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Q9ABF5 (DEF_CAUCR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 76. 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

Short name=PDF
EC=3.5.1.88
Alternative name(s):
Polypeptide deformylase
Gene names
Name:def
Ordered Locus Names:CC_0272
OrganismCaulobacter crescentus (strain ATCC 19089 / CB15) [Reference proteome] [HAMAP]
Taxonomic identifier190650 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaCaulobacteralesCaulobacteraceaeCaulobacter

Protein attributes

Sequence length173 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 – 173173Peptide deformylase HAMAP-Rule MF_00163
PRO_0000082759

Sites

Active site1411 By similarity
Metal binding981Iron By similarity
Metal binding1401Iron By similarity
Metal binding1441Iron By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9ABF5 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 7BE0E9341CF9195F

FASTA17319,445
        10         20         30         40         50         60 
MAIRRILTVD NAADLATLKK ISTPVEAVTD ELRALMDDML ETMYDAPGIG LAAVQVGEPV 

        70         80         90        100        110        120 
RVIVMDLARE GEDKAPRYFV NPEILASSED LQGYEEGCLS VPEYYDEVER PSKVTLRYMN 

       130        140        150        160        170 
YQGETVVEEA EGLFAVCIQH EMDHLEGVLF IDHLSRLRRD RAMAKVKKAR RAA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE005673 Genomic DNA. Translation: AAK22259.1.
PIRG87282.
RefSeqNP_419091.1. NC_002696.2.

3D structure databases

ProteinModelPortalQ9ABF5.
SMRQ9ABF5. Positions 18-171.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK22259; AAK22259; CC_0272.
GeneID942379.
KEGGccr:CC_0272.
PATRIC21297462. VBICauCre124313_0269.

Phylogenomic databases

eggNOGCOG0242.
HOGENOMHOG000243509.
KOK01462.
OMADMYDTMD.
OrthoDBEOG664CMF.

Enzyme and pathway databases

BioCycCAULO:CC0272-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 nameDEF_CAUCR
AccessionPrimary (citable) accession number: Q9ABF5
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: June 1, 2001
Last modified: May 14, 2014
This is version 76 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