Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Peptide deformylase

Gene

defB

Organism
Streptococcus thermophilus JIM 8232
Status
Unreviewed-Annotation score: -Protein inferred from homologyi

Functioni

Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.UniRule annotation

Catalytic activityi

Formyl-L-methionyl peptide + H2O = formate + methionyl peptide.UniRule annotationSAAS annotation

Cofactori

Fe2+UniRule annotationNote: Binds 1 Fe2+ ion.UniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi131IronUniRule annotation1
Metal bindingi174IronUniRule annotation1
Active sitei175UniRule annotation1
Metal bindingi178IronUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolaseUniRule annotationSAAS annotation
Biological processProtein biosynthesisUniRule annotationSAAS annotation
LigandIronUniRule annotation, Metal-bindingUniRule annotationSAAS annotation

Names & Taxonomyi

Protein namesi
Recommended name:
Peptide deformylaseUniRule annotationSAAS annotation (EC:3.5.1.88UniRule annotationSAAS annotation)
Short name:
PDFUniRule annotation
Alternative name(s):
Polypeptide deformylaseUniRule annotation
Gene namesi
Name:defBImported
Synonyms:defUniRule annotation
ORF Names:STH8232_0240Imported
OrganismiStreptococcus thermophilus JIM 8232Imported
Taxonomic identifieri1051074 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus
Proteomesi
  • UP000000300 Componenti: Chromosome

Structurei

3D structure databases

ProteinModelPortaliF8LUQ4
SMRiF8LUQ4
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the polypeptide deformylase family.UniRule annotationSAAS annotation

Phylogenomic databases

KOiK01462

Family and domain databases

CDDicd00487 Pep_deformylase, 1 hit
Gene3Di3.90.45.10, 1 hit
HAMAPiMF_00163 Pep_deformylase, 1 hit
InterProiView protein in InterPro
IPR023635 Peptide_deformylase
IPR036821 Peptide_deformylase_sf
PANTHERiPTHR10458 PTHR10458, 1 hit
PfamiView protein in Pfam
PF01327 Pep_deformylase, 1 hit
PIRSFiPIRSF004749 Pep_def, 1 hit
PRINTSiPR01576 PDEFORMYLASE
SUPFAMiSSF56420 SSF56420, 1 hit
TIGRFAMsiTIGR00079 pept_deformyl, 1 hit

Sequencei

Sequence statusi: Complete.

F8LUQ4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDAQTKIIRA SHMIDMNDII REGNPTLRAV AEDVTLPLSD EDIILGEKMM
60 70 80 90 100
QFLRNSQDPV IAEKMGLRGG VGLAAPQLDI SKRIIAVLVP NPEDAKGNPP
110 120 130 140 150
KEAYSLQEIM YNPKVVAHSV QEAALGNGEG CLSVDRDVPG YVVRHARVTI
160 170 180 190 200
EYFNKEGEKK RIKLRGYDSI VVQHEIDHTN GIMFYDRINK DNPFTIKDGL

LIIE
Length:204
Mass (Da):22,777
Last modified:September 21, 2011 - v1
Checksum:i0E3CA97B1C7E7ADA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FR875178 Genomic DNA Translation: CCC18991.1
RefSeqiWP_011225356.1, NC_017581.1

Genome annotation databases

EnsemblBacteriaiCCC18991; CCC18991; STH8232_0240
GeneIDi31939607
KEGGistu:STH8232_0240
PATRICifig|1051074.3.peg.170

Similar proteinsi

Entry informationi

Entry nameiF8LUQ4_STRTR
AccessioniPrimary (citable) accession number: F8LUQ4
Entry historyiIntegrated into UniProtKB/TrEMBL: September 21, 2011
Last sequence update: September 21, 2011
Last modified: October 25, 2017
This is version 45 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health