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Protein

Methionyl-tRNA formyltransferase

Gene

fmt

Organism
Dehalococcoides mccartyi (strain ATCC BAA-2100 / JCM 16839 / KCTC 5957 / BAV1)
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

BioCyciDSP216389:GH6D-1436-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:DehaBAV1_1386
OrganismiDehalococcoides mccartyi (strain ATCC BAA-2100 / JCM 16839 / KCTC 5957 / BAV1)
Taxonomic identifieri216389 [NCBI]
Taxonomic lineageiBacteriaChloroflexiDehalococcoidiaDehalococcoidalesDehalococcoidaceaeDehalococcoides

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 315315Methionyl-tRNA formyltransferasePRO_1000077297Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliA5FPB5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni115 – 1184Tetrahydrofolate (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.

A5FPB5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVMNELKIV FMGSPEFALT PLKMLLAEGY DICGVYTQPD RPAGRGRELC
60 70 80 90 100
PPPVKTLALE HGLAVYQPQS LKKPEEQAFL KELKPDVIVV AAYGLILPQA
110 120 130 140 150
VLDIPVYGVL NIHPSLLPRY RGATPVAATL LGGDEWAGVS LMKLEAGLDT
160 170 180 190 200
GPVYSRSMVA IRPEDTTPIL ADKLAFIGGC MLLELLSQIP SLPEPQVQDN
210 220 230 240 250
TQASYFGMVT KEMGLINWQT SAVEIERRVR AFFPWPGVFT TFNQKTLKIL
260 270 280 290 300
EAKPRNLGLG LKPSEVRVYE QSRVMVGSAS GELEIIRLQL EGKAGCSAAD
310
FVRGQRNFDG VNLGV
Length:315
Mass (Da):34,393
Last modified:June 12, 2007 - v1
Checksum:i17BC986E195D752A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000688 Genomic DNA. Translation: ABQ17963.1.
RefSeqiWP_012034267.1. NC_009455.1.

Genome annotation databases

EnsemblBacteriaiABQ17963; ABQ17963; DehaBAV1_1386.
KEGGideb:DehaBAV1_1386.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000688 Genomic DNA. Translation: ABQ17963.1.
RefSeqiWP_012034267.1. NC_009455.1.

3D structure databases

ProteinModelPortaliA5FPB5.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABQ17963; ABQ17963; DehaBAV1_1386.
KEGGideb:DehaBAV1_1386.

Phylogenomic databases

HOGENOMiHOG000261177.
KOiK00604.
OMAiGCINSHA.
OrthoDBiEOG6B09WV.

Enzyme and pathway databases

BioCyciDSP216389:GH6D-1436-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 BAA-2100 / JCM 16839 / KCTC 5957 / BAV1.

Entry informationi

Entry nameiFMT_DEHMB
AccessioniPrimary (citable) accession number: A5FPB5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: June 12, 2007
Last modified: March 16, 2016
This is version 57 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.