23, 2008 - v1
Checksum:i3D980A8546B82421
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001108 Genomic DNA. Translation: ACF46588.1.
RefSeqiWP_012506121.1. NC_011059.1.

Genome annotation databases

EnsemblBacteriaiACF46588; ACF46588; Paes_1570.
KEGGipaa:Paes_1570.
PATRICi23043004. VBIProAes37017_1670.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001108 Genomic DNA. Translation: ACF46588.1.
RefSeqiWP_012506121.1. NC_011059.1.

3D structure databases

ProteinModelPortaliB4S9B8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi290512.Paes_1570.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACF46588; ACF46588; Paes_1570.
KEGGipaa:Paes_1570.
PATRICi23043004. VBIProAes37017_1670.

Phylogenomic databases

eggNOGiENOG4105CAE. Bacteria.
COG0223. LUCA.
HOGENOMiHOG000261177.
KOiK00604.
OMAiQRDKPFG.
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.
[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.
ProtoNetiSearch...

Entry informationi

Entry nameiFMT_PROA2
AccessioniPrimary (citable) accession number: B4S9B8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: September 23, 2008
Last modified: November 2, 2016
This is version 52 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, 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.