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

def

Organism
Listeria innocua serovar 6a (strain CLIP 11262)
Status
Reviewed-Annotation score: Annotation score: 2 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 bindingi110 – 1101IronUniRule annotation
Metal bindingi153 – 1531IronUniRule annotation
Active sitei154 – 1541UniRule annotation
Metal bindingi157 – 1571IronUniRule annotation

GO - Molecular functioni

  1. iron ion binding Source: InterPro
  2. peptide deformylase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. translation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

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:lin1043
OrganismiListeria innocua serovar 6a (strain CLIP 11262)
Taxonomic identifieri272626 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesListeriaceaeListeria
ProteomesiUP000002513 Componenti: Chromosome

Organism-specific databases

GenoListiLIN1043.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 183183Peptide deformylasePRO_0000082796Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi272626.lin1043.

Structurei

3D structure databases

ProteinModelPortaliQ92CX8.
SMRiQ92CX8. Positions 1-178.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the polypeptide deformylase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0242.
HOGENOMiHOG000243507.
KOiK01462.
OMAiSQDPKIA.
OrthoDBiEOG6PZXGQ.

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.
TIGRFAMsiTIGR00079. pept_deformyl. 1 hit.

Sequencei

Sequence statusi: Complete.

Q92CX8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLTMDDIVRE GHPALREVAT EVTFPLSDEE KKLGHDMLEF LINSQDEELA
60 70 80 90 100
EKYGLRGGVG IAAPQLAVTK RFLAIHVHDE KDRLYSYVLY NPKIRSHSVQ
110 120 130 140 150
QACLSGGEGC LSVDREVPGY VVRSERVTID AFDENGTPLK LRFKGYPAIV
160 170 180
VQHEIDHLNG VMFYDHINKE NPSYLPPDVD VFG
Length:183
Mass (Da):20,610
Last modified:December 1, 2001 - v1
Checksum:i1D7B2637B2B73D59
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL596167 Genomic DNA. Translation: CAC96274.1.
PIRiAB1563.
RefSeqiNP_470380.1. NC_003212.1.

Genome annotation databases

KEGGilin:lin1043.
PATRICi20298805. VBILisInn102668_1070.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL596167 Genomic DNA. Translation: CAC96274.1.
PIRiAB1563.
RefSeqiNP_470380.1. NC_003212.1.

3D structure databases

ProteinModelPortaliQ92CX8.
SMRiQ92CX8. Positions 1-178.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272626.lin1043.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGilin:lin1043.
PATRICi20298805. VBILisInn102668_1070.

Organism-specific databases

GenoListiLIN1043.

Phylogenomic databases

eggNOGiCOG0242.
HOGENOMiHOG000243507.
KOiK01462.
OMAiSQDPKIA.
OrthoDBiEOG6PZXGQ.

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.
TIGRFAMsiTIGR00079. pept_deformyl. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: CLIP 11262.

Entry informationi

Entry nameiDEF_LISIN
AccessioniPrimary (citable) accession number: Q92CX8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: December 1, 2001
Last modified: April 1, 2015
This is version 73 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

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.