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 1

Gene

def1

Organism
Bacillus cereus (strain ATCC 14579 / DSM 31)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

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 bindingi90 – 901IronUniRule annotation
Metal bindingi132 – 1321IronUniRule annotation
Active sitei133 – 1331UniRule annotation
Metal bindingi136 – 1361IronUniRule 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

Enzyme and pathway databases

BioCyciBCER226900:GJEU-3861-MONOMER.

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:BC_3865
OrganismiBacillus cereus (strain ATCC 14579 / DSM 31)
Taxonomic identifieri226900 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
ProteomesiUP000001417 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 156156Peptide deformylase 1PRO_0000082735Add
BLAST

Proteomic databases

PRIDEiQ819U0.

Interactioni

Protein-protein interaction databases

STRINGi226900.BC3865.

Structurei

Secondary structure

1
156
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi12 – 154Combined sources
Helixi26 – 4116Combined sources
Beta strandi45 – 484Combined sources
Helixi49 – 524Combined sources
Beta strandi56 – 627Combined sources
Turni65 – 673Combined sources
Beta strandi69 – 8820Combined sources
Beta strandi98 – 11114Combined sources
Beta strandi117 – 1237Combined sources
Helixi124 – 13714Combined sources
Helixi142 – 1443Combined sources
Beta strandi146 – 1494Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WS0X-ray1.70A1-156[»]
1WS1X-ray2.00A1-156[»]
ProteinModelPortaliQ819U0.
SMRiQ819U0. Positions 1-151.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ819U0.

Family & Domainsi

Sequence similaritiesi

Belongs to the polypeptide deformylase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0242.
KOiK01462.
OMAiIEYYDEN.
OrthoDBiEOG664CMF.

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.

Q819U0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVLEIIKHP NEVLETPCER VINFDKKLVK LLKDMHETML IADGVGLAAP
60 70 80 90 100
QVGVSLQVAV VDVDDDTGKI ELINPSILEK RGEQVGPEGC LSFPGLYGEV
110 120 130 140 150
ERADYIKVRA QNRRGKVFLL EAEGFLARAI QHEIDHLHGV LFTSKVTRYY

EENELE
Length:156
Mass (Da):17,480
Last modified:May 31, 2003 - v1
Checksum:i0B68AB39485C4D8A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016877 Genomic DNA. Translation: AAP10787.1.
RefSeqiNP_833586.1. NC_004722.1.

Genome annotation databases

EnsemblBacteriaiAAP10787; AAP10787; BC_3865.
GeneIDi1206210.
KEGGibce:BC3865.
PATRICi32603761. VBIBacCer54481_3984.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016877 Genomic DNA. Translation: AAP10787.1.
RefSeqiNP_833586.1. NC_004722.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WS0X-ray1.70A1-156[»]
1WS1X-ray2.00A1-156[»]
ProteinModelPortaliQ819U0.
SMRiQ819U0. Positions 1-151.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi226900.BC3865.

Proteomic databases

PRIDEiQ819U0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAP10787; AAP10787; BC_3865.
GeneIDi1206210.
KEGGibce:BC3865.
PATRICi32603761. VBIBacCer54481_3984.

Phylogenomic databases

eggNOGiCOG0242.
KOiK01462.
OMAiIEYYDEN.
OrthoDBiEOG664CMF.

Enzyme and pathway databases

BioCyciBCER226900:GJEU-3861-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ819U0.
PROiQ819U0.

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: ATCC 14579 / DSM 31.

Entry informationi

Entry nameiDEF1_BACCR
AccessioniPrimary (citable) accession number: Q819U0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 14, 2003
Last sequence update: May 31, 2003
Last modified: March 3, 2015
This is version 80 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.