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Protein

Methionyl-tRNA formyltransferase

Gene

fmt

Organism
Chloroflexus aurantiacus (strain ATCC 29364 / DSM 637 / Y-400-fl)
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

Enzyme and pathway databases

BioCyciCSP480224:GHIY-38-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Methionyl-tRNA formyltransferaseUniRule annotation (EC:2.1.2.9UniRule annotation)
Gene namesi
Name:fmtUniRule annotation
Ordered Locus Names:Chy400_0038
OrganismiChloroflexus aurantiacus (strain ATCC 29364 / DSM 637 / Y-400-fl)
Taxonomic identifieri480224 [NCBI]
Taxonomic lineageiBacteriaChloroflexiChloroflexiaChloroflexalesChloroflexineaeChloroflexaceaeChloroflexus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 310310Methionyl-tRNA formyltransferasePRO_1000190016Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliB9LFJ4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni109 – 1124Tetrahydrofolate (THF) bindingUniRule annotation

Sequence similaritiesi

Belongs to the Fmt family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000261177.
KOiK00604.
OMAiGCINSHA.
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.
[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.

B9LFJ4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRILFLGSPS FAVHALEALV AAGHEIVGVV TQPDRPAGRD RRLTPPPVKI
60 70 80 90 100
AAMAHNLPVL QPETLRDPTV VETLSALQPE VGVVAAYGEI LRRAVLSIPP
110 120 130 140 150
LGYLNIHPSL LPLYRGPTPV AGAILAGETV TGVTIMLLDP SMDSGPILAQ
160 170 180 190 200
AVVDLPPTAR AGQLTDELFR IGADLLVQVL PRYARGEIEP RPQDHSRATV
210 220 230 240 250
TKMLKKEDGR IDWSLPAIVI ERMTRAYDPW PGAYTFWRGQ PLRIIKAAVA
260 270 280 290 300
SADGTNVPGT VIGRSGSGHP LVQTGSDALE LIEVQPASRR PMSGSAWLAG
310
VHADNIRLGE
Length:310
Mass (Da):33,137
Last modified:March 24, 2009 - v1
Checksum:iC238A6878775B27A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001364 Genomic DNA. Translation: ACM51482.1.
RefSeqiWP_012255944.1. NC_012032.1.

Genome annotation databases

EnsemblBacteriaiACM51482; ACM51482; Chy400_0038.
KEGGichl:Chy400_0038.
PATRICi21419423. VBIChlSp61043_0033.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001364 Genomic DNA. Translation: ACM51482.1.
RefSeqiWP_012255944.1. NC_012032.1.

3D structure databases

ProteinModelPortaliB9LFJ4.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACM51482; ACM51482; Chy400_0038.
KEGGichl:Chy400_0038.
PATRICi21419423. VBIChlSp61043_0033.

Phylogenomic databases

HOGENOMiHOG000261177.
KOiK00604.
OMAiGCINSHA.
OrthoDBiEOG6B09WV.

Enzyme and pathway databases

BioCyciCSP480224:GHIY-38-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.
[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...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 29364 / DSM 637 / Y-400-fl.

Entry informationi

Entry nameiFMT_CHLSY
AccessioniPrimary (citable) accession number: B9LFJ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 24, 2009
Last modified: March 16, 2016
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.