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Protein

Peptide deformylase 1

Gene

def1

Organism
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-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 annotation

Cofactori

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi126 – 1261IronUniRule annotation
Metal bindingi168 – 1681IronUniRule annotation
Active sitei169 – 1691UniRule annotation
Metal bindingi172 – 1721IronUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

Iron, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Peptide deformylase 1UniRule annotation (EC:3.5.1.88UniRule annotation)
Short name:
PDF 1UniRule annotation
Alternative name(s):
Polypeptide deformylase 1UniRule annotation
Gene namesi
Name:def1UniRule annotation
Ordered Locus Names:SCO0883
ORF Names:SCM1.16
OrganismiStreptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Taxonomic identifieri100226 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomycesStreptomyces albidoflavus group
ProteomesiUP000001973 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 218218Peptide deformylase 1PRO_0000082852Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi100226.SCO0883.

Structurei

3D structure databases

ProteinModelPortaliQ9RD27.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the polypeptide deformylase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0242.
HOGENOMiHOG000243508.
InParanoidiQ9RD27.
KOiK01462.
OMAiELELVGW.
OrthoDBiEOG664CMF.
PhylomeDBiQ9RD27.

Family and domain databases

Gene3Di3.90.45.10. 1 hit.
HAMAPiMF_00163. Pep_deformylase.
InterProiIPR000181. Fmet_deformylase.
IPR023635. Peptide_deformylase.
[Graphical view]
PANTHERiPTHR10458. PTHR10458. 1 hit.
PfamiPF01327. Pep_deformylase. 1 hit.
[Graphical view]
PIRSFiPIRSF004749. Pep_def. 1 hit.
PRINTSiPR01576. PDEFORMYLASE.
SUPFAMiSSF56420. SSF56420. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9RD27-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGTPSDRVPL AERVEELLAV GGPLPIVAAG DPVLRRAAEP YDGQVAPALF
60 70 80 90 100
ERFVEALRLT MHAAPGVGLA APQVGVGLRV AVIEDPAPVP DEVRVARGRV
110 120 130 140 150
PQPFRVLVNP SYEPAGAGRA AFFEGCLSVP GWQAVVARHA EVRLRAHDEH
160 170 180 190 200
GRAVDEVFAG WPARIVQHET DHLDGTLYLD RAELRSLASN AAMAELWSQP
210
TPRRAASALG FELPGPAA
Length:218
Mass (Da):23,198
Last modified:May 1, 2000 - v1
Checksum:i7F45248A0797288D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL939107 Genomic DNA. Translation: CAB62674.1.
RefSeqiNP_625182.1. NC_003888.3.
WP_011027414.1. NC_003888.3.

Genome annotation databases

EnsemblBacteriaiCAB62674; CAB62674; CAB62674.
GeneIDi1096306.
KEGGisco:SCO0883.
PATRICi23731304. VBIStrCoe124346_0874.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL939107 Genomic DNA. Translation: CAB62674.1.
RefSeqiNP_625182.1. NC_003888.3.
WP_011027414.1. NC_003888.3.

3D structure databases

ProteinModelPortaliQ9RD27.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi100226.SCO0883.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB62674; CAB62674; CAB62674.
GeneIDi1096306.
KEGGisco:SCO0883.
PATRICi23731304. VBIStrCoe124346_0874.

Phylogenomic databases

eggNOGiCOG0242.
HOGENOMiHOG000243508.
InParanoidiQ9RD27.
KOiK01462.
OMAiELELVGW.
OrthoDBiEOG664CMF.
PhylomeDBiQ9RD27.

Family and domain databases

Gene3Di3.90.45.10. 1 hit.
HAMAPiMF_00163. Pep_deformylase.
InterProiIPR000181. Fmet_deformylase.
IPR023635. Peptide_deformylase.
[Graphical view]
PANTHERiPTHR10458. PTHR10458. 1 hit.
PfamiPF01327. Pep_deformylase. 1 hit.
[Graphical view]
PIRSFiPIRSF004749. Pep_def. 1 hit.
PRINTSiPR01576. PDEFORMYLASE.
SUPFAMiSSF56420. SSF56420. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-471 / A3(2) / M145.

Entry informationi

Entry nameiDEF1_STRCO
AccessioniPrimary (citable) accession number: Q9RD27
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: May 1, 2000
Last modified: July 22, 2015
This is version 84 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

External Data

Dasty 3

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 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.