def

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 key	Position(s)	DescriptionActions	Length
Metal bindingⁱ	91	IronUniRule annotation	1
Metal bindingⁱ	133	IronUniRule annotation	1
Active siteⁱ	134	UniRule annotation	1
Metal bindingⁱ	137	IronUniRule annotation	1

GO - Molecular functionⁱ

metal ion binding Source: UniProtKB-KW
peptide deformylase activity Source: UniProtKB-EC

Complete GO annotation...

GO - Biological processⁱ

translation Source: UniProtKB-KW

Complete GO annotation...

Keywordsⁱ

Molecular function	Hydrolase
Biological process	Protein biosynthesis
Ligand	Iron, Metal-binding

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Peptide deformylaseUniRule annotation (EC:3.5.1.88UniRule annotation) Short name: PDFUniRule annotation Alternative name(s): Polypeptide deformylaseUniRule annotation
Gene namesⁱ	Name:defUniRule annotation Ordered Locus Names:STH1343
Organismⁱ	Symbiobacterium thermophilum (strain T / IAM 14863)
Taxonomic identifierⁱ	292459 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Bacteria › Terrabacteria group › Firmicutes › Clostridia › Clostridiales › Symbiobacteriaceae › Symbiobacterium › Symbiobacterium thermophilum
Proteomesⁱ	UP000000417 Componentⁱ: Chromosome

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000301114	1 – 217	Peptide deformylaseAdd BLAST		217

Interactionⁱ

Protein-protein interaction databases

STRINGⁱ	292459.STH1343.

STRINGⁱ

292459.STH1343.

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	Q67PR5.
SMRⁱ	Q67PR5.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Sequence similaritiesⁱ

Belongs to the polypeptide deformylase family.UniRule annotation

Phylogenomic databases

eggNOGⁱ	ENOG4108Z02. Bacteria. COG0242. LUCA.
HOGENOMⁱ	HOG000243508.
KEGG Orthology (KO) More...KOⁱ	K01462.
OMAⁱ	VCIQHEI.
Database of Orthologous Groups More...OrthoDBⁱ	POG091H02B0.

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd00487. Pep_deformylase. 1 hit.
Gene3Dⁱ	3.90.45.10. 1 hit.
HAMAPⁱ	MF_00163. Pep_deformylase. 1 hit.
InterProⁱ	View protein in InterPro IPR023635. Peptide_deformylase.
PANTHERⁱ	PTHR10458. PTHR10458. 1 hit.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF01327. Pep_deformylase. 1 hit.
PIRSFⁱ	PIRSF004749. Pep_def. 1 hit.
PRINTSⁱ	PR01576. PDEFORMYLASE.
SUPFAMⁱ	SSF56420. SSF56420. 1 hit.
TIGRFAMsⁱ	TIGR00079. pept_deformyl. 1 hit.

Sequenceⁱ

Sequence statusⁱ: Complete.

Q67PR5-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MAILEIVKEP AEVLRKKAKP VTKINASIRK LLDDMTETMY AAPGVGLAAP 
        60         70         80         90        100
QVGVSKRLIV VDPQDGSGQL YQLINPEIVK AEGWVKGTEG CLSIPGMVGD 
       110        120        130        140        150
VWRYEKVQVV ALDRTGKKVW IDAEGYLARI FQHEIDHLDG ILYTDKCTNL 
       160        170        180        190        200
RPVSEDGEEE EEAEVAEVMP EPEAEGAGEP SAEGAGQAAA EAGAEEGEQV 
       210 
TTGVSGERRG SAAAKEE

Length:217

Mass (Da):23,242

Last modified:October 11, 2004 - v1

Checksum:ⁱDAA0BEF5C915026C

GO

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AP006840 Genomic DNA. Translation: BAD40328.1.
NCBI Reference Sequences More...RefSeqⁱ	WP_011195474.1. NC_006177.1.

Genome annotation databases

EnsemblBacteriaⁱ	BAD40328; BAD40328; STH1343.
KEGGⁱ	sth:STH1343.

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.

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AP006840 Genomic DNA. Translation: BAD40328.1.
NCBI Reference Sequences More...RefSeqⁱ	WP_011195474.1. NC_006177.1.

3D structure databases

ProteinModelPortalⁱ	Q67PR5.
SMRⁱ	Q67PR5.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

STRINGⁱ	292459.STH1343.

STRINGⁱ

292459.STH1343.

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblBacteriaⁱ	BAD40328; BAD40328; STH1343.
KEGGⁱ	sth:STH1343.

Phylogenomic databases

eggNOGⁱ	ENOG4108Z02. Bacteria. COG0242. LUCA.
HOGENOMⁱ	HOG000243508.
KEGG Orthology (KO) More...KOⁱ	K01462.
OMAⁱ	VCIQHEI.
Database of Orthologous Groups More...OrthoDBⁱ	POG091H02B0.

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd00487. Pep_deformylase. 1 hit.
Gene3Dⁱ	3.90.45.10. 1 hit.
HAMAPⁱ	MF_00163. Pep_deformylase. 1 hit.
InterProⁱ	View protein in InterPro IPR023635. Peptide_deformylase.
PANTHERⁱ	PTHR10458. PTHR10458. 1 hit.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF01327. Pep_deformylase. 1 hit.
PIRSFⁱ	PIRSF004749. Pep_def. 1 hit.
PRINTSⁱ	PR01576. PDEFORMYLASE.
SUPFAMⁱ	SSF56420. SSF56420. 1 hit.
TIGRFAMsⁱ	TIGR00079. pept_deformyl. 1 hit.
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	DEF_SYMTH
Accessionⁱ	Q67PR5Primary (citable) accession number: Q67PR5
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	September 11, 2007
	Last sequence update:	October 11, 2004
	Last modified:	June 7, 2017
	This is version 85 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

UniProtKB - Q67PR5 (DEF_SYMTH)

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Peptide deformylase

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Functionⁱ

Catalytic activityⁱ

Cofactorⁱ

Sites

GO - Molecular functionⁱ

GO - Biological processⁱ

Keywordsⁱ

Names & Taxonomyⁱ

PTM / Processingⁱ

Molecule processing

Interactionⁱ

Protein-protein interaction databases

Structureⁱ

3D structure databases

Family & Domainsⁱ

Sequence similaritiesⁱ

Phylogenomic databases

Family and domain databases

Sequenceⁱ

Sequence databases

Genome annotation databases

Similar proteinsⁱ

Cross-referencesⁱ

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Family and domain databases

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ

Documents

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - Q67PR5 (DEF_SYMTH)

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Peptide deformylase

def

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including length and molecular weight.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Documents

Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

PTM / Processingⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Sequenceⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ