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Q8PCN7 (DEF1_XANCP) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peptide deformylase 1

Short name=PDF 1
EC=3.5.1.88
Alternative name(s):
Polypeptide deformylase 1
Gene names
Name:def1
Ordered Locus Names:XCC0687
OrganismXanthomonas campestris pv. campestris (strain ATCC 33913 / NCPPB 528 / LMG 568) [Reference proteome] [HAMAP]
Taxonomic identifier190485 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas

Protein attributes

Sequence length171 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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 By similarity. HAMAP-Rule MF_00163

Catalytic activity

Formyl-L-methionyl peptide + H2O = formate + methionyl peptide. HAMAP-Rule MF_00163

Cofactor

Binds 1 Fe2+ ion By similarity. HAMAP-Rule MF_00163

Sequence similarities

Belongs to the polypeptide deformylase family.

Ontologies

Keywords
   Biological processProtein biosynthesis
   LigandIron
Metal-binding
   Molecular functionHydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processtranslation

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Molecular_functioniron ion binding

Inferred from electronic annotation. Source: InterPro

peptide deformylase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 171171Peptide deformylase 1 HAMAP-Rule MF_00163
PRO_0000082885

Sites

Active site1421 By similarity
Metal binding991Iron By similarity
Metal binding1411Iron By similarity
Metal binding1451Iron By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8PCN7 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 92C65439C03E1F1E

FASTA17119,106
        10         20         30         40         50         60 
MIREIIRMGD KRLLRVAPPV TNLGSDELHA LVADMFETMD AARGVGLAAP QIAVDLQLMV 

        70         80         90        100        110        120 
FGFEASERYP EAPAVPRTAL ANVQIEPLSD EMENGWEGCL SIPGLRAVIP RHRVIRYSGF 

       130        140        150        160        170 
APDGTPIERE AEGFHARVVQ HEYDHLVGRL YPSRIENFDT FGFEDVLSYD L 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE008922 Genomic DNA. Translation: AAM40003.1.
RefSeqNP_636079.1. NC_003902.1.

3D structure databases

ProteinModelPortalQ8PCN7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING190485.XCC0687.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM40003; AAM40003; XCC0687.
GeneID1001340.
KEGGxcc:XCC0687.
PATRIC24072034. VBIXanCam115730_0752.

Phylogenomic databases

eggNOGCOG0242.
HOGENOMHOG000243508.
KOK01462.
OMARVCQVGD.
OrthoDBEOG664CMF.
ProtClustDBPRK12846.

Enzyme and pathway databases

BioCycXCAM190485:GIXZ-686-MONOMER.

Family and domain databases

Gene3D3.90.45.10. 1 hit.
HAMAPMF_00163. Pep_deformylase.
InterProIPR000181. Fmet_deformylase.
IPR023635. Peptide_deformylase.
[Graphical view]
PANTHERPTHR10458. PTHR10458. 1 hit.
PfamPF01327. Pep_deformylase. 1 hit.
[Graphical view]
PIRSFPIRSF004749. Pep_def. 1 hit.
PRINTSPR01576. PDEFORMYLASE.
SUPFAMSSF56420. SSF56420. 1 hit.
TIGRFAMsTIGR00079. pept_deformyl. 1 hit.
ProtoNetSearch...

Entry information

Entry nameDEF1_XANCP
AccessionPrimary (citable) accession number: Q8PCN7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 25, 2002
Last sequence update: October 1, 2002
Last modified: February 19, 2014
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families